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glnD

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Gluconobacter oxydans (strain 621H)
Length
949 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
105.398 kDa
Sequence
MKETSFWGETPSLSFADDTDKPLSDRTASPPCDPASSLQTALDTAAAQGQTTRENVLSILRRHLGSGNATVRREFEKRRMSGIDAARALARQADDMVCALAELAAQKHESPGETLCLCATGGYGAGLLAPFSDIDILFLIPGDPTPAMTARIEFILYALWDLGLRVGHATRSIAECVRDADSDLTIRTALLDLRFLHGERGLARDLRCALGADLQNDRLCEFVMGKIAEREQRHRRFGDNPYMVEPNIKEGRGGLRDLQTLNWMGRAALGCAVSTPDRSGQPAEAPQTPSFASFGLLTDRESLRARRSWDFLWTVRLHLHYITGRAEERLTFDVQPVIGGRMGYATHGRQRGVERFMRHYFLTARDVMRLTSVLQPVVLMHLQDQTTGEPPKVVPGPEEFQTIAGRICPIEPVTFAAQPREMFRLLDCGRRHDLPLHPIAMQQIIRNERHAVTLRDDPETAKIFLDLLCEPSADETKAVPFWLPILNETGLLGRLLPDWSRVVGQMQFDSYHIYTVDEHIVEAVRMMGQIEAGRMADEIPLAYTLASDLRSRRALYVAVLLHDIGKGRGGDHSEIGADLALTICPQLGLDPEETDTVSWLVLHHLLLSQTAFTRDIDDPRTILDLADTIQSPERLRLLLLLTIADMRAVSPKVWNAWKATLLRELFSRVAEVLEGGLAATERDSRVNHARELARDGLTGILPESSIDRFLDLGYPSYWLGFDTDTQMRHARMVHDSDRYRSPVTVEAYPIPERGVTELTVLCADHPGLFSQIAGALAVSGASIVDARIHTLSDGMALDTFWVQDGEGCSFEEPHQLGRLNHLVEQALSGRLDIRKGIEDASHHSTSRRMRAIHVPPRVVIDNTASDRHTVIEVNGRDRPGLLHDVTSALSSASLQISSAHITTYGMRAVDVFYVRDLLGMKITDPVRLARLRETLLASLTSAPVTTPAS

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Sinorhizobium medicae (strain WSM419)
Length
949 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
106.228 kDa
Sequence
MARHETSFPEILDVAALRARCDFIASAHAEQREPMRRALLAAFKEANIAGRAKARELLAADGAGIKCAERISWLQDQLITLLHDFVLNQVFDAAKAPETSRIAVTAVGGYGRGTLAPGSDIDLLFLLPAKKAVWAEPAIEFMLYILWDLGFKVGHATRTIEDCIRLSRADMTIRTAILECRYVCGSVALASELETRFDHEIVRNTGPEFIAAKLAERDERHRKAGDTRYLVEPNVKEGKGGLRDLHTLFWISKYFYRVKDSADLVKLGVLSRQEYKLFQKAEDFLWAVRCHMHFLTGKAEERLSFDIQREIAEALGYHDHPGLSAVERFMKHYFLVAKDVGDLTRIFCSALEDQQAKDAPGISGVISRFRNRVRKIPGTLDFVDDGGRIALASPDVFKRDPVNLLRMFHIADINGLEFHPAALKQVTRSLSLITPHLRENEEANRLFLSILTSRRNPELILRRMNEAAVLGRFIPEFGKIVSMMQFNMYHHYTVDEHLLRAVDVLSRIERGLEEEAHPLTAMLMPAIEDREALYVAVLLHDIAKGRPEDHSVAGAKVARKLCPRFRLSPKQTETVVWLVEEHLTMSMVAQTRDLNDRKTIVDFAERVQSLERLKMLLILTVCDIRAVGPGVWNGWKGQLLRTLYYETELLLSGGFSELSRKERAKHAADMLEEALADWPKEERQTYVRLHYQPYLLTVALDEQVRHAAFIREADAAGRTLATMVRTHDFHAITEITVLSPDHPRLLTVIAGACAAAGANIVGAQIHTTSDGRALDTILVNREFSVAEDETRRAASIGKLIEDVLSGRKKLPDVIASRTRSKKRSRAFTVTPEVTISNALSNKFTVIEVEGLDRTGLLSEVTAVLSDLSLDIASAHITTFGEKVIDTFYVTDLVGSKITSENRQMNIAARLKAVLAGEVDEARERMPSGIIAPTPVPRASHGSKATKAET

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Sinorhizobium medicae (strain WSM419)
Length
949 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
106.228 kDa
Sequence
MARHETSFPEILDVAALRARCDFIASAHAEQREPMRRALLAAFKEANIAGRAKARELLAADGAGIKCAERISWLQDQLITLLHDFVLNQVFDAAKAPETSRIAVTAVGGYGRGTLAPGSDIDLLFLLPAKKAVWAEPAIEFMLYILWDLGFKVGHATRTIEDCIRLSRADMTIRTAILECRYVCGSVALASELETRFDHEIVRNTGPEFIAAKLAERDERHRKAGDTRYLVEPNVKEGKGGLRDLHTLFWISKYFYRVKDSADLVKLGVLSRQEYKLFQKAEDFLWAVRCHMHFLTGKAEERLSFDIQREIAEALGYHDHPGLSAVERFMKHYFLVAKDVGDLTRIFCSALEDQQAKDAPGISGVISRFRNRVRKIPGTLDFVDDGGRIALASPDVFKRDPVNLLRMFHIADINGLEFHPAALKQVTRSLSLITPHLRENEEANRLFLSILTSRRNPELILRRMNEAAVLGRFIPEFGKIVSMMQFNMYHHYTVDEHLLRAVDVLSRIERGLEEEAHPLTAMLMPAIEDREALYVAVLLHDIAKGRPEDHSVAGAKVARKLCPRFRLSPKQTETVVWLVEEHLTMSMVAQTRDLNDRKTIVDFAERVQSLERLKMLLILTVCDIRAVGPGVWNGWKGQLLRTLYYETELLLSGGFSELSRKERAKHAADMLEEALADWPKEERQTYVRLHYQPYLLTVALDEQVRHAAFIREADAAGRTLATMVRTHDFHAITEITVLSPDHPRLLTVIAGACAAAGANIVGAQIHTTSDGRALDTILVNREFSVAEDETRRAASIGKLIEDVLSGRKKLPDVIASRTRSKKRSRAFTVTPEVTISNALSNKFTVIEVEGLDRTGLLSEVTAVLSDLSLDIASAHITTFGEKVIDTFYVTDLVGSKITSENRQMNIAARLKAVLAGEVDEARERMPSGIIAPTPVPRASHGSKATKAET

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Rhizobium meliloti (strain 1021)
Length
949 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
106.382 kDa
Sequence
MARHETSFPEILDVAALRARCDFIASAHAEQREPMRRALLAAFKEANVAGRAKARELLAADGAGIKCAERISWLQDQLITLLHDFVLNQVFDAAKAPEASRIAVTAVGGYGRGTLAPGSDIDLLFLLPAKKAVWAEPAIEFMLYILWDLGFKVGHATRTIEECIRLSRADMTIRTAILECRYVCGSAALANELETRFDHEIVRNTGPEFIAAKLAERDERHRKAGDTRYLVEPNVKEGKGGLRDLHTLFWISKYFYRVKDSADLVKLGVLSKQEYKLFQKAEDFLWAVRCHMHFLTGKAEERLSFDIQREIAEALGYHDHPGLSAVERFMKHYFLVAKDVGDLTRIFCSALEDQQAKDTPGITGVISRFRNRVRKIAGTLDFVDDGGRIALAGTDVFKRDPVNLMRLFHIADINGLEFHPAALKQVTRSLGLITPHLRENEEANRLFLSILTSRRNPELILRRMNEAGVLGRFIPEFGKIVSMMQFNMYHHYTVDEHLLRSVDVLSRIERGLEEEAHPLTAMLMPGIEDREALYVAVLLHDIAKGRPEDHSVAGAKVARKLCPRFRLTPKQTEMVVWLVEEHLTMSMVAQTRDLNDRKTIVDFAERVQSLERLKMLLILTVCDIRAVGPGVWNGWKGQLLRTLYYETELLLSGGFSELSRKERAKHAAHMLEEALADWPKKERQAYVRLHYQPYLLTVALEEQVRHAGFIREADRAGRTLATMVRTHDFHAITEITVLSPDHPRLLTVIAGACAAAGANIVGAQIHTTSDGRALDTILVNREFSVAEDETRRAASIGKLIEDVLSGRKRLPEVIASRTRVKKRSRAFTVTPEVTISNTLSNKFTVIEVEGLDRTGLLSEVTAVLSDLSLDIASAHITTFGEKVIDTFYVTDLVGSKITSENRQMNIAARLKAVLAGEVDEARERMPSGIIAPTPVSRVPHGSKTTKAET

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Rhizobium tropici
Length
948 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
106.423 kDa
Sequence
METHHIDFSTVLDVSALKAECEALAKRGLDKNEERSALLALLKKASQDGREEARRLLIADGSGLNCAHRISWLQDQIITVLYDLTVHHAYPKQAGVFSVTAVGGYGRDTLAPGSDIDLLFLFQPKPASETHKAVEFILYMLWDMGFKVGHATRSVEECIREAKSDMTVRTAILETRYICGNVALERELQARFDKEIVTNTGPEFIAAKLAERDERHRKAGDTRYLVEPNVKEGKGGLRDLHTLFWISKYYYHVRDPAELVKLGVLSKQEYRLFEKAEDFLWAVRCHMHFLTGKAEERLSFDIQRDIAAALDYNARPGLSAVERFMKHYFLVAKDVGDLTRILCAALEDQQAKATPGLTGVISRFANRSRKIPGTVEFVEDRGRIALANPDVFKRDPVSLIRLFFVADINGLEFHPDALKRVTRSLSLIDNDLRENEEANRLFLSILTSKRDPALILRRMNEAGVLGRFIPEFGKIVSMMQFNMYHHYTVDEHLIRAVEVLSEIDKGRAEDIHPLTNKLMPNIEDRDALYVAVLLHDIAKGREEDHSEAGAAVARKLCPRFGLSPKQTELVVWLIAEHLTMSMVAQTRDLTDRKTIIDFADRVQSLDRLKMLLILTVCDIRAVGPGVWNGWKGQLLRTLYYETELLLSGGFSEVSRKERAEAAAEALEHALADWSQKERKAYVKLHYQPYLLSVPLEDQIRHTQFMRESDKAGKVLATMVRTDSFHAITEITVLSPDHPRLLTVIAGACAAAGANIADAQIFTTSDGRALDTIHVSREFPDDADELRRAATIGKMIEDVLAGRKRLPEVIATRTKNRRKNKAFVIPPSVIITNSLSNKFTVIEVECLDRPGLLSEITAVLSDLSLDIQSARITTFGEKVIDTFYVADLVGQKISNENRRAYITARLKAVMAGEEDEMRERMPSGIIAPAATRGVAVEKSDTEKKAGSAA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Rhizobium leguminosarum bv. viciae
Length
944 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD likely hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism.
Similarity
Belongs to the GlnD family.
Mass
106.218 kDa
Sequence
MRDLDFTNILDVELLQKQCDAVAEANRNRPDVLRADLLAVLKKASTEGRQKAREALMADGGGLNCAYRISWLQDQITTVLYNFATAHIFPQQKDKFAVTAVGGYGRDTLAPGSDIDLLFLFLPRPAEETHKAVEFMLYVLWDMGFKVGHATRTVEECIALSKSDMTIRTAILEMRYICGLQRLETELETRFDKEIVTGTGPEFIAAKLAERDERHRKAGDTRYLVEPNVKEGKGGLRDLHTLFWISKYYYHVRDQAELVKLGVLSKHEYRLLEKADDFLWAVRCHMHFLTGKAEERLSFDIQREIAEAFGYHTRPGLSAVERFMKHYFLVAKDVGDLTRILCAALEDQQAKSIPGLTGVISRFTHRNRKIAGSVEFVEDRGRIALADPEVFKRDPVNIIRLFHVADINGLEFHPDALKRVTRSLALIDNALRENDEANRLFMSILTSKRDPALILRRMNEAGVLGRFIPEFGKIVAMMQFNMYHHYTVDEHLIRTVDILSEIDKGRAEDLHPLANKLMPGIEDREALYVAVLLHDIAKGRQEDHSIAGARVARKLCVRFGLSQKQTEIVVWLIEEHLTMSMVAQTRDLTDRKTITDFADRVQSLDRLKMLLILTICDIRAVGPGVWNGWKGQLLRTLYYETELLLAGGFSEVSRKERANAAAEALHSALADWSQKDRNTYTKLHYQPYLLSVPLEDQIRHAHFIRQADKAGQALATMVRTDSFHAITEITVLSPDHPRLLAVIAGACAAAGANIVDAQIFTTSDGRALDTIHVSREFTDDADELRRAATIGRMIEDVLSGRKRLPEVIATRARNRKKSKAFVIPPSVNITNSLSNKFTVIEVECLDRPGLLSEITAVLSDLSLDIQSARITTFGEKVIDTFYVTDLVGQKISGDSKRANITARMKAVMAEEEDELRERMPSGIIAPAATARTPPASEKKAGSPI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Agrobacterium fabrum (strain C58 / ATCC 33970)
Length
942 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
106.204 kDa
Sequence
MAIKDLDFSDILDVSALKRDCDVIFKEDSKRIADIKSDLLPIFRRASTEGREKARELLKADGSGIDCARRISWLQDRLIETLYDLACQHVYPKDAPQIAVAAVGGYGRGTLAPGSDIDLLFLLPAKNTPDMHKAVEFVLYLLWDLGFKVGHATRTVDECIRLSKSDMTIRTAILEVRAICGRKSLTDDLEKRFESEVVTGTGPEFIAAKLAERDQRHRKAGDTRYLVEPNVKEGKGGLRDLHTLFWIAKYYYHVRDTADLVKLGVLSRSELKLFEKADDFLWAVRCQMHFITGKAEERLSFDIQREIADALNYQPRPGLSAVERFMKHYFLVAKDVGDLTRIVCAALEDRQAKDVPGLSGVLSRFAHRVRKIPGSVEFVEDRGRIALARPDVFKNDPVNLIRLFHIADINNLELHPDALRVVTRSLSLINDELRENEEANRLFLSILTSRRDPALTLRRMNEAGVLGKFIPEFGKIVAMMQFNMYHHYTVDEHLIRSVGVLSEVDKGTAVDAHPLANQLMPGVEEREALYVAVLLHDVAKGRQEDHSIAGARVARKLCQRFRLTGKQTETVVWLIEQHLLMSMVAQTRDLHDRKTITDFADKVQSMERLKMLLILTVCDIRAVGPGVWNGWKGQLLRSLYYETELLLSGGFSEVSRKERAQIARQALYDALEDWGQKARRKYTKLHYEPYLLTVALEDQVRHTRFMREADKQEKALSTMVRTHSFHAITEITVLAPDHPRLLSIITGACAAAGANIADAQIFTTSDGRALDTILINREFPIDEDETRRGANVGKLIEEVLSGKQRLPEMIATRTKSRRKKSAFTIPPSVTISNGLSNKFTVIEVECLDRPGLLADMTAVIADLSLDIHSARITTFGEKVIDTFYVTDLFGQKVTNDNRQASIAQRLKAVMSEQEDELRDRMPNGIIAHPDVAALPAARTAKA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Agrobacterium vitis (strain S4 / ATCC BAA-846)
Length
941 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
105.604 kDa
Sequence
MAKHDLSDATLPDFKALEAECMSIVLQNGKVPETRAAILPLLKKASIDGREAALRHLTTNGSGLECAGMISNLQDNLITLVHRMVTQAVYPTTQQEFAVAAVGGYGRSTLAPGSDIDLLFLLSVKAGADARKAVEFLLYILWDLGFKVGHATRLVEECIRLSRTDMTIRTAILETRFICGEALLVGELQKRFDAEVVEKTAPEFIAAKLAERDERHRKAGDTRYLVEPNVKEGKGGLRDLHTLFWIAKYYYRISDPADLVKLGVLSRQEWRMFQKSDDFLWAVRCHMHFATGKPEERLSFDLQPEIARNLGYNARPGLSEVERFMKHYFHVAKNVGDLTRIVCASLEDKQAKAAPGLTAAIGRFAHRPRRIPGTPEFIEDRGRIALSGPDIFKRDPINIMRFFHVADLHGLEFHPDALKAITRCLPLIDHDFRENEEANRLFLSILTSKRDPALMLTRMNEAGVLGKFIPDFGRIVSMMQFNMYHHYTVDEHLIRSVGILAEVDQGQHADIHPLAVKLMPNIEERTVLFVAVLLHDIAKGRQEDHSIAGAKVARRLCPRLGLNDKQTELVVWLIDQHLLMSMVAQTRDLHDRKTITDFAEKVQSLDRLRMLLVLTVCDIRAVGPGVWNGWKGQLLRTLYYETELLLSGGFSESPRKERAKQAAEQLAEALSDWSQKDQKTYTKLHYQPYLLTVPLEDQVRHAHFIRQADKADQALATMVRTHSFHAITEITVLAPDHPRLLSIIAGACAAAGANIADAQIFTTSDGRALDTILINREFPIDEDEMRRANTISKMIEDVLAGKKRLPEVIATRTKGRKRNKTFTVKPHVTISNSLSNKFTVIEIECLDRIGLLAEVTAVLADLSLDIHSARITTFGEKVIDTFYVIDLVGQKITNENRQGSISVRLKAVMSEQPDELREQMPSGIIAPAATKSPAAEKKARV

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Caulobacter vibrioides (strain ATCC 19089 / CB15)
Length
940 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.396 kDa
Sequence
MPRRLRPTRLEHVVDGHALRARLSAAALDSIGNEAEQRARAIDILKQALFRGRMIAKERLENGASGVETSRLLSGVTDEVITALYDFTTVHVFRARNPTEGERLCLLAVGGYGRGTLAPFSDIDLLFLRPYKQTPHAESVIEYMLYALWDLGFKVGHASRTIEECVRLSKEDFTIRTSILEARRLTGDERLAEDLKKRFRDEVMKATGAQFVAAKLKERDDRQARAGASRYMVEPNVKEGKGGLRDLHTLMWIAEYLHPVDRPEDVFKMEVFSIRETKAFIRAFDFLHAVRAHLHFTTGRPEERLTFDLQPEIARRMGYGDRGDAPAVERFMRRYFLIAKEVGTLTRAFSAKLEAEHFKNEPKGISRFLPGARPKRKALDVEGFYEDGGRLNIEGQEIFEADPVNLIRLFKIADERDLDLHPDAFTAVTRALPLITSRVRRDPDACRAFLDLLARGKRSYRTLTLMNDAGVLGRFIPEFGRVVAQMQFNMYHSYTVDEHTLRAVGVIGDIAAGRLVDDHPLAVSIMPLIEDREALFLAMLLHDTGKGGVGGQEKAGARSARSACERLGVERSKVELVAWLVENHLVMSDFAQKRDVSDPGTVAAFARIVENPERLRLLLVITVADIRAVGPGVWNGWKGQLLRELYNATEAVFRGGRGSDAAANVQRHQESTAEAARAALLETDPAAKGWVAAMENAYFSAFSQDDLFHHAELARRAAIQGGAAAEGQVRPGSNAAEVVIAAKDRRGLFADLALAISSLGGNVVGARVFTSRQGQALDVFYVQDVTGAPFGCENPRALRRLADALEAAGKGDALAVEPRRGSEQTRAAAFAIAPSVTIDNDASNDATVVEASGRDRPGLLHALAKTLADSALSIQSAHIDGYGERAVDAFYVQTTEGGKVTDTRKLNALKADLLAALEQNEASAPAARPGLRRARASVAR

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Caulobacter vibrioides (strain NA1000 / CB15N)
Length
940 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.396 kDa
Sequence
MPRRLRPTRLEHVVDGHALRARLSAAALDSIGNEAEQRARAIDILKQALFRGRMIAKERLENGASGVETSRLLSGVTDEVITALYDFTTVHVFRARNPTEGERLCLLAVGGYGRGTLAPFSDIDLLFLRPYKQTPHAESVIEYMLYALWDLGFKVGHASRTIEECVRLSKEDFTIRTSILEARRLTGDERLAEDLKKRFRDEVMKATGAQFVAAKLKERDDRQARAGASRYMVEPNVKEGKGGLRDLHTLMWIAEYLHPVDRPEDVFKMEVFSIRETKAFIRAFDFLHAVRAHLHFTTGRPEERLTFDLQPEIARRMGYGDRGDAPAVERFMRRYFLIAKEVGTLTRAFSAKLEAEHFKNEPKGISRFLPGARPKRKALDVEGFYEDGGRLNIEGQEIFEADPVNLIRLFKIADERDLDLHPDAFTAVTRALPLITSRVRRDPDACRAFLDLLARGKRSYRTLTLMNDAGVLGRFIPEFGRVVAQMQFNMYHSYTVDEHTLRAVGVIGDIAAGRLVDDHPLAVSIMPLIEDREALFLAMLLHDTGKGGVGGQEKAGARSARSACERLGVERSKVELVAWLVENHLVMSDFAQKRDVSDPGTVAAFARIVENPERLRLLLVITVADIRAVGPGVWNGWKGQLLRELYNATEAVFRGGRGSDAAANVQRHQESTAEAARAALLETDPAAKGWVAAMENAYFSAFSQDDLFHHAELARRAAIQGGAAAEGQVRPGSNAAEVVIAAKDRRGLFADLALAISSLGGNVVGARVFTSRQGQALDVFYVQDVTGAPFGCENPRALRRLADALEAAGKGDALAVEPRRGSEQTRAAAFAIAPSVTIDNDASNDATVVEASGRDRPGLLHALAKTLADSALSIQSAHIDGYGERAVDAFYVQTTEGGKVTDTRKLNALKADLLAALEQNEASAPAARPGLRRARASVAR

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Phenylobacterium zucineum (strain HLK1)
Length
938 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.982 kDa
Sequence
MPPRLRPTHLEYVVDGVKLRSQLSAAALEHAGDELAQRRAALEILKNALFRGRMIAKERLENGAGGIETARLLSGVTDEVVSALYDFTTVHVFRARNPTEGERLALMAVGGYGRGTLAPFSDIDLLFVRPYKQTAHAESVIEYMLYALWDLGFKVGHASRTIDECLKLSREDFTIRTSILEARRLTGDEKLAGELVERFRKEVVKGTGAEFVAAKLKERDERHARAGASRYMVEPNVKEGKGGLRDLNTLFWIAQYLHPGESLEKVMHLEIFDRREVRTFIQALDFLWAVRCHLHFATGRPEERLSFDLQPEIARRMGYGDRGDAPAVERFMRRYFLFAKDVGSLTRVFAAKLEADRVKTAPKGISRFIPGRAQKRKPLDEPGFHEVGGRLGVDPEIFEADPVNLLKLFRIADQRNLDLHPDAFTAASRASGLITSAVRRDRHAAKVFLDILARGRDPQRTLALMNEAGVLGRFVPEFGRIVAQMQFNMYHSYTVDEHTLRAVGVIADIAAGRLAEDHPLAVQTMPLIADREALFLAMLLHDTGKGGAGGQELAGARAARQACERLGLERSKIELVAWLVEHHLVMSDYAQKRDVSDPRTVADFARIVQSPERLRLLLVLTVADIRAVGPGVWNGWKGQLMRELYTATEAVFRGGRGSDAAAALKRYQENAAYDARVSLAKADPLAEPWADAMEDAYFTAFSEAEVLAHARLAQQAGGGAAAEGRIRSELNAAEVVVAAADRPRLFVDLAEAITAAGANVMGARVFTSRAGQALDVFYVQDASGQPFGSHDPRALARLAETLACAARGEPVAREPRKPQDLGRTAAFAITPAVMLDNEASETSTVVEASGRDRPGLLAALARTISDAGLSILSAHIDGYGERAVDAFYVVDADGRKLTDARKRNALKSALLAALTKAEAETAQARRTNLQRARASVAR

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Length
936 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
105.094 kDa
Sequence
MTIPRIRQPRAVIDRKALTVVLEDLAATVTDNRERRARLLAVLKGALGDGRAEVRRRFLEEKGTGAAVFAENSHLMDQIIRLLFDFTTTHVYPRANRTIGEQMTVLAVGGYGRGEMSPQSDVDLLFLLPYKATPLHEQVVEYMLYTLWDMGLKVGHATRSIEECIRQARGDLTIRTAMLETRYLWGDRALYGQLKTKFWTGVVTGTGPDFVEAKLAERDERHLRMGDSRYVLEPNIKDGKGGLRDLHTLLWIARYIYGVSDMRELVELGVLSADAATKFGRARAFLWTVRCHLHYLADRPEERLTFDVQPAIAARMGYTDRNSGRGVERFMKHYFLMAKTVGDLTRIFCAVLEDQQKRRPILSIATLLMRKRNLGDFVLDGGRLAVAGRGAFREHPLQLISLFKVAHDHGLDIHPDTLRLVTEHLPTVTLLRNDAKANALFMEILTSRKDPELALRQLSESGVLARFIPDFGRVTAQMQFDMYHVYTTDEHTIRAIGLLHRLETGALRDRMPAAADAVHKVQSRRALYLAVLLHDIAKGRGGDHSILGAEVAMRLGPRLGMSEEETETVAWLVRHHLDMSRTAFKRDLDDIKTILDFTGLVQSVERLHLLLALTTVDILAVGPAVWNNWKSSLLRELYTHSKDVLTSGFQAEARDKRVAHKREELAAALADWPQASRERYLDLHYPAYWLTFDSATHLRHARMLRRARDAGLTVAVEVLPDPERAVSEVLVATDDHPGLFSKIAGAMALAGVNILDAKITTMSDGGALDIFTVQTLEGHAIEKEERIARLAKTVRDVLTGDLPLEKALRRQPPRLPERTRHLTVPPRVIVDNQASKTHTVIEINGRDRPGFLYAVTRALTDVAVQISSARVSTYGERVVDSFYVKDVFGMKIVHRAKLAQIREALEAAITQTVPRKVEEGAEQGAEKADAGEIVAA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168)
Length
934 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
105.778 kDa
Sequence
MSAHDLKLEEIVNPETLRRKLNELADSTDENYTSPTVRKVVLQALKDALVRGRANAEGMLMKDGGGTLCAKRLSFLMDTLIEALFEFATTKAYPMINPSKAENMAIVAVGGYGRGGLAPGSDIDLLFLLPYKQTPWGEQVVEYMLYMLWDMGLKVGHSTRNIDECIRLSREDMTIRTAILDARFLTGNRELFKTLVTRFDEEIVKDTGPEFIQAKLAERDQRHRKAGETRYLVEPNVKEGKGGQRDLHTLFWITKYFYRVKTKEELVKLGVLSRAELKLFNKAEDFLWAVRCHMHFATLKAEERLSFDIQPEIAQRLGYTAHPGQNYVERFMKHYFLVAKDVGDLTRIISAALEEQQAKHVPGFNRIFLTFSRRKRKLSADGDFVSENHRINIARPEVFKEDPVNIIRLFHLADKHGLEFHPEAMQSLTRSLKLINSDLRENPEANKLFLEILTSPRNPELILRRMNESGVLGKFIPDFGKIVAMMQFNMYHHYTVDEHLLRCIAVLSEIEHGELENEHPLSNHLITTVKRDRNLLYVALLLHDIAKGRPEDHSVAGARIARRLGPRLGLTPTETETVEWLVREHLTMSMVAQSRDLNDRKTIIDFADTVQTMERLKLLLILTVCDIKAVGPGVWNGWKGQLLRTLFYETELVLTGGFSELSRADRDHQAREALADRLSDWPKDKRDAYLALHYTNYFLTVSLEDQVRHAHFIREADRNERALATMAKPHTFEAVTEITVLAPDHPRLLSIITGACAAAGANIVDAQIFTTGDGRALDTILISREFDTDDDERRRAERVGKVIEDVLSGKAHLPDVLAKRTKPKRAAKAFKVEPRVEINNTLSNKFTVIEVEGLDRPGLLSELTGLISDLSLDIASAHITTFGEKVIDSFYVTDLVGHKISNATRQGNIRRKLLGVLSGENGSKTNGRSSQAAA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Azospirillum brasilense
Length
933 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnZ, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
104.602 kDa
Sequence
MLSTRAASADASDAKDAGTANIPNKRAILSRRKLAEDLETLVAEHGTGDKLRPALIARLRGALNDGRAEVRARFEAKGSGEDCVRQNCYLADGVVRSLADLTVTHIFPTPNPTSGEVFDIVATGGYGRGELAPFSDIDLLFLLPYKRTPRVEQVVEYMLYILWDLGLKVGHAVRSVDDCIRQSKADVTIRTAILESRYLWGPRKLFHRLRRRFDREVVAGTGPEFVEAKLAERDNRHLKLGDSAYVLEPNLKDGKGGLRDLQTLFWIAKYLYRVEDVDDLVGKKVLLPEEAHGFAKAQNFLWTARCHLHYLTGRMEDRMTFDVQTSIGNRMGYTDHAGTKGVERFMKHYFLVAKDVGDLTRIFCAALEAESKRPPKFNILRLAALARRKDVDGFVVDGERLNVRSDRQFKDEPLDMIRLFHTAQQNDIDIHPNALRAITRSLSVVGPKLRADPEANRLFLEILTGRKDPEITLRRMNEAGVLARFIPDFGRVVAQMQYDMYHVYTVDEHTLFALGILHKIEMGELTDELPLSSEVIHKVVSRRALYVAVLLHDIAKGRGGDHSILGARVAEKLCPRLGLTAEETETVAWLVRWHLAMSYTAFKRDLEDDKTVRDFVSLVQSPERLRLLLVLTVADIRAVGPQRWNNWKATLLRELYNRSEEVMSGGLSVEGRGRRIQAAQAALRDELSDFDAADFERHLALGYPAYWLAFDAETLGRQARLVRGRLRDERPLTVNTRIDRGRAITEVTIFATDHHGLFSRLAGALAAAGADIVDARIFTMTNGMALDVFTVQDAAGGGAFESGDKLAKLSVMIEKVLSGQLKPLHDLTKRKAPHASRTRVFHVPPRVLIDNNASTTHTVIEVNGRDRPGLLYDLTRALTNLTLQISSAKISTYGEKAIDVFYVKDVFGLKVTHENKLAQIRERLLHALADPSA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Length
933 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
105.28 kDa
Sequence
MAKISLKLDELIDGEALRREMTALTTATAGDGSGAAARAGVLQLLKARLAEGRKIAEAMLKEDGGGNACAERLSHLMDELIRALYDFAATHVYRVKNRSSAERMAVVAVGGYGRGTLAPGSDIDLLFLLPYKQTPWGEQTVEYMLYMLWDLGLKVGHATRNIDECLRLSRTDITIRTSILEARFLWGERKLYDELMLRFDHEVVRTTGPEYVQAKLAERDERHAKAGESRYLVEPNVKDGKGGLRDLQTLFWIGKYFYRVRTGEELVEKGVFTEAEYREFQKAEDFLWAVRCHMHFLTGKAEERLHFDIQREIAERLGYTTHPGLSAVERFMKHYFLVAKDVGDLTRIFCAALEEEQAKHVPGFNRIFLTFQRRKRKLAGTSDFIVDNHRINIADDQVFERDPVNLLRLFWFADKHGLEFHPDALKLLTRSLGLVNKSLRRDEEANRLFLDILTSDRNAELNLRRMNEAGLLGRLIPDFGKIVAMMQFSMYHHYTVDEHLIRCIGVLAEIERGDGEKVHPLSHSLMPGLKKSREALYVAVLLHDIAKGRPEDHSEAGARIARRICPHMGLSAADTETVAWLVENHLAMSMTAQTRDLNDRKTIEDFASIVQSVERLKLLLVLTVCDIRGVGPGVWNGWKGQLLRTLYYETELLLTGGFSEVSRAQRTAAARERLAEALADWPDKDRKRYVGLHYENYLLTVDLPDQLRHAEFVREADAAGKKLATMVKTHQFEAVTEITVLAQDHPRLLSVIAGACVGAGGNIVDAQIFTTADGRALDTILISREFDRDEDERRRAERVGRLIEDVLSGKSWLPEMIEKRTKPKRGAKVFKIPPRAEIRNTLSNRFSVIEVEGLDRPGLLSEITGTLSDLSLDIASAHITTFGEKVIDTFYVTDLTGQKIDSPARIATIRNRLMATLEGIAPERGGKAKAAAE

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182)
Length
931 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
104.895 kDa
Sequence
MDSVTPNSRPESFPEFDSAGLAAAVDALAAQHSGREDMFRAAVVQLLKAELVKARAVAQAQLLKDRHGRRCAERLCFVQDEIIRILYAAATQHLYRSQVPSGAERMAVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYSLWDMGLKVGHATRSVDESIRQARGDMTIRTAILETRYLAGDRPLYDELVERFDTEVVQGTAAEFVAAKLAEREERHRRGGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVRETAELVERGVFDAHEYRTFRRCADFLWSVRCNLHFVSGRPEERLSFDLQREIAVRLGYTSHPGMQDVERFMKHYFLVAKEVGNLTAILCAKLEDQQAKPAPVLSRVISRLKTGNSWRRVPESDDFIVDNNRINLAAPDVFKHDPVNLIRIFRLAQKNNLAFHPDAMRAVTRSLNLINTELRDNPDANRLFMEILTSNDAETVLRRMNETGVLGHFIRAFGRIVSMMQFNMYHHYTVDEHLIRCIGFLQEIERGGIDEFALASDLMRKIRPEHRAVIYISVLLHDVAKGRPEDHSIAGAKVARRLCPRLGFNNADTELVAWLIEEHLTMSTVAQSRDLSDRRTIEKFAAVVQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPVLTGGFSEVNRAKRITAAQAEFRNAFTDWPEDELNTYIGRHYPAYWLKVELPRKIRHARFVRASEDAGHKLAINVGFDPARGVTELTIFAMDHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTIAISREYERDEDEGRRATRIGETIEQVLEGKLRLPDAVARRTTRGKQHKAFSVEPEVSINNQWSELYTVIEVSGLDRPGLLYELTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQINAPTRQAAIKSALLHLLASDDTAAQPAA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Bradyrhizobium sp. (strain ORS 278)
Length
931 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
104.696 kDa
Sequence
MDSVATDSKAFTSADFDSAGIAAAVDALAKQHSGREDMFRAAVVQFLKAELVKARAAAQAQLLQDRHGRHCAERLCVVQDEIIRILYAAATEHLYRSDVPSGAERMAVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYSLWDMGLKVGHATRSVDESIRQARGDMTIRTAILETRYLAGDKPLYDELVQRFDTEVVQGTAAEFVAAKLAEREERHRRGGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVRETAELVERGVFDAHEYRTFRRCSDFLWSVRCNLHFVSGRPEERLSFDLQREIAVRLGYTSHPGMQDVERFMKHYFLVAKQVGNLTAILCAKLEDQQAKAAPVLSRMISRLTTGSTWRRVPESDDFIVDNNRINLAAPDVFKHDPVNLIRIFRLAQKNNLAFHPDAMRAVTRSLNMINAELRENPEANRLFMEILTSNDAETVLRRMNETGVLGHFISAFGRIVSMMQFNMYHHYTVDEHLIRCIGFLQEIERGGHDEFVLASDLMRKIRPEHRAVIYITVLLHDVAKGRPEDHSVAGAKIARRLCPRLGFNNADTELVAWLIEEHLTMSTVAQSRDLSDRRTIEKFAAVVQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPVLTGGFSEVNRAKRITAAQAEFRNAFTDWPEDELNTYIGRHYPAYWLKVELPRKIRHARFVRSSEDAGHKLAINVGFDPARGVTELTIFAMDHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTIAISREYERDEDEGRRATRIGETIEQVLEGKLRLPDAVARRTTRGKQHKAFSVEPEVSINNQWSELYTVIEVSGLDRPGLLYELTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQINAPTRQAAIKSALLHLLASEDAAAQPAA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14)
Length
931 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
104.795 kDa
Sequence
MDLATTNDAAGAGNDFDTARITGDIDALAAKHAGHEDVFRAAVSRLLKAELAKVRDAAQAKLLRDRHGRRCAERLCFIQDEIIRLSFSAATRHLYHSPIPSDGERMAVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLNVGHATRSVNESIRQARRDMTVRTGILETRFLAGDRALYDELVTRFDTEVVQGTAAEFVTAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVHESRELLGCGVFDVREYRTFRRCADFLWSVRCNLHFATGRAEERLSFDLQREIAVRLGYTSHPGMQDVERFMKHYFLTAKDVGDLTAILCAKLEDQQAKPAPVLGRMMSRRRPGTELRRVPEGDDFIIDNNRINLAAPDVFKRDPVNLIRVFRLAQKNNLAFHPDALRTVTRSRRLINAQLRENPEANRLFMEILTSNDAETVLRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYTVDEHLLRCIGILQDIERGGNDELALASELMRKIHPEHRPVIYITTLLHDIAKGRPEDHSIAGARVARRLCPRLGFNASDTELIAWLIEQHLTMSKVAQSRDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPVLTGGFSEVNRVQRIAEAQAEFRAAFTEWSEPELNAYIARHYPAYWLKVDLAHKIRHARFLRASEQGGRKLNINVGFDEARGVTELTIFAADHPWLLSIIAGACASAGANIVDAQIYTTTDGQALDTIAISREYDRDEDEGRRAARIGEIIEQVIDGRLRLPDVVARRAAGKTRLRPFVVEPKVIVNNQWSDRHTVIEVSGLDRPGLLFQLTAAISKLNLNIASAHVATFGERARDVFYVTDLLGARITAPTRQAAIKRALIHLLANGGAAEQSVG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Length
930 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
105.347 kDa
Sequence
MAPASEAGPAQDPLFSGLILPRSRILDAEALTRSILAEIDAAGPLDPKSARAIAVRQMTEAKAAGNRALSETFEARPREARGLIRAQAALTDGLVTAALRVACERLHPLANPTEAERIAVLAVGGYGRAEMAPHSDVDLLFLTPWKITPWAEMVIESMLYMLWDLRLKVGHSSRTVKDCLRLGREDITIRTALLEHRFLAGHAPLAAELDETLWNDLFRGTGAEFIDAKLEERGQRHKRQGGQRYVLEPNVKEGKGGLRDLQTLYWIGKYLNRVPSPSGLVAAGLLTRDEFETFERAESFLWAVRCHLHYATGRATDQLTFDLQVEVAARMGYADTRGRRGVEVFMQDYFRHATRVGELTRVFLAQLEARHEKREPKIMGLFRRKKRLKPEYSLVNGRIDVLDPKAFLADKLNLLRIFEEALRTGFLIHPGAMRLIAANLHLIDEEMQHDREANRIFLDMLLRHGNPERALRRMNELGVLGAFIPEFERIVAMMQFNVYHHYTVDEHTIQCISTLAQIERHELDEELPIANRILTDGISRRVIYVALLLHDIGKGRPEDHSILGAQIARRVAPRFGLTAEECETVEWLVRYHLLMSDMAQKRDIGDPRTVRDFAKAVRSKKRLDLLTVLTVCDIRGVGPGTWNNWKAQLLRKLYRDTVTALDAGLESLNRENRADEAKRALRELLEEWDPKDLRAELARHYPPYWQALSNATHAVFARMLRGLGETEIRIDLDPDPDRDATRACFALADHPGIFSRLAGALALVGANVVDARTYTTKDGYATAVFWIQDSEGSPYEISRLPRLTSMIDKTLKGEVVAREALKDRDKLKKREAQFRFPTHIAFDNEGSDIYTIIEVDTRDRPGLLYDLTRTLAANNIYIASAVIATYGAQVVDSFYVKDMFGLKLHQKNRQETLEKKLRQAIVEGAERAKQ

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Length
929 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
105.033 kDa
Sequence
MDSVTTEHKQEVDDRFDTARITAAVDALAEKHQGREDAFRTAMAQLLKAELIAARAAAQAILLKDRHGRRCAERLCHVQDEIIRILYSAATRHLYRSPIPSGAERMAVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHATRSVDESIRQARGDMTIRTAILETRFLTGDQPLYDELVERFDKEVVQGTASEFVTAKLAEREERHRRGGQSRYLVEPNVKDGKGALRDLHTLFWIAKYVYRVRDTDELVERGVFDAQEYRTFRRCADFLWSVRCNLHFYSGRAEERLSFDLQREIAVRLGYTSHPGMQDVERFMKHYFLVAKEVGNLTAILCAKLEDQQAKPAPVLSRMMARLRPTPAKRRVPDSDDFIVDNNRINVAAPDVFKHDPVNLIRIFRLAQKHNLAFHPDAMRDVTRSLGLINAQLRENPEANRLFMEILTSDNAEIVLRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYTVDEHLIRCVGFLQDIERGGIEEFAVASDLMRKIRPEHRSVIYIATLLHDVAKGRPEDHSIAGAKVARRLCPRLGFSPADTELVAWLIEEHLTMSTVAQSRDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRSLYYETEPVLTGGFSEVDRGKRLTAAYAEFRNAFAEWPADELDAYIARHYPAYWLKVELPRKIRHARFVRSSEQAGHKLAINVGFDEVRGVTELTIFAADHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTISISREYDRDEDEGRRATRIGEMIEDVLEGKLRLPEVVARRTVRSKARPFVIEPEVTINNQWSDRYTVIEVSGLDRPGLLYELTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQINAPTRQSAIKSALTHVMAGDKAVQPAA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Length
929 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
104.542 kDa
Sequence
MSPSRPAADERFDSARVAAEIATLAEKHTGNDAAFRTALAMLMKAELAKARTEAEAQLLRDRHGRRCAERLCYVQDAIIRLLFNAATEYLYNTPTPSSSERMTVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEVILYCLWDIGLKVGHATRSVDECIRQARADMTIRTAILETRFLAGDEALYAELVERFDKEVVEGTAAEFVAAKLAEREERHRRSGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVREASELSERGVFDPAEFRTFRRCEDFLWSVRCNIHFVTKRAEDRLSFDLQREIGVRLGYTSHPGMQDVERFMKHYFLIAKEVGNLTAILCAKLEDQQAKAAPALTRMMARLRPAAKRRRVPESDDFVIDNNRINLAVPDVFKHDPVNLIRIFRLAQKNNLAFHPDAMRSVTRSLSLITPQLRDNPEANRLFVEILTSDNAEPVLRRMNETGVLGRFIRAFGRIVSMMQFNMYHSYTVDEHLIRCVGNLQEIERGGNDEFALSSELIRKIRPDHRAVLYAAVLLHDIAKGQPEDHSTAGAKVARRLCPRFGFSTADTELVAWLIEKHLVMSTVAQSRDLSDRKTIENFAAVVETVEQMKMLTILTTADIRGVGPGVWNGWKAQLIRTLYYETEPVLTGGFSEVNRAERIRAAQAEFRAAFTEWPEADLNAYVARHYPAYWLKVDLQRKIRHARFLRASEQAGHKLAINVGFDEARAVTELTILAVDHPWLLSVIAGACASAGANIVDAQIYTTTDGRALDTISISREYDRDEDEGRRATRIGETIEEVLEGKLRLPEAVARRASSGSKAKLRAFVVEPEVEINNNWSDRYTVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITAPTRQAAIKRALVHLLANGDAAEKPAA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Length
926 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
104.393 kDa
Sequence
MPVSFLSLASQPQIIDYPAIKEEIDSIKKVAAGDPVSEYRAVSLVLKQTVLKGREVIAEALTRRPHQGRIAALSYAYLTDQIIQLALYAMVGDDEKATDNLVILAVGGYGRGEMALHSDVDIAFLSRRSPRKAQKKLIESLISLLWDVGLRVSQSHRSLSDMVKMAKKDITIRTALLESRYLVGDKALFEEASTRFIQKVVAGSGRDFVAAKLLEWDERHLARGDSRYLVEPHLKEGKGGLRDLQSLFWIAKYLYLEKEARHTVLTSPILTDYALVKADLIAGHEAKRFRRCENFLWAVRCHLHILVKRPEERLNFDVQRSLAEKMGYRSKSGKSAVERFMHHYFLVTKMVGNLAALFIDALKVNHYLKPKSRRSGASKQIDGFPVIQGEIVLDDDFFFRHNPAALITLFAVAYRHRLDIHPLTLRQAGRDARLIDEALQNNPVCNAAFLTLFTLPYNPAPILKIMNNTGVLGRFIPDFGRIVAQMQFDMYHHYTVDEHAIRALDILWQIENNKLEDLYPLGSRLFKQLNARLVLYMALFLHDIAKGREGSHSALGAEIALRLCPRFGLTAAETKLVAWLVKNHLLMSHTAFQRDLADAKTITDFANAVKSPERLRLLYLLTVADISAVGPHIWNSWKNQLLTSLYEACSQCLLEGPTGHGAGRQQRIENRQNDVSEKLDWDNDLFHALVKRLPDDYWFSERTDVIAANMQQIIDTDSKGQSISVRGHEMPAYDATMISLYAIDHPGFFYRISGAIHATGGNILDARIHTTRDGMAMDNLLVQNSQGGMIKSGEHLNRMMQAIEDAATSHIRSSNKLAALRPPLFWRGKAFHVEPLVFIDNQASDRFTVIEVNAQDRPALLHDLGCALFNARLTISSAHIATYGERAVDVFYVSDLFSHKITNQNRLKAIEKRLLAAADAARISEK

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Length
926 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
104.393 kDa
Sequence
MPVSFLSLASQPQIIDYPAIKEEIDSIKKVAAGDPVSEYRAVSLVLKQTVLKGREVIAEALTRRPHQGRIAALSYAYLTDQIIQLALYAMVGDDEKATDNLVILAVGGYGRGEMALHSDVDIAFLSRRSPRKAQKKLIESLISLLWDVGLRVSQSHRSLSDMVKMAKKDITIRTALLESRYLVGDKALFEEASTRFIQKVVAGSGRDFVAAKLLEWDERHLARGDSRYLVEPHLKEGKGGLRDLQSLFWIAKYLYLEKEARHTVLTSPILTDYALVKADLIAGHEAKRFRRCENFLWAVRCHLHILVKRPEERLNFDVQRSLAEKMGYRSKSGKSAVERFMHHYFLVTKMVGNLAALFIDALKVNHYLKPKSRRSGASKQIDGFPVIQGEIVLDDDFFFRHNPAALITLFAVAYRHRLDIHPLTLRQAGRDARLIDEALQNNPVCNAAFLTLFTLPYNPAPILKIMNNTGVLGRFIPDFGRIVAQMQFDMYHHYTVDEHAIRALDILWQIENNKLEDLYPLGSRLFKQLNARLVLYMALFLHDIAKGREGSHSALGAEIALRLCPRFGLTAAETKLVAWLVKNHLLMSHTAFQRDLADAKTITDFANAVKSPERLRLLYLLTVADISAVGPHIWNSWKNQLLTSLYEACSQCLLEGPTGHGAGRQQRIENRQNDVSEKLDWDNDLFHALVKRLPDDYWFSERTDVIAANMQQIIDTDSKGQSISVRGHEMPAYDATMISLYAIDHPGFFYRISGAIHATGGNILDARIHTTRDGMAMDNLLVQNSQGGMIKSGEHLNRMMQAIEDAATSHIRSSNKLAALRPPLFWRGKAFHVEPLVFIDNQASDRFTVIEVNAQDRPALLHDLGCALFNARLTISSAHIATYGERAVDVFYVSDLFSHKITNQNRLKAIEKRLLAAADAARISEK

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255)
Length
925 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
104.377 kDa
Sequence
MVLPTTKDATAAGAGFDTVRIIGDIDALAEKHAGHEDVFRSAVSRLLKAELAKVRDAAQAKLLRDRHGRHCAEWLCFVQDEIIRLSFSAATRHLYHSPIPSDGERMAVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLNVGHATRSVNESIRQARRDMTVRTGILEARFLTGDRALYDELISRFDTEVVQGTAAEFVAAKLAEREERHHRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVRESHELLRRNVFDVREYRTFRRCADFLWSVRCNLHFATGRAEERLSFDLQREIAVRLGYTSHPGMQDVERFMKHYFLTAKDVGDLTAILCAKLEDQQAKPAPVLSRAMSKPPGAEVRRVPDSDDFIIDNNRINLAAPDLFKRDPVNLIRLFRLAQKNNLAFHPDALRMVRRSRRLINAQLREDPESNRLFIEILTSNDAETVLRRMNETGVLGEFIRAFGKIVSMMQFNMYHHYTVDEHLIRCIGILQDIERGDNDEVALAGELMRTINPEHRPVIYIATLLHDVAKGRPEDHSIAGARVARRLCPRLGFNAADTELVAWLIEQHLTMSKVAQSRDLSDRKTIENFAAVVQSVERMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPVLTGGFSEVNRAQRMAAAEAEFRAAFTEWSGHELNAYIARHYPAYWLKVDLEHKIRHARFLRASEQSGRKLNINVGFDEARGVTELTILAADHPWLLSIIAGACASAGANIVDAQIYTTTDGQALDTIAISREYERDEDEGRRAARIAEIIEQVLEGRLRLPDVMPSRAAGKRLRPFVVEPKVTINNQWSDRHTMIEVSGLDRPGLLFQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGARITAPTRQAAIKRALVHLLASGNTAE

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Erythrobacter litoralis (strain HTCC2594)
Length
919 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
104.003 kDa
Sequence
MTDPKVPRQRRIIDRRKLAAAVEALAEQQGEKARPAVLKVLREALEKGRDELSQRLLDRPSAGHQITAGHAFLVDQLVRVIFDHVTTHLYPVANRSSSERIAVLAVGGYGRAEMAPQSDVDIAFLHPSRRTPWCEQVTEAMLYFLWDLGFKVGQSSRTPEDMVRMAREDLTIRTALLEARFVWGDRELYDEARKRFWSEVVNGTERQFVAEKLAERDARHERMGGTRYVVEPNVKEGKGGLRDLQTLYWIGKYIHRARGAAELVDAGLLTETEYHGFRRAEGFLLAVRCHLHEITGRPEDRLTFDFQKQIAERMRFAERREKSAVERFMQYYFLQVKRVGSLTGVFLAQMDQQFARKRARTGLLAGFNAKSRMLKGYTVFGGKIAAPGDNWFRDDPVRLIEIFQLAEANGLEIDPRSMRQADRDSVLIKDQVRNDPRANAIFLDLLCGRNDPETALRWMNEAGVFGKFVPDFGRVNAQMQFNMYHHYTVDEHTIRAIGFLSKIEKGELAKEHPRSTREIHKVKSRRVAFVAALLHDIAKGRGGDHSILGAEVAEELCPRFGLDEDETDLVAWLVLQHLLMSSTAQKRDLTDPKTIEDFVAEVQSLERLRHLAILTSVDIRAVGPGTWNSWKGQLLGELYDAAHERLRLGHMKHHRSERVAAKKEAVREALGGKAALLEKHGRLLPDSYWIAEPENVISRNIVQYDVAREISEDLSIHCEFDEERGATLVTVIAADHPGLFYRIAGGIHLAGGNIIDARIHTTRNGWAIDNYLVQDPVGQPFAEERQLARIEQAIADAIANRGELVPKLAKRPLKQTRAGAFDVRPRVLFDNDASGRFTVIEVNARDRAALLNRLGRALFENQVIVQSAHITAYGERAADTFYVTDLTGAKITDESRMDTIRQALLDAASDARQAELEPA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Psychrobacter arcticus (strain DSM 17307 / 273-4)
Length
915 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
104.846 kDa
Sequence
MFNCAVTAIDLTPMPLLSTDNMTTAPLSLSTDTSLIEKSLFGIPEWLLQINDDISRALERGVNIRQLVSARACVIDDLLIGLFKWFELDKTDLALFATGGYGRGELSLHSDIDILLLMPHEIDADTSSKIDNLVALLWDIGLEPALSVRSVSECLEAALDHTIASALLEARLLIGNETLQDVPHQIVNNQWSPRAFYDVKIDEAKARYLQHNATEYNLEPNIKTAPGGLRDIHIVGWVTKRYFRVSKLYDLVQQNFLTEKEFDELSFSEGYLWQIRHYLHELTGRNENKLLFDYQREIAQLMGYDTQPDDQPNAAVERFMRDYYRCAMQISTLSEMLTNHYYETIIEPQLPDEERPKKQPINARFNQVGEQIAMAHHRVFAQHPESILEMFLLMGQYGIKNVRTHTLRALKIAARGIDQAYRDNPTHQTLFLANLKEQNYLFHRLRTMNRYGVLGNYIPAFAQVTGLMQYDLFHRYTVDAHTLFLIRILHRFIDPHFYEDFPLVSSIFQRIERKEILVLAAMFHDIAKGRGGNHSQLGEIESIEFCLAHGMSNADANLVGWLTRYHLLMSMTAQKKDISDPEVVTLFADLVGNVTHLNHLYVLTVADMNATNPQLWNSWRATLMKQLYSQTRRILRADIDAPTNRQDMISATRKQALMMLDNVDNQHMNRDEVLSLWDDLGDEYFLREIAEDILWHTEAILNHPPIGRASNADSPPLVVLREHRELALDAVQVFVYTQDQVNLFAVTMAVFDQMNLDVLDARIITATRDFALDSYVLLDRSGTLLVDSDSQQELKQRLIDAFKNPTAPKLTHKRIPRQLKHFDVETTINFEFNDASSQHIMSLETLDQPGLLARVGQVFLQQQIEVHAARITTLGERAEDMFYISDQNDQALSANKLKTLKTALIESLSVHNDSI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Psychrobacter cryohalolentis (strain K5)
Length
913 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
104.638 kDa
Sequence
MFNCDVTAIDLTPMPLFSADNMTTAFLSTDTSVVEKSLFGIPEWLLQINDDISRALERGVNIRQLVSARACVIDDLLIELFKCFGLDKTDLALFATGGYGRGELSLHSDIDILLLMPHDINADTSSKIDNLVALLWDIGLEPALSVRSVSDCLEAALDHTIASALLEARLLIGNDALQNVPHQIVNNQWSPRSFYDVKIDEAKARYLQHNATEYNLEPNIKTAPGGLRDIHIIGWVTKRYFRVSKLYDLVQQNFLTEKEFDELSFSENYLWQIRHYLHELTGRNENKLLFDYQREIAQLMGYDTQTDDQPNAAVERFMRDYYRCAMQISTLSEMLTNHYYETIIEAQLPDEERPKKQPINARFNQVGDQIAMAHHRVFAQHPESILEMFLLMGQYGIKNVRTHTLRALKIAARGIDQAYRDNPTHQTLFLANLKEQNYLFHRLRTMNRYGVLGNYIPAFAQVTGLMQYDLFHRYTVDAHTLFLIRILHRFTDPHFYEDFPLVSSIFQRIERKEILVLAAMFHDIAKGRGGNHSQLGEIESIEFCLAHGMSTADANLVGWLTRYHLLMSMTAQKKDISDPEVVTLFADLVGNVTHLNHLYVLTVADMNATNPQLWNSWRATLMKQLYSQTRRILRADIDAPTNRQDMISATRKQALVMLDNVDNQHMNRDEVLRLWDDLGDEYFLREIAEDILWHTEAILNHPPIGRASNADSPPLVVLREHRELALDAVQVFVYTQDQVNLFAVTMAVFDQMNLDVLDARIITATRDFALDSYVLLDRSGTLLVDSDSQQELKQRLIDAFKNPTAPKLTHKRIPRQLKHFDVATTINFDFNDASNQHIMSLETLDQPGLLARVGQVFLQQQIEVHAARITTLGERAEDMFYISDQNDQALSADKLKTLKTALIDSLSVRNDRV

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199)
Length
912 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
101.972 kDa
Sequence
MLPRIANQRAIVDRRALADAVSAAFAEQGDRSRPAVVELLRGALDSGRAELARRLEARPSAGTECAHGQAFLVDQLVRVIHDHVVGKVYRASNRSTGERIAIIAVGGYGRGEMAPHSDVDIAFVTPIKPTSWCEQVIEAILYFLWDLGLKVGHSSRSLDEVVRMAKSDLTIRTALLEGRYVWGDRDLFDAASARFWNEVVNGTEKQFVAEKLQERNERHKRLGDSRYVVEPNVKEGKGGLRDLHTLYWIGKYIHKVRDASELVDVGLLTAEEYRAFRRAENFFWAVRCHLHAITRRAEDRLTFDLQREVAMRMNFADRPGKSAVERFMQYFFLQAKQVGSLTGVFLAQLDGQFARQKRSFFASLRSRRKKVGPFFIEGGKLGVPAEDTFQQDPVRLVELFAVAASEKVEIHPEAMRLARRDAGLIDAAVRKDQRANALFLDVLTSRNDPETVLRWMNEAGVFGRFVPDFGRVVAQMQFDMYHHYTVDEHTIRAIGLLASIEKGEAKADHPLASEVVGKVASRRVLYVATLLHDIAKGRRGDHSVLGAEVAMKLCPRLGLSAAETELVAWLVRWHLLMSATAFKRDLADYKTIADFVNTVQSQERLRLLLLLTIVDIRAVGPGVWNSWKRQLLGDLFVSAEEVLRLGHKQHGRAERIIAKKKAVGAILKERDNLIGTVGRQLGDAYWIAEPEDIIALNLQQMDQALGELLSVEAHWYPARGATLVTVLAADHPGLFYRIAGGIHLAGGNIIDARIHTARNGTAVDNFLVQDPLGRPLNEASQIERLKNAIADALANRVKLVPQLAARPLARPRADAFDVRPIVIFDNKASNRFTVIEVGARDRPALLNRLARALFEARLIVHSAHIATYGERAVDTFYVTDVLGEKVDSEARMKAVEKRLLEAAEDRKVKDAA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
Length
908 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.501 kDa
Sequence
MFDTPAVFARITEAAAEAADNAALRGAVVAILRDVQNAGRAAIAEGFAEDPFAARPLTRAYTYLTDGMVKTAMYVASEILHPLATPTQGERIAVLAVGGFGRGEMAPFSDVDLLFLTPYKITAWAESVIESMLYILWDLRLKVGHSSRTVKDCIRLGRDDFTIRTAMLEHRFLAGHAPLARSLDQRLKSELYKDTQREFIEAKLEERDARHRKQGERYMVEPNVKEGKGGLRDLQSLYWIAKYIYEVKETAELVPLGLFTPSEYRTFVQAEEFLWAVRAHLHLVTGRATEQLTFDLQVEVAARMGYQDRAGRRGVEVFMQKYFREATRVGELTRIFLTKLEAAHMKGAPLLERIFRRRRRIKQGYKVVRGRLDVVDPEAFLADKLNLLRIFEEALRTGMLIHPDAMRLVTANLDLIDDGMRNDKEARRIFLDLLLKHGNPERALRRMNELGVLSAFVPEFEPIVAMMQFNMYHSYTVDEHTIQTIVNLAQIEKGELVESLPLASSILKAGVNRKVLYVALLLHDIGKGRPEDHSILGARIARKVAPRLGLSKADCETVEWLVRYHLLMSDMAQKRDISDPRTVRDFAKAVQTTKRLDLLTVLTVCDIRGVGPNTWNNWKATLLRALHAETKRALEMGMEALNREGRGNEAKKALRTALSDWPAGEVKTEIARHYPPYWQGFNVETHVTFAEMLRQLEHSGDPGGIEIRLDPDEDRDATRACFAMADHPGIFSRMAGALALVGANVVDARSYTTKDGYVTDAFWIQDAEGHPYEAARLPRLSQMILKTLKGEVVARDALKSRDKIKKREKAFNVPTHITFDNEGSDIYTIIEVDTRDRPGLLYDLARALAAANVYIANAVIATYGEQVVDSFYVKDMFGLKYHSEAKQRTLETKLRKAITEGAERAAAS

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)
Length
904 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
104.412 kDa
Sequence
MTDKRFSPDNTPPDASSPDSPIDTIAAAQPPVSPLTYADDMLNCQALKQQLELFQLWLGSEFRSGVSAEKLIDARTLFIDRLLQRLWYCHGFENIAQTALVAVGGYGRGELHPLSDIDVLVLSQTELSDEHSQRVGQFITLLWDLKLEVGHSVRTLEECLQEGRADISVATNLIESRMICGDVALFLTLQKHVFSDEFWPSPTFFPAKITEQQERHQRYHSTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSLNEMVGFGFLTEAERKELNECQSFLWRIRFALHLILPRYDNRLLFDRQLNVAQLLQYQGEGNTPVERMMKDFYRMTRRVSELNQMLLQLFDEAILALDASEKPRPIDDEFQLRGNLVDLRDENLFIKKPEAIMRMFYLMVRNRDISGIYSTTLRQLRHARRHLASPLCTIPEARQLFMNILRHPYAVSRALLPMHRHSVLWAYMPLWGNIVGQMQFDLFHAYTVDEHTIRVLLKLESFADEDTRPQHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSELGALDVLEFAALHGLNSREAQLVSWLVRCHLLMSVTAQRRDIQDPTVIQQFATEVQSETRLRYLVSLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDLRERVRHHRLQALALLRMDNIDEEALHHIWSRCRADYFLRHSPNQIAWHARHLLEHDTNKPLVLISHQASRGGTEIFIWSPDRPYLFAAVAGELDRRNLSVHDAQIFTSRDGMAMDTFIVLEPDGSPLAQDRHEMIRHALEQALTQRHYQHPRVRRTSPKLRHFSVPTEVNFLPTHTDRRSYMELSALDQPGLLARIGEIFSDLNLSLHGARISTIGERVEDLFILADSDRRALKPELRLKLQERLTEALNPNDKVPLS

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pectobacterium carotovorum subsp. carotovorum (strain PC1)
Length
904 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
104.374 kDa
Sequence
MTDNRFSPDSTPPDASSPDSPVDTIASTQLPASPLTYADDMLNCQTLKQQLELFQLWLGSEFRSGVSAEKLIDARTLFIDRLLQRLWYFYGFENIAQTSLVAVGGYGRGELHPLSDIDVLVLSQTALSEEHSQRVGQFITLLWDLKLEVGHSVRTLEECLQEGRADISVATNLIESRMICGDVALFLTLQKHVFSDEFWPSSAFFPAKIAEQQERHQRYHSTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSLNEMVGFGFLTEAERKELNECQSFLWRIRFALHLILPRYDNRLLFDRQLNVAQLLQYQGEGNTPVERMMKDFYRMTRRVSELNQMLLQLFDEAILALDASEKPRPIDDEFQLRGNLVDLRDENLFIKKPEAIMRMFYLMVRNRDISGIYSTTLRQLRHARRHLASPLCTIPEARQLFMNILRHPHAVSRALLPMHRHSVLWAYMPLWGNIVGQMQFDLFHAYTVDEHTIRVLLKLESFADEETRPQHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSELGAQDVLEFAALHGLNSREAQLVSWLVRCHLLMSVTAQRRDIQDPTVIQQFATEVQSETRLRYLVSLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDLRERVRHHRLQALALLRMDNIDEEALHHIWSRCRADYFLRHSPNQLAWHARHLLEHDVNKPLVLISHQASRGGTEIFIWSPDRPYLFAAVAGELDRRNLSVHDAQIFTSRDGMAMDTFIVLEPDGSPLAQDRHEMIRHALEQALTQRHYQHPRVRRPSPKLRHFSVPTEVNFLPTHTDRRSYMELSALDQPGLLARIGEIFADLNLSLHGARISTIGERVEDLFILADSDRRALKPELRLKLQERLTEALNPNDKVPLS

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudomonas aeruginosa (strain PA7)
Length
900 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.468 kDa
Sequence
MPQVDPELFDRGQFQAELALKSSPIAAFKKAIRQFREVLDNRFNSGRDIRRLIEDRAWCVDQVLQQAWQRFDWGDDADIALIAVGGYGRGELHPYSDVDLLILLDSEDQESFREPIEGFLTLLWDIGLEVGQSVRSVRQCAEEARADLTVITTLMECRTICGPDSLRQRMLEVTGSTRMWPSKEFFLAKRHEQQRRHAKYNDTEYNLEPNVKGSPGGLRDIQTILWMARRQFGSLNLHALVREGFLVESECSMLASSQEFLWRVRYALHMLAGRAEDRLLFDHQRSIARLFGYEDNDVKLAVERFMQKYYRVVMAISELNDLIVQHFEEVILPCEQPVQIQPLNSRFQLRDGYIEVTHPNVFKRTPFALLEIFVLMAQHPEIKGVRADTIRLLRDSRHLIDDEFRHDIRNTSLFIELFKSSQGIHRNLRRMNRYGILGRYLPEFGHIIGQMQHDLFHIYTVDAHTLNLIKHLRKLNRPEMAEKYPLASKIIDRLPKPELIYIAGLYHDIAKGRGGDHSELGAVDAEAFCQSHQLPLWDTQLVSWLVQNHLVMSTTAQRKDLSDPQVIFDFAQLVGDQTHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRQTQTAALDQLVRNGIDQDDAEQLWSQLGDDYFLRHTAGDVAWHTEAILQHPDDGTPLVLIKETTQREFESGSQIFIYAADQHDFFAVTVAAMDQLNLSIQDARIITSTSQFTLDTYIVLDADGDSIGNNPERIAEIREGLIDALKNPDDYPTIIQRRVPRQLKHFAFAPQVTISTDALRQVSVLEVIAPDRPGLLARIGGIFLDFDLSVQNAKIATLGERVEDVFYITDARNQPLADPDLCKRLQAALVEQLSQDNGRDTLPTRINF

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudomonas aeruginosa (strain LESB58)
Length
900 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.432 kDa
Sequence
MPQVDPELFDRGQFQAELALKSSPIAAFKKAIRQFREVLDNRFNSGRDIRRLIEDRAWCVDQILQQAWQRFDWGDDADIALVAVGGYGRGELHPYSDVDLLILLDSEDQESFREPIEGFLTLLWDIGLEVGQSVRSVQQCAEEARADLTVITTLMECRTICGPDSLRQRMLRVTGSAHMWPSKEFFLAKRHEQQRRHAKYNDTEYNLEPNVKGSPGGLRDIQTILWMARRQFGSLNLHALVREGFLVESECSMLASSQEFLWRVRYALHMLAGRAEDRLLFDHQRSIARLFGYEDNDVKLAVERFMQKYYRVVMAISELNDLIIQHFEEVILPCEQPVQIQPLNSRFQLRDGYIEVTHPNVFKRTPFALLEIFVLMAQHPEIKGVRADTIRLLRDSRHLIDDEFRHDIRNTSLFIELFKSSQGIHRNLRRMNRYGILGRYLPEFGHIIGQMQHDLFHIYTVDAHTLNLIKHLRKLNRPEMAEKYPLASKIIDRLPKPELIYIAGLYHDIAKGRGGDHSELGAVDAEAFCQSHQLPLWDTQLVSWLVQNHLVMSTTAQRKDLSDPQVIFDFAQLVGDQTHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRQTQTAALDQLVRNGIDQDDAEQLWSQLGDDYFLRHTAGDVAWHTEAILQHPDDGTPLVLIKETTQREFESGSQIFIYAADQHDFFAVTVAAMDQLNLSIQDARIITSTSQFTLDTYIVLDADGDSIGNNPERIAEIREGLIDALKNPDDYPTIIQRRVPRQLKHFAFAPQVTISTDALRQVSVLEVIAPDRPGLLARIGGIFLDFDLSVQNAKIATLGERVEDVFYITDARNQPLADPDLCKRLQAALVEQLSQDNGRDTLPTRINF

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudomonas aeruginosa (strain UCBPP-PA14)
Length
900 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.418 kDa
Sequence
MPQVDPELFDRGQFQAELALKSSPIAAFKKAIRQFREVLDNRFNSGRDIRRLIEDRAWCVDQILQQAWQRFDWGDDADITLVAVGGYGRGELHPYSDVDLLILLDSEDQESFREPIEGFLTLLWDIGLEVGQSVRSVQQCAEEARADLTVITTLMECRTICGPDSLRQRMLQVTGSAHMWPSKEFFLAKRHEQQRRHAKYNDTEYNLEPNVKGSPGGLRDIQTILWMARRQFGSLNLHALVREGFLVESECSMLASSQEFLWRVRYALHMLAGRAEDRLLFDHQRSIARLFGYEDNDVKLAVERFMQKYYRVVMAISELNDLIIQHFEEVILPCEQPVQIQPLNSRFQLRDGYIEVTHPNVFKRTPFALLEIFVLMAQHPEIKGVRADTIRLLRDSRHLIDDEFRHDIRNTSLFIELFKSSQGIHRNLRRMNRYGILGRYLPEFGHIIGQMQHDLFHIYTVDAHTLNLIKHLRKLNRPEMAEKYPLASKIIDRLPKPELIYIAGLYHDIAKGRGGDHSELGAVDAEAFCQSHQLPPWDTQLVSWLVQNHLVMSTTAQRKDLSDPQVIFDFAQLVGDQTHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRQTQTAALDQLVRNGIDQDDAEQLWSQLGDDYFLRHTAGDVAWHTEAILQHPDDGTPLVLIKETTQREFESGSQIFIYAADQHDFFAVTVAAMDQLNLSIQDARIITSTSQFTLDTYIVLDADGDSIGNNPERIAEIREGLIDALKNPDDYPTIIQRRVPRQLKHFAFAPQVTISTDALRQVSVLEVIAPDRPGLLARIGGIFLDFDLSVQNAKIATLGERVEDVFYITDARNQPLADPDLCKRLQAALVEQLSQDNGRDTLPTRINF

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Length
900 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.404 kDa
Sequence
MPQVDPELFDRGQFQAELALKSSPIAAFKKAIRQFREVLDNRFNSGRDIRRLIEDRAWCVDQILQQAWQRFDWGDDADIALVAVGGYGRGELHPYSDVDLLILLDSEDQESFREPIEGFLTLLWDIGLEVGQSVRSVQQCAEEARADLTVITTLMECRTICGPDSLRQRMLQVTGSAHMWPSKEFFLAKRHEQQRRHAKYNDTEYNLEPNVKGSPGGLRDIQTILWMARRQFGSLNLHALVREGFLVESECSMLASSQEFLWRVRYALHMLAGRAEDRLLFDHQRSIARLFGYEDNDVKLAVERFMQKYYRVVMAISELNDLIIQHFEEVILPCEQPVQIQPLNSRFQLRDGYIEVTHPNVFKRTPFALLEIFVLMAQHPEIKGVRADTIRLLRDSRHLIDDEFRHDIRNTSLFIELFKSSQGIHRNLRRMNRYGILGRYLPEFGHIIGQMQHDLFHIYTVDAHTLNLIKHLRKLNRPEMAEKYPLASKIIDRLPKPELIYIAGLYHDIAKGRGGDHSELGAVDAEAFCQSHQLPLWDTQLVSWLVQNHLVMSTTAQRKDLSDPQVIFDFAQLVGDQTHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRQTQTAALDQLVRNGIDQDDAEQLWSQLGDDYFLRHTAGDVAWHTEAILQHPDDGTPLVLIKETTQREFESGSQIFIYAADQHDFFAVTVAAMDQLNLSIQDARIITSTSQFTLDTYIVLDADGDSIGNNPERIAEIREGLIDALKNPDDYPTIIQRRVPRQLKHFAFAPQVTISTDALRQVSVLEVIAPDRPGLLARIGGIFLDFDLSVQNAKIATLGERVEDVFYITDARNQPLADPDLCKRLQAALVEQLSQDNGRDTLPTRINF

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudomonas entomophila (strain L48)
Length
900 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.904 kDa
Sequence
MPQVDPELFDRGQFQAELALKASPIAAFKKAIRMAGEVLDKRFREGREIRRLIEDRAWFVDNILQQAWNQFDWGNPDGIALVAVGGYGRGELHPYSDIDLLILLDAAEHEQYRDAIERFLTLLWDIGLEVGQSVRTVDECAEQARADLTVITNLMESRTIAGPEPLRQRMLDATSTAHMWPSKEFFLAKRAELKARHHKYNDTEYNLEPNVKGGPGGLRDIQTVLWVARRQYGTLNLHALAGEDFLLESENELLASSQAFLWRVRYALHMLAGRAEDRLLFDHQRSIATLLGFNDENPKRAIEQFMQQYYRVVMSISQLCDLIIQHFEEVILADDDSGTTQPLNARFRLHDGYIEAVHPNVFRRTPFAMLEIFVLMAQHPEIKGVRADTVRLLREHRHLIDDKFRNDIRNTSLFIELFKCEIGIHRNLRRMNRYGILGRYLPEFGLIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTPVSEKFPLASKLMGRLPKPELIYLAGLYHDIGKGRQGDHSELGAVDAHAFCARHQLPAWDSRLIVWLVLNHLVMSTTAQRKDLSDPQVINDFALHVGDETRLDYLYVLTVADINATNPSLWNSWRASLLRQLYTETKRALRRGLENPLDREEQIRQTQSAALDILVREGTDPDDVEQLWSQLGDDYFLKHNAADVAWHSDAILQQPADSGPLVLIKETTQREFEGGTQIFIYAPDQHDFFAVTVAAMAQLNLNIHDARIITSSSQFTLDTYIVLDNDGGSIGDNPQRVKQIRDGLTEALRTPEDYPAIIQRRVPRQLKHFDFPPQVTILNDAQRPVTILEITAPDRPGLLARIGRIFLEFDISLQNAKIATLGERVEDVFFITDADNQPLSDPQLCSRLQEAIIQQLQAGQASEASPSRMTF

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
Length
900 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.314 kDa
Sequence
MPQVDPELFDRGQFQAELALKASPIAAFKKAIRQAREVLDTRFRSGREIRRLIEDRAWFIDNILQKAWDQFSWSEDADIALVAVGGYGRGELHPYSDIDLLILLDSADHEIFRDSIERFLTLLWDIGLEVGQSVRSVDECAEQARADLTVITNLMESRTIAGPEHLRQRMLQVTSTEHMWPSKDFFLAKRAEQKARHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLRALAGEGFLVESENALLASSQEFLWKVRYALHMLAGRAEDRLLLDHQRSIATLLGFEGEDAKQSIESFMQQYYRVVMSIAQLSDLIIQHFEEVILAPEDEAPPQPINARFQLHDGYIEAINDNVFKRTPFAMLEIFVLMAQHPEIKGVRADTIRLLREHRHLIDDDFRHDIRNTSLFIELFKCEIGIHRNLRRMNRYGILGRYLPEFGFIVGQMQHDLFHIYTVDAHTLNLIKHLRKMQYTPISEKFPLASKLMGKLPKPELIYLAGLYHDIGKGRHGDHSEIGAVDAEAFCVRHQLPQWDTRLIVWLVQNHLVMSTTAQRKDLSDPQVIHDFAQIVVDQTRLDYLYVLTVADIYATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRQTQSAALDILVRNGTDPDEVEQLWSQLGDDYFLRHTAGDVAWHSDAILQQPADGGPLVLIKEITQREFEGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARIITSSSQFTLDTYIVLDNDGESIGNNPQRVEQIRKGLTDALRNPDDYPTIIQRRVPRQLKHFAFAPEVTIHNDAQRPVTVLELSAPDRPGLLARIGKIFLEFDLSLQNAKIATLGERVEDVFFITDAHNQPLSDPQLCSRLQDAIVEQLSVSHEPTIEMTRLSI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudomonas fluorescens (strain SBW25)
Length
900 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.012 kDa
Sequence
MPQVDPELFDRGQFQAELALKASPIAAFKKAIRQAREVLDGRFRSGRDIRRLIEDRAWFVDNILQKAWEQFSWSEDADIALVAVGGYGRGELHPYSDIDLLILLDSADHEIFRDSIERFLTLLWDIGLEVGQSVRSVDECAEEARADLTVITNLMESRTIAGPERLRQRMLEVTSTAHMWPSKDFFLAKRAEQKARHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLRALAGEGFLVESENALLASSQEFLWKVRYALHMLAGRSEDRLLFDHQRSIATLLGFEGEDAKTSIESFMQQYYRVVMSIAQLSDLIIQHFEEVILAPEDEAPPQPINSRFQLHDGYIEARNDNVFRRTPFAMLEIFVLMAQQPEIKGVRADTIRLLRENRHLIDDDFRNDIRNTSLFIELFKCKIGIHRNLRRMNRYGILGRYLPEFGFIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTQVSEKFPLASKLMAKLPKPELIYLAGLYHDIGKGRHGDHSEIGAVDAEAFCQRHQLPLWDSRLIVWLVQNHLVMSTTAQRKDLSDPQVIHDFAGIVEDETRLDYLYVLTVSDINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRRTQSAALDILVRGGNDPDDVEQLWSQLGDDYFLRHTAGDVAWHSDAILQQPADGGPLVLIKETTQREFEGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARVITSSSQFTLDTYIVLDTEGESIGDNPVRVKKIREGLTEALRNPDDYPTIIQRRVPRQLKHFAFAPQVTISNDAQRPVTVLELSAPDRPGLLARIGGIFLEFDLSLQNAKIATLGERVEDVFFITDADNQPLSDPELCRRLQDAIVQQLSVTQEPGVELTRLTI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1)
Length
900 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.521 kDa
Sequence
MPQVDPELFDRGQFQAELALKASPIAAFKKAIRLAGEVLDKRFSAGSDIRPLIEARAWLVDNILQQAWNQFDWGDQSGIALVAVGGYGRGELHPHSDIDLLILLGAAEHEQYRDAIERFLTLLWDIGLEVGQSVRTVDECAEQARADLTVITNLMESRTIAGPEALRQRMLEVTSTAHMWPSKEFFLAKRAELKARHHKYNDTEYNLEPNVKGSPGGLRDIQTVLWVARRQYGTLNLHALAGEGFLLESENELLASSQDFLWKVRYALHMLAGRAEDRLLFDHQRSIATLLGYSDENPKRAIEQFMQQYYRVVMSISQLCDLIIQHFEEVILADEESGSTQPLNARFRLHDGYIEAAHPNVFKRTPFAMLEIFVLMAQHPEIKGVRADTVRLLREHRHLIDDTFRTDIRNTSLFIELFKCEIGIHRNLRRMNRYGILGRYLPEFGLIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTPVSEKFPLASKLMGRLPKPELIYLAGLYHDIGKGRQGDHSEIGAVDAQKFCERHQLPAWDSRLIVWLVQNHLVMSTTAQRKDLSDPQVINDFALHVGDETRLDYLYVLTVADINATNPSLWNSWRASLLRQLYTETKRALRRGLENPLDREEQIRQTQSSALDILVREGTDPDDVEQLWAQLGDDYFLKHTAADVAWHTDAILQQPADGGPLVLIKETTQREFEGGTQIFIYAPDQHDFFAVTVAAMSQLNLNIHDARIITSSSQFTLDTYIVLDNDGGSIGDNPQRVKQIRDGLTEALRNPEDYPTIIQRRVPRQLKHFDFPPQVTILNDAQRPVTILEITAPDRPGLLARLGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQPLSDPQLCSRLQEAIVQQLQAGQGSDTSQTRVTF

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudomonas fluorescens (strain Pf0-1)
Length
900 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.82 kDa
Sequence
MPQVDPELFDRGQFQAELALKASPIAAFKKAIRQAREVLDARFRAGRDIRRLIEDRAWFVDNILQKAWDQFDWSEDADIALVAVGGYGRGELHPYSDIDLLILLDSADHEIFRDSIERFLTLLWDIGLEVGQSVRSVDECAEEARADLTVVTNLMESRTICGPERLRQRMLDVTSTAHMWPSKDFFLAKRAEQKARHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLRALAGEGFLVESENALLASSQEFLWKVRYALHMLAGRSEDRLLFDHQRTIAGLLGFEGDDAKQAVENFMQQYFRVVMSIAQLSDLIIQHFEEVILAPEDEAPPQPINSRFQLHDGYIEARNDNVFRRTPFAMLEIFVLMAQQPEIKGVRADTIRLLRENRHLIDDNFRNDIRNTSLFIELFKCKIGIHRNLRRMNRYGILGRYLPEFGFIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTQVSEKFPLAAKLMAKLPKPELIYMAGLYHDIGKGRHGDHSEIGAVDAEAFCQRHQLPVWDSRLIVWLVQNHLVMSTTAQRKDLSDPQVIHDFALAVGDETRLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRQTQSAALDILVRGGTDPDDVEQLWAQLGDDYFLRHTAGDVAWHTDAILQQPADGGPLVLIKETTQREFEGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARVITSSSQFTLDTYIVLDTDGDSIGDNPVRVKQIRDGLTEALRNPADYPTIIQRRVPRQLKHFAFAPQVTIHNDAQRPVTVLELTAPDRPGLLARVGGIFLEFDLSLQNAKIATLGERVEDVFFITDAHNQPLSDPLLCSRLQDAIVEQLSVNQEPDIKLSRISI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudomonas putida (strain GB-1)
Length
900 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.573 kDa
Sequence
MPQVDPELFDRGQFQAELALKASPIAAFKKAIRLAGEVLDKRFRAGSEIRPLIEARAWLVDNILQQAWNQFDWGDQSGIALVAVGGYGRGELHPHSDIDLLILLGAAEHEQYRDAIERFLTLLWDIGLEVGQSVRTVDECAEQARADLTVITNLMESRTICGPEALRQRMLEVTSTAHMWPSKEFFLAKRAELKARHHKYNDTEYNLEPNVKGSPGGLRDIQTVLWVARRQYGTLNLHALAGEGFLLESENELLASSQDFLWKVRYALHMLAGRAEDRLLFDHQRSLATLLGYGDDNPKRAIEQFMQQYYRVVMSISQLCDLIVQHFEEVILADEESGSTQPLNARFRLHDGYIEAANPNVFKRTPFAMLEIFVLMAQRPEIKGVRADTVRLLREHRHLIDDTFRTDIRNTSLFIELFKCEIGIHRNLRRMNRYGILGRYLPEFGLIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTPVSEKFPLASKLMGRLPKPELIYLAGLYHDIGKGRQGDHSEIGAVDAQKFCERHQLPAWDSRLIVWLVQNHLVMSTTAQRKDLSDPQVINDFALHVGDETRLDYLYVLTVADINATNPSLWNSWRASLLRQLYTETKRALRRGLENPLDREEQIRQTQSSALDILVREGTDPDDVEQLWSQLGDDYFLKHNAADVAWHTDAILQQPADGGPLVLIKETTQREFEGGTQIFIYAPDQHDFFAVTVAAMSQLNLNIHDARIITSSSQFTLDTYIVLDNDGGSIGDNPQRVKQIRDGLTEALRNPEDYPTIIQRRVPRQLKHFDFPPQVTILNDAQRPVTILEITAPDRPGLLARLGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQPLSDPQLCSRLQEAIVQQLQAGQGSDTSPTRVTF

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
Length
900 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.621 kDa
Sequence
MPQVDPELFDRGQFQAELALKASPIAAFKKAIRLAGEVLDKRFRAGSDIRPLIEARAWLVDNILQQAWNQFDWGDQSGIALVAVGGYGRGELHPHSDIDLLILLGAAEHEQYRDAIERFLTLLWDIGLEVGQSVRTVDECAEQARADLTVITNLMESRTIAGPEALRQRMLEVTSTAHMWPSKEFFLAKRAELKARHHKYNDTEYNLEPNVKGSPGGLRDIQTVLWVARRQYGTLNLHALAGEGFLLESENELLASSQDFLWKVRYALHMLAGRAEDRLLFDHQRSIATLLGYSDENPKRAIEQFMQQYYRVVMSISQLCDLIIQHFEEVILADEESGSTQPLNARFRLHDGYIEATHPNVFKRTPFAMLEIFVLMAQHPEIKGVRADTVRLLREHRHLIDDTFRTDIRNTSLFIELFKCEIGIHRNLRRMNRYGILGRYLPEFGLIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTPVSEKFPLASKLMGRLPKPELIYLAGLYHDIGKGRQGDHSEIGAVDAQKFCERHQLPAWDSRLIVWLVQNHLVMSTTAQRKDLSDPQVINDFALHVGDETRLDYLYVLTVADINATNPSLWNSWRASLLRQLYTETKRALRRGLENPLDREEQIRQTQSSALDILVREGTDPDDVEQLWAQLGDDYFLKHTAADVAWHTDAILQQPADGGPLVLIKETTQREFEGGTQIFIYAPDQHDFFAVTVAAMSQLNLNIHDARIITSSSQFTLDTYIVLDNDGGSIGDNPQRVKQIRDGLTEALRNPEDYPTIIQRRVPRQLKHFDFPPQVTILNDAQRPVTILEITAPDRPGLLARLGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQPLSDPQLCSRLQEAIVQQLQAGQGSDTSQTRVTF

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudomonas putida (strain W619)
Length
900 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.914 kDa
Sequence
MPQVDPELFDRGQFQAELALKASPIAAFKKAIRQAGEVLDRRFRDGRDIRRLIEDRAWLVDNILQQAWKQFDWGDADGIALVAVGGYGRGELHPHSDIDLLILLRDAEHEQYRDAIERFLTLLWDIGLEVGQSVRTVDECAEQARADLTVITNMMESRTIAGREALRQRMLEVTSTAHMWPSKEFFLAKRAELKARHHKYNDTEYNLEPNVKGSPGGLRDIQTVLWVARRQYGTLNLHALAGEGFLLESENELLASSQDFLWKVRYALHMLAGRAEDRLLFDHQRSIAALLGYSDENPKRAIEQFMQQYYRVVMSISQLCDLIIQHFEEVILADDDSGTTQPLNARFRLHDGYIEAVNANVFKRTPFAMLEIFVLMAQHPEIKGVRADTVRLLREHRHLIDDTFRNDIRNTSLFIELFKCEIGIHRNLRRMNRYGILGRYLPEFGLIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTPVSEKFPLASKLMGRLPKPELIYLAGLYHDIGKGRQGDHSELGAVDAKKFCERHQLPAWDSRLIVWLVQNHLVMSTTAQRKDLSDPQVINDFALHVGDETRLDYLYVLTVADINATNPSLWNSWRASLLRQLYSETKRALRRGLENPLDREEQIRQTQSAALDILVREGTDPDDVEQLWSQLGDDYFLKHNAADVAWHSDAILQQPADGGPLVLIKETTQREFEGGTQIFIYAPDQHDFFAVTVAAMSQLNLNIHDARIITSSSQFTLDTYIVLDNDGGSIGDNPQRVKQIRDGLTEALRNPEDYPTIIQRRVPRQLKHFNFPPQVTILNDAQRAVTILEITAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQPLSDPQLCSRLQEAIVQQLQAGQASDASPTRVTF

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudomonas stutzeri (strain A1501)
Length
900 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.974 kDa
Sequence
MPQVDPELFDRSQFQAELALKASPIAAYKKAIRQARQVLDERFRAGRDIRRLIEDRAWFVDQILRSAWSRFDWDKGADIALVAVGGYGRGELHPYSDIDLLILLDENDQEIFREPIEGFLTLLWDIGLEVGQAVRSVAECADEARADLTVITNLMESRTIAGPERLRQAMLQVTSTQQMWPSKEFFLAKRNEQRARHAKYNNTEYNLEPNVKGSPGGLRDIQTILWIARREFGTLNLQAMVDQGFITEGEHSLLTAAQEFLWKVRYGLHMLAGRAEDRLLFDHQRSLAALLGYEDSDAKLAIERFMQKYYRVVMSIAELSDLVGQHFAEVILWEGESGPIVPLNSRFQVRDGYLEVSNPAIFKRTPFAILETFVLLAQHPDIQGVRSDTIRLLRDHRYLIDDTFRQDLRNTSLFIELFKCKEGIHRNLRRMNRYGILGRYLPEFGHIVGQMQHDLFHIYTVDAHTLNVIKYLRKLTKPGVAEKYPLASKLVEKLPKPELIYIAGLYHDIAKGRGGDHSELGAVDAEQFCRRHKLPAWDTRLVVWLVENHLVMSTTAQRKDLSDPQVINDFAQRVGDETHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALKRGLENPLGREEQIRQTQRAALDDLVRHGTDPDDAEQLWAQLGDDYFLRHTATDVAWHTDAIIEHPANGGPLVLIKETTQREFEGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARILTSSSQFTLDTYIVLEADGSPIGNNPERIEEIRSGLIAALRNPDDYLTIIQRRVPRQLKHFAFPPQVTIHNDTQRPQTILEIIAPDRPGLLARVGQLFLDFDLSVQNAKIATLGERVEDVFFVTDADNQPLSDPQLCLRLQQAIIKELQQENEQQPSPSSIVI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
Length
899 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.58 kDa
Sequence
MPQVDPDLFDPGQFQAELALKSSPIPAYKKALRCAREVLDARFQEGRDIRRLIEDRAWFVDQILALAWNRFDWSEDADIALIAVGGYGRGELHPYSDIDLLILMDGADHEVFREPIEGFLTLLWDIGLEVGQSVRSLAECAEEAQADLTVITNLMESRTIAGPEHLRQRMQEVTSAQRMWPSRAFFLAKRDEQKTRHARYNDTEYNLEPNVKGSPGGLRDIQTLLWIARRQFGTINLHAMVGQGFLLESEYTLLASSQEFLWKVRYALHMLAGRAEDRLLFDLQRQIAGLLGYEDSDAKLAVERFMQKYYRVVLGIAELTELVFQHFEEVILPGDAAGRVEPLNERFQVRDGYLEVTHAGVFQETPSALLEIFVLLARRPEIRGVRADTIRLLRDHRYLIDDAFRRDPHNTGLFIELFKSRQGIHRNLRRMNRYGILGRYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKNLRKLFWPELAEKYPLASKLIEKLPKPELIYLAGLYHDIGKGRGGDHSELGAADALAFCQRHDLPAMDTQLIVWLVRNHLLMSTTAQRKDLSDPQVIFDFAQKVRDQTYLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKHALRRGLEQPVGREEQIRQTQKAALDILVRSGTDPDDAEHLWTQLGDDYFLRHTSSDIAWHTEAILQHPSSGGPLVLIKETTQREFEGATQIFIYAPDQHDFFAVTVAAMDQLNLSIHDARVITSTSQFTLDTYIVLDADGGSIGNNPARIQEIRQGLVEALRNPADYPTIIQRRVPRQLKHFAFAPQVTIQNDALRPVTILEIIAPDRPGLLARIGKIFLDFDLSLQNAKIATLGERVEDVFFVTDAHNQPLSDPELCARLQLAIAEQLADGDSYIQPSRISI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Azotobacter vinelandii
Length
899 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory protein GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII protein and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII protein, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.58 kDa
Sequence
MPQVDPDLFDPGQFQAELALKSSPIPAYKKALRCAREVLDARFQEGRDIRRLIEDRAWFVDQILALAWNRFDWSEDADIALIAVGGYGRGELHPYSDIDLLILMDGADHEVFREPIEGFLTLLWDIGLEVGQSVRSLAECAEEAQADLTVITNLMESRTIAGPEHLRQRMQEVTSAQRMWPSRAFFLAKRDEQKTRHARYNDTEYNLEPNVKGSPGGLRDIQTLLWIARRQFGTINLHAMVGQGFLLESEYTLLASSQEFLWKVRYALHMLAGRAEDRLLFDLQRQIAGLLGYEDSDAKLAVERFMQKYYRVVLGIAELTELVFQHFEEVILPGDAAGRVEPLNERFQVRDGYLEVTHAGVFQETPSALLEIFVLLARRPEIRGVRADTIRLLRDHRYLIDDAFRRDPHNTGLFIELFKSRQGIHRNLRRMNRYGILGRYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKNLRKLFWPELAEKYPLASKLIEKLPKPELIYLAGLYHDIGKGRGGDHSELGAADALAFCQRHDLPAMDTQLIVWLVRNHLLMSTTAQRKDLSDPQVIFDFAQKVRDQTYLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKHALRRGLEQPVGREEQIRQTQKAALDILVRSGTDPDDAEHLWTQLGDDYFLRHTSSDIAWHTEAILQHPSSGGPLVLIKETTQREFEGATQIFIYAPDQHDFFAVTVAAMDQLNLSIHDARVITSTSQFTLDTYIVLDADGGSIGNNPARIQEIRQGLVEALRNPADYPTIIQRRVPRQLKHFAFAPQVTIQNDALRPVTILEIIAPDRPGLLARIGKIFLDFDLSLQNAKIATLGERVEDVFFVTDAHNQPLSDPELCARLQLAIAEQLADGDSYIQPSRISI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudomonas mendocina (strain ymp)
Length
899 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.887 kDa
Sequence
MPQMDPELFDRGQFQAELALKSSPIAAFKKAIRHAREVLDARFKGGRDIRRLVEDRAWFVDQILQEAWKRFAWSEDADIALLAVGGYGRGELHPYSDIDLLILLDSSDHEIFREPIEGFLTLLWDIGLEVGQSVRSVDECAEEARADLTVITNLMESRTIAGPEHLRQRMQQVTSSEQMWPSKHFYLAKREERKARHAKYNDTEYNLEPNVKGSPGGLRDIQTVLWVARRQFGTLNLQALVGQGFLLESEYALLSSSQEFLWKVRYALHMLAGRAEDRLLFDYQARIAALFGYQDGDGKRSIEHFMQKYYRVVMGISELSDLINQHFEEVILRAGESGPATPLNSRFQVRDGYIEVTHPNVFKRTPFAILEVFVLMAQNPEIKGVRADSIRLLRDSRHLIDDDFRKDIRNTSLFIELFKCKEGIHRNLRRMNRYGILGRYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKHLRKFRWPELAEKFPLASKLIDRLPKPELIYLAGLYHDIGKGRGGDHSELGAVDAEAFARRHQLPAWDSALIVWLVQHHLVMSTTAQRKDLSDPQVIHDFAQFVGDQTHLDYLYVLTVADINATNPSLWNSWRASLLRQLYTETKRALRRGLENPLDREEQIRQTQSAALDILVRGGTDPDDAEQLWSQLGDDYFLRHTANDVAWHTEAILQHPADSGPLVLIKETTQREFEGGTQIFIYAPDQHDFFAVTVAAMSQLNLNIHDARIITSTSQFTLDTYVVLDADGGSIGDNPARIKQIREGLIEALKNPDEYPTIIQRRVPRQLKHFAFAPQVTIHNDAQRPVTILELTAPDRPGLLARIGRIFLEYDLSLQNAKIATLGERVEDVFFVTDANNQPLSDPELCARLQETIVRRLSEPSAQPQSLQIDI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Psychrobacter sp. (strain PRwf-1)
Length
899 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.339 kDa
Sequence
MFISDPTDSLITPLPDLTAHSEAQSRNLGIPDWLKQIEADIATALEKGVDIRHLVEARAASIDSLLIELFKLHELTQTDLALFAVGGYGRGELSPYSDVDILILSPDTLSAEISQKVDGFVARLWDVGIEPGIAVRTIEDCLQVATDITVATNLLEARLLIGNDSLSAIPNNVVQQTWSQKEFYDAKMAEARARHLLHNGTEYNLEPDIKKSPGGLRDIHTIGWITKRYFRITKLYDLVPQDFLTEKEFDELMFAEGFLWRIRHHLHHLTGRNENKLLFDYQRDIAERMGYEQSEEDEPNAAVENFMRDYYRCAMQISTLSEMLTSHYYETLIEARLPESERPEKSVLNARFNRVGDHIAIAHHHVFAQHPEAILEMFLLMGQHGIKHIRTRTLRALKIAARGIDQHYRDNPLHKKLFLDNLKEQNYLFHRLRIMKRYGVLANYMPQFVNLIGLMQYDLFHRYTVDAHILLLIRMLHRFTSPKYQDDFALVGSIYKRIERKEIIVLAAIFHDIAKGRGGDHSELGERDAIEFCLSHGMSEADAKLIGWLTRYHLLMSMTAQKQDISDPEVVTKFANLVGNVTHLNHLYVLTVADMNATNPQLWNSWRASLMKQLYTQTRRILRADLDAPTNRQEMIATTRQQALTMLDKVDNQHMNREEVLALWDELGDEYFLREIPEAIMWHTEAILNHPPIGRASDANSEPLIVLREHRELALDAVQIFIYTQDQANLFAVTMAVFDQMNLDVLDARIITATRDFALDSYVLLDRHGTLLTDPESREELTRRLIDAFKNPETPKLVQKRLPRRLKNFQVPTTIDFNYNEASRQHVMSLTTLDQPGLLARIGQVFLNEGIEVHAARITTLGERAEDMFYISDIGDNMLSDAKLERLRTTLIDVLTPSC

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
Length
898 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.672 kDa
Sequence
MPQVDPDLFDRGQFQAELALKASPIAAFKKAIRRAKDVLDDRFKSGRDIRRLIEDRAWFVDNILQKAWDQFEWSEDADIALLAVGGYGRGELHPYSDIDLLILLDSDDHEVFREPIERFLTLLWDIGLEVGQSVRSVNECAQEGRADLTVITNLMESRTIAGPEHLRQRMLEVTSTEHMWPSKEFFLAKHAEQKKRHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLHALAGEGFLLGSENALLASSQEFLWKVRYALHMLAGRSEDRLLFDYQVRIAGLLGYEDSDAKLAIERFMQKYYRVVMSIAELSDLIIQHFEEVILSDDSGTAQPINSRFQLHDGYIEATNPNVFKRTPFAMIEIFVLMAQHPEIKGVRADTIRLLREHRHLINDDFRNDIRNTSLFIELFKCETGIHRNLRRMNRYGILGLYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTEVSEKFPLASKIMARLPKPELIYLAGLYHDIGKGRGGDHSELGAIDAQAFGTRHHLPDWDTRLIVWLVSNHLVMSTTAQRKDLSDPQVIHDFAQFVGDEVHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRRTQTAALDILVRNGTDPDDVEQLWSALGDDYFLRHTAGDVAWHSDAILQQPADGGPLVLIKETTQREFEGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARIITSSSKFTLDTYIVLDNEGGSIGDNPERVQEIRNGLTEALRNPDDYPTIIKRRVPRQLKHFAFAPQVTIHNDAQRPVTVLELLAPDRPGLLARIGKIFLEFDLSLQNAKIATLGERVEDVFFITDANNHPLSDPQLCSQLQDAIVKQLSVNSEPGHDLRISI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Length
898 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.738 kDa
Sequence
MPQVDPDLFDRGQFQAELALKASPIAAFKKAIRRARDVLDNRFRSGRDIRRLIEDRAWFVDNILQQAWDQFEWSEDADIALLAVGGYGRGELHPYSDIDLLILLESDDHEVFREPIERFLTLLWDIGLEVGQSVRSVDECAQEGRADLTVITNLMESRTIAGPEHLRQRMLEVTSTQHMWPSKEFFLAKHAEQKKRHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLHALAGEGFLLGSENALLASSQEFLWKVRYALHMLAGRSEDRLLFDYQVRIAGLLGYEDNDAKLAIERFMQKYYRVVMSIAELSDLIIQHFEEVILSDDDGTPQPINSRFQLHDGYIEATNPNVFRRTPFAMLEIFVLMAQHPEIKGVRADTIRLLREHRHLINDDFRNDIRNTSLFIELFKCEIGIHRNLRRMNRYGILGLYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTEVSEKFPLASKIMARLPKPELIYLAGLYHDIGKGRGGDHSELGAVDAQAFGTRHHLPAWDNRLIVWLVSNHLVMSTTAQRKDLSDPQVIHDFAQFVGDEVHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRRTQTAALDILVRSGTDPDDVEQLWSALGDDYFLRHTAGDVAWHSDAILQQPADGGPLVLIKETTQREFEGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARIITSSSQFTLDTYIVLDHEGGSIGNNPERIQDIRDGLTEALRNPDDYPTIIKRRVPRQLKHFAFAPQVTIHNDAQRPVTVLELLAPDRPGLLARIGKIFLEFDLSLQNAKIATLGERVEDVFFITDANNQPLSDPQLCSQLQEAIVKQLSVNSEPGGDLRISI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudomonas syringae pv. syringae (strain B728a)
Length
898 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.87 kDa
Sequence
MPQVDPDLFDRGQFQAELALKASPIAAFKKAIRRARDVLDERFRSGRDIRRLIEDRAWFVDNILQKAWDQFEWSEDADIALLAVGGYGRGELHPYSDIDLLILLDSDDHEVFREPIERFLTLLWDIGLEVGQSVRSVNECAQEGRADLTVITNLMESRTIAGPEHLRQRMLEVTSTEHMWPSKEFFLAKHAEQKKRHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLHALAGEGFLLGSENALLASSQEFLWKVRYALHMLAGRSEDRLLFDYQVRIAGLLGYEDNDAKLAIERFMQKYYRVVMSIAELSDLIIQHFEEVILSDDSGTPQPINSRFQLHDGYIEATHQNVFKRTPFAMIEIFVLMAQHPEIKGVRADTIRLLREHRHLINDEFRNDIRNTSLFIELFKCEIGIHRNLRRMNRYGILGLYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTEVSEKFPLASKIMGRLPKPELIYLAGLYHDIGKGRGGDHSELGAIDAQAFGARHHLPAWDTRLIVWLVSNHLVMSTTAQRKDLSDPQVIHDFAQFVGDEVHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRRTQTAALDILVRNGTDPDDVEQLWSALGDDYFLRHTAGDVAWHSDAILQQPADGGPLVLIKETTQREFEGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARIITSSSKFTLDTYIVLDHEGGSIGNNPERIQDIREGLTEALRNPDDYPTIIKRRVPRQLKHFAFAPQVTIHNDAQRPVTVLELLAPDRPGLLARIGKIFLEFDLSLQNAKIATLGERVEDVFFITDANNHPLSDPQLCRQLQDAIVKQLSVNSEPGNDLRISI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Sodalis glossinidius (strain morsitans)
Length
896 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.328 kDa
Sequence
MQGDPMPDQILQFTHPPVPRQPPVKPSSPLTWPDDALNRPFLKERLDEFQRWLADAFDAGETAEILVDARTLYIDQLLRQLWHYHGLAHAPHTALVAVGGYGRGELHPLSDIDVLVLSQAPLTPPQQQHISELLTLLWDLKLEVGHSVRSIAECLEEGRADLTVATNLIESRLICGDLALFLTLQKQVFSDDFWPSRAFFPAKLAEQQERHSRYHGTSYNLEPDIKSSPGGLRDIHTLLWVAHRHFGATSMDEMVGFGFITRAERDELNECQSFLWRTRFALHLVLNRYDNRLLFDRQQNVAQLLRYQGEGNLPVERMMKDFFRVTRRVSELNQMLLQLFDEAILALAPDEKPQPLDDEFQLRGNLIDLRDETLFSRQPEAILLLFWQMVRNRHIEGIYSATLRQLRYARRHLKAPLCTSPEARTLFMRILHQPGAVKHALLPMHRHSVLWAYMPQWSNIVGQMQFDLFHAYTVDEHTIRVLLKLESFADESQRPYHPLCVELFPRLSQRHLLLVAALFHDIAKGRGGDHSQLGARDVLEFAALHDLPAEDAQLVAWLVESHLVMSVTAQRRDIQEPDVLVQFAGEMQSESRLHYLLCLTVADICATNETLWNSWKQSLLRELFFATEKQLRRGIHVSPDVRERVRHNRRQSLVLLRMEGIDEQRLQEIWSRCRADYFLRHTPNQLAWHARHMVLHDHDEPLVLISPQATRGGTEIFIHNQDRPYLFAAVTGELDRRNLSVHDAQIFTNRDGMAMDTFVVLEPDGSPLSPDRHPVIRQALLQILLPGDYRHPRVRRPSSKLRHFNVDTSVVFLPSPTERRSYLELTALDQPGLLARVSEVFVDLGISLHGARISTIGERVEDLFILADGDRRALSRAMQAEVRRRLTEALNPNDKV

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Sodalis glossinidius (strain morsitans)
Length
896 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.328 kDa
Sequence
MQGDPMPDQILQFTHPPVPRQPPVKPSSPLTWPDDALNRPFLKERLDEFQRWLADAFDAGETAEILVDARTLYIDQLLRQLWHYHGLAHAPHTALVAVGGYGRGELHPLSDIDVLVLSQAPLTPPQQQHISELLTLLWDLKLEVGHSVRSIAECLEEGRADLTVATNLIESRLICGDLALFLTLQKQVFSDDFWPSRAFFPAKLAEQQERHSRYHGTSYNLEPDIKSSPGGLRDIHTLLWVAHRHFGATSMDEMVGFGFITRAERDELNECQSFLWRTRFALHLVLNRYDNRLLFDRQQNVAQLLRYQGEGNLPVERMMKDFFRVTRRVSELNQMLLQLFDEAILALAPDEKPQPLDDEFQLRGNLIDLRDETLFSRQPEAILLLFWQMVRNRHIEGIYSATLRQLRYARRHLKAPLCTSPEARTLFMRILHQPGAVKHALLPMHRHSVLWAYMPQWSNIVGQMQFDLFHAYTVDEHTIRVLLKLESFADESQRPYHPLCVELFPRLSQRHLLLVAALFHDIAKGRGGDHSQLGARDVLEFAALHDLPAEDAQLVAWLVESHLVMSVTAQRRDIQEPDVLVQFAGEMQSESRLHYLLCLTVADICATNETLWNSWKQSLLRELFFATEKQLRRGIHVSPDVRERVRHNRRQSLVLLRMEGIDEQRLQEIWSRCRADYFLRHTPNQLAWHARHMVLHDHDEPLVLISPQATRGGTEIFIHNQDRPYLFAAVTGELDRRNLSVHDAQIFTNRDGMAMDTFVVLEPDGSPLSPDRHPVIRQALLQILLPGDYRHPRVRRPSSKLRHFNVDTSVVFLPSPTERRSYLELTALDQPGLLARVSEVFVDLGISLHGARISTIGERVEDLFILADGDRRALSRAMQAEVRRRLTEALNPNDKV

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Yersinia pseudotuberculosis serotype O:1b (strain IP 31758)
Length
893 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.158 kDa
Sequence
MSDNHTEHSLSLTLTPTISEQPALPSTYLDSDIHCPILKQRLDAFQRWQAEAFNSGTSAEVLIAARSDYIDHLLQRLWTFYGFDKVPETALVAVGGYGRGELHPLSDIDVLVLSKQRLNDEQAQRVGQLITLLWDLKLEVGHSVRTLEECLLEGLADLTIATNMIESRLICGDVALFLQMQKHIFSDSFWPSPQFFHAKVVEQQERHKRYHGTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSLSEMVDFGFLTNAERNELNESQSFLWRIRFALHLVLTRYDNRLLFDRQLSVAQLLRYEGEGNEPVEHMMKDFYRMTRRVSELNNMLLQLFDEAILALDANEKPRPLDEEFQLRGDLIDLRDENLFVRQPEAIMRMFYLMVRNQDIKGIYSTTVRRLRHARRHLKAPLCHIPEARKLFMAILRHPGAVSRALLPMHRHSVLWAYMPQWGSIVGQMQFDLFHAYTVDEHTIRVLLKIESFADEDTRPRHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSILGAHDAVEFAEQHGLNSRESQLVAWLVRCHLLMSVTAQRRDIQDPAVIQQFSAEVQSETRLRYLVSLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNSPDLRERVRHHRLQALALLRMDNIDEEALHRIWSRCRADYFLRHSPNQLAWHARHLLEHDSTKPLVLVSRQATRGGTEIFIWSPDRPSLFAAVVGELDRRNLSVHDAQIFTNRDGMAMDTFIVLEPDGSPLAQDRHPIISHALQQAINRSDYQHPPRVRRLSPKLRHFSVPTEANFLPTHNERRTYLELIALDQPGLLARVGKIFADLGLSLHSARITTIGERVEDLFVLADKDRRALSLETRRELAQRLADTLNPNDKL

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Yersinia pestis bv. Antiqua (strain Antiqua)
Length
893 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.158 kDa
Sequence
MSDNHTEHSLSLTLTPTISEQPALPSTYLDSDIHCPILKQRLDAFQRWQAEAFNSGTSAEVLIAARSDYIDHLLQRLWTFYGFDKVPETALVAVGGYGRGELHPLSDIDVLVLSKQRLNDEQAQRVGQLITLLWDLKLEVGHSVRTLEECLLEGLADLTIATNMIESRLICGDVALFLQMQKHIFSDSFWPSPQFFHAKVVEQQERHKRYHGTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSLSEMVDFGFLTNAERNELNESQSFLWRIRFALHLVLTRYDNRLLFDRQLSVAQLLRYEGEGNEPVEHMMKDFYRMTRRVSELNNMLLQLFDEAILALDANEKPRPLDEEFQLRGDLIDLRDENLFVRQPEAIMRMFYLMVRNQDIKGIYSTTVRRLRHARRHLKAPLCHIPEARKLFMAILRHPGAVSRALLPMHRHSVLWAYMPQWGSIVGQMQFDLFHAYTVDEHTIRVLLKIESFADEDTRPRHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSILGAHDAVEFAEQHGLNSRESQLVAWLVRCHLLMSVTAQRRDIQDPAVIQQFSAEVQSETRLRYLVSLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNSPDLRERVRHHRLQALALLRMDNIDEEALHRIWSRCRADYFLRHSPNQLAWHARHLLEHDSTKPLVLVSRQATRGGTEIFIWSPDRPSLFAAVVGELDRRNLSVHDAQIFTNRDGMAMDTFIVLEPDGSPLAQDRHPIISHALQQAINRSDYQHPPRVRRLSPKLRHFSVPTEANFLPTHNERRTYLELIALDQPGLLARVGKIFADLGLSLHSARITTIGERVEDLFVLADKDRRALSLETRRELAQRLADTLNPNDKL

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Yersinia pestis
Length
893 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.158 kDa
Sequence
MSDNHTEHSLSLTLTPTISEQPALPSTYLDSDIHCPILKQRLDAFQRWQAEAFNSGTSAEVLIAARSDYIDHLLQRLWTFYGFDKVPETALVAVGGYGRGELHPLSDIDVLVLSKQRLNDEQAQRVGQLITLLWDLKLEVGHSVRTLEECLLEGLADLTIATNMIESRLICGDVALFLQMQKHIFSDSFWPSPQFFHAKVVEQQERHKRYHGTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSLSEMVDFGFLTNAERNELNESQSFLWRIRFALHLVLTRYDNRLLFDRQLSVAQLLRYEGEGNEPVEHMMKDFYRMTRRVSELNNMLLQLFDEAILALDANEKPRPLDEEFQLRGDLIDLRDENLFVRQPEAIMRMFYLMVRNQDIKGIYSTTVRRLRHARRHLKAPLCHIPEARKLFMAILRHPGAVSRALLPMHRHSVLWAYMPQWGSIVGQMQFDLFHAYTVDEHTIRVLLKIESFADEDTRPRHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSILGAHDAVEFAEQHGLNSRESQLVAWLVRCHLLMSVTAQRRDIQDPAVIQQFSAEVQSETRLRYLVSLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNSPDLRERVRHHRLQALALLRMDNIDEEALHRIWSRCRADYFLRHSPNQLAWHARHLLEHDSTKPLVLVSRQATRGGTEIFIWSPDRPSLFAAVVGELDRRNLSVHDAQIFTNRDGMAMDTFIVLEPDGSPLAQDRHPIISHALQQAINRSDYQHPPRVRRLSPKLRHFSVPTEANFLPTHNERRTYLELIALDQPGLLARVGKIFADLGLSLHSARITTIGERVEDLFVLADKDRRALSLETRRELAQRLADTLNPNDKL

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Yersinia pestis bv. Antiqua (strain Angola)
Length
893 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.158 kDa
Sequence
MSDNHTEHSLSLTLTPTISEQPALPSTYLDSDIHCPILKQRLDAFQRWQAEAFNSGTSAEVLIAARSDYIDHLLQRLWTFYGFDKVPETALVAVGGYGRGELHPLSDIDVLVLSKQRLNDEQAQRVGQLITLLWDLKLEVGHSVRTLEECLLEGLADLTIATNMIESRLICGDVALFLQMQKHIFSDSFWPSPQFFHAKVVEQQERHKRYHGTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSLSEMVDFGFLTNAERNELNESQSFLWRIRFALHLVLTRYDNRLLFDRQLSVAQLLRYEGEGNEPVEHMMKDFYRMTRRVSELNNMLLQLFDEAILALDANEKPRPLDEEFQLRGDLIDLRDENLFVRQPEAIMRMFYLMVRNQDIKGIYSTTVRRLRHARRHLKAPLCHIPEARKLFMAILRHPGAVSRALLPMHRHSVLWAYMPQWGSIVGQMQFDLFHAYTVDEHTIRVLLKIESFADEDTRPRHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSILGAHDAVEFAEQHGLNSRESQLVAWLVRCHLLMSVTAQRRDIQDPAVIQQFSAEVQSETRLRYLVSLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNSPDLRERVRHHRLQALALLRMDNIDEEALHRIWSRCRADYFLRHSPNQLAWHARHLLEHDSTKPLVLVSRQATRGGTEIFIWSPDRPSLFAAVVGELDRRNLSVHDAQIFTNRDGMAMDTFIVLEPDGSPLAQDRHPIISHALQQAINRSDYQHPPRVRRLSPKLRHFSVPTEANFLPTHNERRTYLELIALDQPGLLARVGKIFADLGLSLHSARITTIGERVEDLFVLADKDRRALSLETRRELAQRLADTLNPNDKL

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Yersinia pestis bv. Antiqua (strain Nepal516)
Length
893 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.158 kDa
Sequence
MSDNHTEHSLSLTLTPTISEQPALPSTYLDSDIHCPILKQRLDAFQRWQAEAFNSGTSAEVLIAARSDYIDHLLQRLWTFYGFDKVPETALVAVGGYGRGELHPLSDIDVLVLSKQRLNDEQAQRVGQLITLLWDLKLEVGHSVRTLEECLLEGLADLTIATNMIESRLICGDVALFLQMQKHIFSDSFWPSPQFFHAKVVEQQERHKRYHGTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSLSEMVDFGFLTNAERNELNESQSFLWRIRFALHLVLTRYDNRLLFDRQLSVAQLLRYEGEGNEPVEHMMKDFYRMTRRVSELNNMLLQLFDEAILALDANEKPRPLDEEFQLRGDLIDLRDENLFVRQPEAIMRMFYLMVRNQDIKGIYSTTVRRLRHARRHLKAPLCHIPEARKLFMAILRHPGAVSRALLPMHRHSVLWAYMPQWGSIVGQMQFDLFHAYTVDEHTIRVLLKIESFADEDTRPRHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSILGAHDAVEFAEQHGLNSRESQLVAWLVRCHLLMSVTAQRRDIQDPAVIQQFSAEVQSETRLRYLVSLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNSPDLRERVRHHRLQALALLRMDNIDEEALHRIWSRCRADYFLRHSPNQLAWHARHLLEHDSTKPLVLVSRQATRGGTEIFIWSPDRPSLFAAVVGELDRRNLSVHDAQIFTNRDGMAMDTFIVLEPDGSPLAQDRHPIISHALQQAINRSDYQHPPRVRRLSPKLRHFSVPTEANFLPTHNERRTYLELIALDQPGLLARVGKIFADLGLSLHSARITTIGERVEDLFVLADKDRRALSLETRRELAQRLADTLNPNDKL

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Yersinia pestis (strain Pestoides F)
Length
893 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.158 kDa
Sequence
MSDNHTEHSLSLTLTPTISEQPALPSTYLDSDIHCPILKQRLDAFQRWQAEAFNSGTSAEVLIAARSDYIDHLLQRLWTFYGFDKVPETALVAVGGYGRGELHPLSDIDVLVLSKQRLNDEQAQRVGQLITLLWDLKLEVGHSVRTLEECLLEGLADLTIATNMIESRLICGDVALFLQMQKHIFSDSFWPSPQFFHAKVVEQQERHKRYHGTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSLSEMVDFGFLTNAERNELNESQSFLWRIRFALHLVLTRYDNRLLFDRQLSVAQLLRYEGEGNEPVEHMMKDFYRMTRRVSELNNMLLQLFDEAILALDANEKPRPLDEEFQLRGDLIDLRDENLFVRQPEAIMRMFYLMVRNQDIKGIYSTTVRRLRHARRHLKAPLCHIPEARKLFMAILRHPGAVSRALLPMHRHSVLWAYMPQWGSIVGQMQFDLFHAYTVDEHTIRVLLKIESFADEDTRPRHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSILGAHDAVEFAEQHGLNSRESQLVAWLVRCHLLMSVTAQRRDIQDPAVIQQFSAEVQSETRLRYLVSLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNSPDLRERVRHHRLQALALLRMDNIDEEALHRIWSRCRADYFLRHSPNQLAWHARHLLEHDSTKPLVLVSRQATRGGTEIFIWSPDRPSLFAAVVGELDRRNLSVHDAQIFTNRDGMAMDTFIVLEPDGSPLAQDRHPIISHALQQAINRSDYQHPPRVRRLSPKLRHFSVPTEANFLPTHNERRTYLELIALDQPGLLARVGKIFADLGLSLHSARITTIGERVEDLFVLADKDRRALSLETRRELAQRLADTLNPNDKL

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Yersinia pseudotuberculosis serotype I (strain IP32953)
Length
893 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.172 kDa
Sequence
MSDNHTEHSLSLTLTPTISEQPVLPSTYLDSDINCPILKQRLDAFQRWQAEAFNSGTSAEVLIAARSDYIDHLLQRLWTFYGFDNVPETALVAVGGYGRGELHPLSDIDVLVLSKQRLNDEHAQRVGQLITLLWDLKLEVGHSVRTLEECLLEGLADLTIATNMIESRLICGDVALFLQMQKHIFSDSFWPSPQFFHAKVVEQQERHKRYHGTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSLSEMVDFGFLTNAERNELNESQSFLWRIRFALHLVLTRYDNRLLFDRQLSVAQLLRYEGEGNEPVEHMMKDFYRMTRRVSELNNMLLQLFDEAILALEANEKPRPLDEEFQLRGDLIDLRDENLFVRQPEAIMRMFYLMVRNQDIKGIYSTTVRRLRHARRHLKAPLCHIPEARKLFMAILRHPGAVSRALLPMHRHSVLWAYMPQWGSIVGQMQFDLFHAYTVDEHTIRVLLKIESFADEDTRPRHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSILGAHDAVEFAEQHGLNSRESQLVAWLVRCHLLMSVTAQRRDIQDPAVIQQFSAEVQSETRLRYLVSLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNSPDLRERVRHHRLQALALLRMDNIDEEALHRIWSRCRADYFLRHSPNQLAWHARHLLEHDSTKPLVLVSRQATRGGTEIFIWSPDRPSLFAAVVGELDRRNLSVHDAQIFTNRDGMAMDTFIVLEPDGSPLAQDRHPIISHALQQAINRSDYQHPPRVRRLSPKLRHFSVPTEANFLPTHNERRTYLELIALDQPGLLARVGKIFADLGLSLHSARITTIGERVEDLFVLADKDRRALSLETRRELAQRLADTLNPNDKL

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Yersinia pseudotuberculosis serotype O:1b (strain IP 31758)
Length
893 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.158 kDa
Sequence
MSDNHTEHSLSLTLTPTISEQPALPSTYLDSDIHCPILKQRLDAFQRWQAEAFNSGTSAEVLIAARSDYIDHLLQRLWTFYGFDKVPETALVAVGGYGRGELHPLSDIDVLVLSKQRLNDEQAQRVGQLITLLWDLKLEVGHSVRTLEECLLEGLADLTIATNMIESRLICGDVALFLQMQKHIFSDSFWPSPQFFHAKVVEQQERHKRYHGTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSLSEMVDFGFLTNAERNELNESQSFLWRIRFALHLVLTRYDNRLLFDRQLSVAQLLRYEGEGNEPVEHMMKDFYRMTRRVSELNNMLLQLFDEAILALDANEKPRPLDEEFQLRGDLIDLRDENLFVRQPEAIMRMFYLMVRNQDIKGIYSTTVRRLRHARRHLKAPLCHIPEARKLFMAILRHPGAVSRALLPMHRHSVLWAYMPQWGSIVGQMQFDLFHAYTVDEHTIRVLLKIESFADEDTRPRHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSILGAHDAVEFAEQHGLNSRESQLVAWLVRCHLLMSVTAQRRDIQDPAVIQQFSAEVQSETRLRYLVSLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNSPDLRERVRHHRLQALALLRMDNIDEEALHRIWSRCRADYFLRHSPNQLAWHARHLLEHDSTKPLVLVSRQATRGGTEIFIWSPDRPSLFAAVVGELDRRNLSVHDAQIFTNRDGMAMDTFIVLEPDGSPLAQDRHPIISHALQQAINRSDYQHPPRVRRLSPKLRHFSVPTEANFLPTHNERRTYLELIALDQPGLLARVGKIFADLGLSLHSARITTIGERVEDLFVLADKDRRALSLETRRELAQRLADTLNPNDKL

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Yersinia pestis bv. Antiqua (strain Antiqua)
Length
893 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.158 kDa
Sequence
MSDNHTEHSLSLTLTPTISEQPALPSTYLDSDIHCPILKQRLDAFQRWQAEAFNSGTSAEVLIAARSDYIDHLLQRLWTFYGFDKVPETALVAVGGYGRGELHPLSDIDVLVLSKQRLNDEQAQRVGQLITLLWDLKLEVGHSVRTLEECLLEGLADLTIATNMIESRLICGDVALFLQMQKHIFSDSFWPSPQFFHAKVVEQQERHKRYHGTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSLSEMVDFGFLTNAERNELNESQSFLWRIRFALHLVLTRYDNRLLFDRQLSVAQLLRYEGEGNEPVEHMMKDFYRMTRRVSELNNMLLQLFDEAILALDANEKPRPLDEEFQLRGDLIDLRDENLFVRQPEAIMRMFYLMVRNQDIKGIYSTTVRRLRHARRHLKAPLCHIPEARKLFMAILRHPGAVSRALLPMHRHSVLWAYMPQWGSIVGQMQFDLFHAYTVDEHTIRVLLKIESFADEDTRPRHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSILGAHDAVEFAEQHGLNSRESQLVAWLVRCHLLMSVTAQRRDIQDPAVIQQFSAEVQSETRLRYLVSLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNSPDLRERVRHHRLQALALLRMDNIDEEALHRIWSRCRADYFLRHSPNQLAWHARHLLEHDSTKPLVLVSRQATRGGTEIFIWSPDRPSLFAAVVGELDRRNLSVHDAQIFTNRDGMAMDTFIVLEPDGSPLAQDRHPIISHALQQAINRSDYQHPPRVRRLSPKLRHFSVPTEANFLPTHNERRTYLELIALDQPGLLARVGKIFADLGLSLHSARITTIGERVEDLFVLADKDRRALSLETRRELAQRLADTLNPNDKL

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Yersinia pestis
Length
893 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.158 kDa
Sequence
MSDNHTEHSLSLTLTPTISEQPALPSTYLDSDIHCPILKQRLDAFQRWQAEAFNSGTSAEVLIAARSDYIDHLLQRLWTFYGFDKVPETALVAVGGYGRGELHPLSDIDVLVLSKQRLNDEQAQRVGQLITLLWDLKLEVGHSVRTLEECLLEGLADLTIATNMIESRLICGDVALFLQMQKHIFSDSFWPSPQFFHAKVVEQQERHKRYHGTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSLSEMVDFGFLTNAERNELNESQSFLWRIRFALHLVLTRYDNRLLFDRQLSVAQLLRYEGEGNEPVEHMMKDFYRMTRRVSELNNMLLQLFDEAILALDANEKPRPLDEEFQLRGDLIDLRDENLFVRQPEAIMRMFYLMVRNQDIKGIYSTTVRRLRHARRHLKAPLCHIPEARKLFMAILRHPGAVSRALLPMHRHSVLWAYMPQWGSIVGQMQFDLFHAYTVDEHTIRVLLKIESFADEDTRPRHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSILGAHDAVEFAEQHGLNSRESQLVAWLVRCHLLMSVTAQRRDIQDPAVIQQFSAEVQSETRLRYLVSLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNSPDLRERVRHHRLQALALLRMDNIDEEALHRIWSRCRADYFLRHSPNQLAWHARHLLEHDSTKPLVLVSRQATRGGTEIFIWSPDRPSLFAAVVGELDRRNLSVHDAQIFTNRDGMAMDTFIVLEPDGSPLAQDRHPIISHALQQAINRSDYQHPPRVRRLSPKLRHFSVPTEANFLPTHNERRTYLELIALDQPGLLARVGKIFADLGLSLHSARITTIGERVEDLFVLADKDRRALSLETRRELAQRLADTLNPNDKL

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Yersinia pestis bv. Antiqua (strain Angola)
Length
893 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.158 kDa
Sequence
MSDNHTEHSLSLTLTPTISEQPALPSTYLDSDIHCPILKQRLDAFQRWQAEAFNSGTSAEVLIAARSDYIDHLLQRLWTFYGFDKVPETALVAVGGYGRGELHPLSDIDVLVLSKQRLNDEQAQRVGQLITLLWDLKLEVGHSVRTLEECLLEGLADLTIATNMIESRLICGDVALFLQMQKHIFSDSFWPSPQFFHAKVVEQQERHKRYHGTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSLSEMVDFGFLTNAERNELNESQSFLWRIRFALHLVLTRYDNRLLFDRQLSVAQLLRYEGEGNEPVEHMMKDFYRMTRRVSELNNMLLQLFDEAILALDANEKPRPLDEEFQLRGDLIDLRDENLFVRQPEAIMRMFYLMVRNQDIKGIYSTTVRRLRHARRHLKAPLCHIPEARKLFMAILRHPGAVSRALLPMHRHSVLWAYMPQWGSIVGQMQFDLFHAYTVDEHTIRVLLKIESFADEDTRPRHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSILGAHDAVEFAEQHGLNSRESQLVAWLVRCHLLMSVTAQRRDIQDPAVIQQFSAEVQSETRLRYLVSLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNSPDLRERVRHHRLQALALLRMDNIDEEALHRIWSRCRADYFLRHSPNQLAWHARHLLEHDSTKPLVLVSRQATRGGTEIFIWSPDRPSLFAAVVGELDRRNLSVHDAQIFTNRDGMAMDTFIVLEPDGSPLAQDRHPIISHALQQAINRSDYQHPPRVRRLSPKLRHFSVPTEANFLPTHNERRTYLELIALDQPGLLARVGKIFADLGLSLHSARITTIGERVEDLFVLADKDRRALSLETRRELAQRLADTLNPNDKL

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Yersinia pestis bv. Antiqua (strain Nepal516)
Length
893 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.158 kDa
Sequence
MSDNHTEHSLSLTLTPTISEQPALPSTYLDSDIHCPILKQRLDAFQRWQAEAFNSGTSAEVLIAARSDYIDHLLQRLWTFYGFDKVPETALVAVGGYGRGELHPLSDIDVLVLSKQRLNDEQAQRVGQLITLLWDLKLEVGHSVRTLEECLLEGLADLTIATNMIESRLICGDVALFLQMQKHIFSDSFWPSPQFFHAKVVEQQERHKRYHGTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSLSEMVDFGFLTNAERNELNESQSFLWRIRFALHLVLTRYDNRLLFDRQLSVAQLLRYEGEGNEPVEHMMKDFYRMTRRVSELNNMLLQLFDEAILALDANEKPRPLDEEFQLRGDLIDLRDENLFVRQPEAIMRMFYLMVRNQDIKGIYSTTVRRLRHARRHLKAPLCHIPEARKLFMAILRHPGAVSRALLPMHRHSVLWAYMPQWGSIVGQMQFDLFHAYTVDEHTIRVLLKIESFADEDTRPRHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSILGAHDAVEFAEQHGLNSRESQLVAWLVRCHLLMSVTAQRRDIQDPAVIQQFSAEVQSETRLRYLVSLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNSPDLRERVRHHRLQALALLRMDNIDEEALHRIWSRCRADYFLRHSPNQLAWHARHLLEHDSTKPLVLVSRQATRGGTEIFIWSPDRPSLFAAVVGELDRRNLSVHDAQIFTNRDGMAMDTFIVLEPDGSPLAQDRHPIISHALQQAINRSDYQHPPRVRRLSPKLRHFSVPTEANFLPTHNERRTYLELIALDQPGLLARVGKIFADLGLSLHSARITTIGERVEDLFVLADKDRRALSLETRRELAQRLADTLNPNDKL

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Yersinia pestis (strain Pestoides F)
Length
893 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.158 kDa
Sequence
MSDNHTEHSLSLTLTPTISEQPALPSTYLDSDIHCPILKQRLDAFQRWQAEAFNSGTSAEVLIAARSDYIDHLLQRLWTFYGFDKVPETALVAVGGYGRGELHPLSDIDVLVLSKQRLNDEQAQRVGQLITLLWDLKLEVGHSVRTLEECLLEGLADLTIATNMIESRLICGDVALFLQMQKHIFSDSFWPSPQFFHAKVVEQQERHKRYHGTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSLSEMVDFGFLTNAERNELNESQSFLWRIRFALHLVLTRYDNRLLFDRQLSVAQLLRYEGEGNEPVEHMMKDFYRMTRRVSELNNMLLQLFDEAILALDANEKPRPLDEEFQLRGDLIDLRDENLFVRQPEAIMRMFYLMVRNQDIKGIYSTTVRRLRHARRHLKAPLCHIPEARKLFMAILRHPGAVSRALLPMHRHSVLWAYMPQWGSIVGQMQFDLFHAYTVDEHTIRVLLKIESFADEDTRPRHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSILGAHDAVEFAEQHGLNSRESQLVAWLVRCHLLMSVTAQRRDIQDPAVIQQFSAEVQSETRLRYLVSLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNSPDLRERVRHHRLQALALLRMDNIDEEALHRIWSRCRADYFLRHSPNQLAWHARHLLEHDSTKPLVLVSRQATRGGTEIFIWSPDRPSLFAAVVGELDRRNLSVHDAQIFTNRDGMAMDTFIVLEPDGSPLAQDRHPIISHALQQAINRSDYQHPPRVRRLSPKLRHFSVPTEANFLPTHNERRTYLELIALDQPGLLARVGKIFADLGLSLHSARITTIGERVEDLFVLADKDRRALSLETRRELAQRLADTLNPNDKL

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Yersinia pseudotuberculosis serotype I (strain IP32953)
Length
893 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.172 kDa
Sequence
MSDNHTEHSLSLTLTPTISEQPVLPSTYLDSDINCPILKQRLDAFQRWQAEAFNSGTSAEVLIAARSDYIDHLLQRLWTFYGFDNVPETALVAVGGYGRGELHPLSDIDVLVLSKQRLNDEHAQRVGQLITLLWDLKLEVGHSVRTLEECLLEGLADLTIATNMIESRLICGDVALFLQMQKHIFSDSFWPSPQFFHAKVVEQQERHKRYHGTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSLSEMVDFGFLTNAERNELNESQSFLWRIRFALHLVLTRYDNRLLFDRQLSVAQLLRYEGEGNEPVEHMMKDFYRMTRRVSELNNMLLQLFDEAILALEANEKPRPLDEEFQLRGDLIDLRDENLFVRQPEAIMRMFYLMVRNQDIKGIYSTTVRRLRHARRHLKAPLCHIPEARKLFMAILRHPGAVSRALLPMHRHSVLWAYMPQWGSIVGQMQFDLFHAYTVDEHTIRVLLKIESFADEDTRPRHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSILGAHDAVEFAEQHGLNSRESQLVAWLVRCHLLMSVTAQRRDIQDPAVIQQFSAEVQSETRLRYLVSLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNSPDLRERVRHHRLQALALLRMDNIDEEALHRIWSRCRADYFLRHSPNQLAWHARHLLEHDSTKPLVLVSRQATRGGTEIFIWSPDRPSLFAAVVGELDRRNLSVHDAQIFTNRDGMAMDTFIVLEPDGSPLAQDRHPIISHALQQAINRSDYQHPPRVRRLSPKLRHFSVPTEANFLPTHNERRTYLELIALDQPGLLARVGKIFADLGLSLHSARITTIGERVEDLFVLADKDRRALSLETRRELAQRLADTLNPNDKL

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
Length
892 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.044 kDa
Sequence
MSDNHTEHSVLPAVTKVIPEQPASPATYLDSELNCPELKQRLETFQSWLADAFNGGISAETLIAARSDYIDRLLGRLWTFYGFDDVPETALVAVGGYGRGELHPLSDIDVLILSKQRLNDEHAQRVGQLITLLWDLKLEVGHSVRTLEECLLEGLADLTVATNMVESRLICGDVALFLQMQKHIFSDNFWPSPKFFHAKVVEQQERHKRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLSEMVDFGFLTKAERNELIESQSFLWRIRFALHLVLTRYDNRLLFDRQLSVAQLLQYQGEGNEPVERMMKDFYRMTRRVSELNNMLLQLFDEAILALDTNEKPRPLDDEFQLRGDLIDLRDENLFVDKPEAIMRMFYLMVRNQDIKGIYSTTVRRLRHARRHLKQPLCNIPEARKLFMAILRHPGAVSRALLPMHRHSVLWAYMPQWGSIVGQMQFDLFHAYTVDEHTIRVLLKLESFADESTRPRHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSILGAHDVLEFAEQHGLNSREAQLVAWLVRCHLLMSVTAQRRDIQDPAVIQQFSAEVQSETRLRYLVSLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNSPDLRERVRHHRLQALALLRMDNIDEEALHHIWSRCRADYFLRHSPNQLAWHARHLLEHDSTKPLVLVSRQATRGGTEIFIWCPDRPSLFAAVVGELDRRNLSVHDAQIFTNRDGMAMDTFIVLEPDGSPLAQDRHPIIIHALQQAMTRQNYQHPRVRRLSPKLRHFSVPTETNFLPTHNERRTYLELIALDQPGLLARVGDIFADLGLSLHSARITTIGERVEDLFVLADKDRRALSIETRRELAQRLTDTLNPNDKL

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
Length
892 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.044 kDa
Sequence
MSDNHTEHSVLPAVTKVIPEQPASPATYLDSELNCPELKQRLETFQSWLADAFNGGISAETLIAARSDYIDRLLGRLWTFYGFDDVPETALVAVGGYGRGELHPLSDIDVLILSKQRLNDEHAQRVGQLITLLWDLKLEVGHSVRTLEECLLEGLADLTVATNMVESRLICGDVALFLQMQKHIFSDNFWPSPKFFHAKVVEQQERHKRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLSEMVDFGFLTKAERNELIESQSFLWRIRFALHLVLTRYDNRLLFDRQLSVAQLLQYQGEGNEPVERMMKDFYRMTRRVSELNNMLLQLFDEAILALDTNEKPRPLDDEFQLRGDLIDLRDENLFVDKPEAIMRMFYLMVRNQDIKGIYSTTVRRLRHARRHLKQPLCNIPEARKLFMAILRHPGAVSRALLPMHRHSVLWAYMPQWGSIVGQMQFDLFHAYTVDEHTIRVLLKLESFADESTRPRHPLCVELYPRLPQPELLLLAALFHDIAKGRGGDHSILGAHDVLEFAEQHGLNSREAQLVAWLVRCHLLMSVTAQRRDIQDPAVIQQFSAEVQSETRLRYLVSLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNSPDLRERVRHHRLQALALLRMDNIDEEALHHIWSRCRADYFLRHSPNQLAWHARHLLEHDSTKPLVLVSRQATRGGTEIFIWCPDRPSLFAAVVGELDRRNLSVHDAQIFTNRDGMAMDTFIVLEPDGSPLAQDRHPIIIHALQQAMTRQNYQHPRVRRLSPKLRHFSVPTETNFLPTHNERRTYLELIALDQPGLLARVGDIFADLGLSLHSARITTIGERVEDLFVLADKDRRALSIETRRELAQRLTDTLNPNDKL

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Serratia proteamaculans (strain 568)
Length
892 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.2 kDa
Sequence
MSENFRQQDTSVISPQAVPVQPEYPNAYGDEEINCIALKQRLEQFQLWLAAAFNAGSSAESLVAARSDFIDRLLRRLWVFYGFEDIPETALVAVGGYGRGELHPLSDIDVLVLSQRRLNEQQSQRVGEFITLLWDLKLEVGHSVRTLEECLLEGLADLTVATNLIESRMICGDVALFLQMQKHIFSDGFWPSPQFFHAKVVEQQERHQRYHGTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSLDEMVGFGFLTQAERNELNECQSFLWRIRFALHLVLPRYDNRLLFDRQLNVAQLLRYEGEGNEPVERMMKDFYRMTRRVGELNHMLLQLFDEAILALDATEKPRPLNDDFQLRGDLIDLRDETLFIRQPESIMRMFYLMVRNREIKGIYSTTVRQLRHARRHLKQPLCTIPEARELFMAILRHPGAVSRALVPMHRHSVLWAYMPQWGKIVGQMQFDLFHAYTVDEHTIRVLQKLESFADAETRPRHPLCVELYPRLPNPELLLLAALFHDIAKGRGGDHSILGAQDVLEFAEVHGLNSREAQLVAWLVRCHLLMSVTAQRRDIQDPTVIQQFSAEVQSETRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNSPDLRERVRHHRLQALALLRMDNIDEEALHRIWSRCRADYFLRHSPNQLAWHARHLLAHDSTKPLVLVSRQATRGGTEIFIWSPDRPYLFAAVAGEMDRRNLSVHDAQIFTNRDGMAMDTFIVLEPDGSPLAQDRHTAIRHALLQAITQREYQPPRVRRPSSKLRHFSVPTEVSFLPTHTDRRSYLELTALDQPGLLARVGEVFADLNLSLHGARISTIGERVEDLFILADSDRRALNPETRRKLEQRLTEALNPNDKM

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / NCIMB 11848 / C-107)
Length
892 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.332 kDa
Sequence
MPNFTGNTRPDPTLFEPAAFAKWIDTSEAPLLLLRSFLKEGIENLKQRFLTGTSAAELLPLHAWLVDQILVQACRLHTKKCPERVALVAVGGYGRGTLHPYSDIDILLLLTEETDSILQNSIGHFISFLWDTGLEMGHSVRTVAECQQAARDDLSFITSLMEARLLFGPELLFKNLQTAIAPEQIWNSRQFFLAKQAEQITRHHKYHDTAYNLEPNLKEGPGGLRDIQMIQWVSKRYFNTWSFDSLLQHDFLTVSERKELLESQSFLWQLRYGLHTLTGRREDRLLFDHQIALAKQLGYHDQGPHLAVEQLMKDYYRTAENTGRLNEMLLQLLEERILLVDAKVHVRPINERFQARNGFLEVINPSVFKHTPSALLEVFLLLQQHPEIKGVRASTIRLIREHRHLIDDNFRADSFNRALFMEIMRQSRGITRELRRMNKYGILGAYLPVFGKIVGQMQYDMFHAYTVDEHTLFLIHNLRRFALPKYAQELPLCSEIFQRISKPELLYLAGLFHDIAKGRGGDHSKLGAKDALRFCLYHGLSRDDSRLVAWLVAHHLLMSMTAQRRDINDPKVIQRFAREVGDERRLNHLYLLTAADIRATNPNLWNSWKDALLNKLYTATQQALRQGLEYPVDKKEHIRDIQNEARQALLKDGWTEQKLDILWSQIDADYFLRHTPNEIRWHIKALAQKEPHDGAPRILVRIHNQEPGTMEVFIYARAHALIFTVTTRTMAQLDLDVLDARIITTGHGFVLESFVVREAATIRAEADLEFRLQEIQEVLTQRLTQPDRAPPYRPGFIPRKLKLFKFPTTITFTKDRRNQCTVMELTTNNWPGLLSRVCRALASCQVRLVNAKITTLGTQVVDVFFICNQQDKPLTPEQQQQLKEAIYTYLER

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Cronobacter sakazakii (strain ATCC BAA-894)
Length
892 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.003 kDa
Sequence
MMSNTLPEQSVNTTLAPLPGQPDYPATWPADALNCAQIKQHLDAFQQWLGAAFDDGYTAEQLIEARTEFIDQLLQRLWIAAGFGDTPDTALVAVGGYGRGELHPLSDIDLLILSRKRLSEAQAQKVGELLTLLWDVKLEVGHSVRTLEECLLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSDGFWPSEKFFAAKVEEQNERHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLREMVGFGFLTEAERNELDECQHLLWRIRFALHLELNRYDNRLLFDRQLSVAQRLRYEGEGNEPVEHMMKDFYRVTRRVGELNQMLLQLFDEAILALTTDEKPRVLDDDFQLRGTLIDLRDETLFIREPQAILRMFYMMVRNRDITGIYSTTLRHLRHARRHLKQPLCYIPEARSLFLAMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLLKLESFAKEETRAKHPLCVDLWPRLSHPELILIAALFHDIAKGRGGDHSVLGAQDILKFAELHGLNSRETQLVAWLVRHHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQSTPDMRERVRHHQLQALALLRMENIDEEALHHIWGRCRANYFVRHSPNQLAWHARHLLRHDLSKPLILLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDDMAMDTFIVLEPDGSPLSPDRHEAIRHGLEQAITQRTWQPPQPRRQPAKLRHFTVETEVNFLPTHTDRKSFLELIALDQPGLLARVGQVFADLGISLHGARISTIGERVEDLFIIATADRRGLNNLLQQEVRQRLTEDLNPNDKV

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli O8 (strain IAI1)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.396 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli (strain K12 / MC4100 / BW2952)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.39 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDVDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVHNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGNPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli (strain K12 / DH10B)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.39 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDVDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVHNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGNPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli O9:H4 (strain HS)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.396 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli O1:K1 / APEC
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.358 kDa
Sequence
MNTLPEQYANTALPTLSGQPQNPCAWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli O6:K15:H31 (strain 536 / UPEC)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.408 kDa
Sequence
MNTLPEQYANTALPTLHGQPQNPCAWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.378 kDa
Sequence
MNTLPEQYANTALPTLHGQPQNPCAWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLGKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.405 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECILEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGNPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli (strain K12)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.39 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDVDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVHNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGNPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.414 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCAWPRDELTVCGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli (strain SE11)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.396 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli (strain SMS-3-5 / SECEC)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.373 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCGWPRDELTVCGIKAHIDTFQRWLGDAFDNGISAEELVEARTEFIDQLLQRLWIDAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli (strain UTI89 / UPEC)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.358 kDa
Sequence
MNTLPEQYANTALPTLSGQPQNPCAWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.433 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCAWPRDELTVCGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDVDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVEQMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGSLIDLRDETLFMRQPEAILRMFYTMVRNSEITGIYSTTLRHLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHHIWSRCRANYFVRHSPNQLAWHARHLLKHDLSKSLVLLSPHATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.383 kDa
Sequence
MNTLPEQYANTALPTLPNQPQNPGVWPRAELTVAGIKARIDIFQHWLGEAFDSGICAEQLIEARTEFIDQLLQRLWIEAGFGQIADLALVAVGGYGRGELHPLSDIDLLILSRKNLPDEQAQKVGELLTLLWDIKLDVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLALQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECLHILWRIRFALHLVLSRYDNRLLFDRQLSVAQRLNYSGEGNDPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFIREPEAILRMFYMMVRNSAITGIYSTTLRHLRHARRHLSQPLCYIPEARTLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLPHPELILIAALFHDIAKGRGGDHSVLGAQDVLTFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTETRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEAVLHKIWTRCRANYFVRHSPNQLAWHARHLLQHDLRQPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLAPDRHEVIRASLEQTITQRSWQPPQPRRQPAKLRHFTVETEVNFLPTHTDRKSFLELIALDQPGLLARVGQIFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQLEVQQRLTAALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Salmonella choleraesuis (strain SC-B67)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.322 kDa
Sequence
MNTHPEQHANTALPTLPDQPQNPGVWPRAELTVAGIKARIDIFQHWLGEAFDSGICAEQLIEARTEFIDQLLQRLWIEAGFGQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELLTLLWDVKLDVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLALQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNDPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPVDDEFQLRGTLIDLRDDTLFIREPQAILRMFYMMVRNSAITGIYSTTLRHLRHARRHLSQPLCYIPEARTLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLPHPELILIAALFHDIAKGRGGDHSVLGAQDVLTFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTETRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEAALHKIWTRCRANYFVRHSPNQLAWHARHLLQHDLRQPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLAADRHDVIRTGLEQTITQRSWQPPQPRRQPAKLRHFTVETEVNFLPTHTDRKSFMELIALDQPGLLARVGQIFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQLEVQQRLTAAFNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Salmonella dublin (strain CT_02021853)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.322 kDa
Sequence
MNTLPEQHANTALPTLPDQPQNPGVWPRAELTVADIKARIDIFQHWLGEAFDSGICAEQLIEARTEFIDQLLQRLWIEAGFGQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELLTLLWDVKLDVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVVLFLALQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNDPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPVDDEFQLRGTLIDLRDDTLFIREPQAILRMFYMMVRNSAITGIYSTTLRHLRHARRHLSQPLCYIPEARTLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLPHPELILIAALFHDIAKGRGGDHSVLGAQDVLTFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTETRLRFLACLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEAALHKIWTRCRANYFVRHSPNQLAWHARHLLQHDLRQPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLAADRHDVIRTGLEQTITQRSWQPPQPRRQPAKLRHFTVETEVNFLPTHTDRKSFMELIALDQPGLLARVGQIFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQLEVQQRLTAALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Salmonella enteritidis PT4 (strain P125109)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.264 kDa
Sequence
MNTLPEQHANTALPTLPDQPQNPGVWPRAELTVAGIKARIDIFQHWLGEAFDSGICAEQLIEARTEFIDQLLQRLWIEAGFGQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELLTLLWDVKLDVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLALQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNDPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPVDDEFQLRGTLIDLRDDTLFIREPQAILRMFYMMVRNSAITGIYSTTLRHLRHARRHLSQPLCYIPEARTLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLPHPELILIAALFHDIAKGRGGDHSVLGAQDVLTFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTETRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEAALHKIWTRCRANYFVRHSPNQLAWHARHLLQHDLRQPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLAADRHDVIRTGLEQTITQRSWQPPQPRRQPAKLRHFTVETEVNFLPTHTDRKSFMELIALDQPGLLARVGQIFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQLEVQQRLTAALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Salmonella gallinarum (strain 287/91 / NCTC 13346)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.235 kDa
Sequence
MNTLPEQHANTALPTLPDQPQNPGVWPRAELTVAGIKARIDIFQHWLGEAFDSGICAEQLIEARTEFIDQLLQRLWIEAGFGQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELLTLLWDVKLDVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLALQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECLHILWRIRFALHLVVSRYDNRLLFDLQLSVAQRLNYSGEGNDPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPVDDEFQLRGTLIDLRDDTLFIREPQAILRMFYMMVRNSAITGIYSTTLRHLRHARRHLSQPLCYIPEARTLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLPHPELILIAALFHDIAKGRGGDHSVLGAQDVLTFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTETRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEAALHKIWTRCRANYFVRHSPNQLAWHARHLLQHDLRQPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLAADRHEVIRTGLEQTITQRSWQPPQPRRQPAKLRHFTVETEVNFLPTHTDRKSFMELIALDQPGLLARVGQIFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQLEVQQRLTAALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Salmonella heidelberg (strain SL476)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.264 kDa
Sequence
MNTLPEQHANTALPTLPDQPQNPGVWPRAELTVAGIKARIDIFQHWLGEAFDSGICAEQLIEARTEFIDQLLQRLWIEAGFGQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELLTLLWDVKLDVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLALQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNDPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPVDDEFQLRGTLIDLRDDTLFIREPQAILRMFYMMVRNSAITGIYSTTLRHLRHARRHLSQPLCYIPEARTLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLPHPELILIAALFHDIAKGRGGDHSVLGAQDVLTFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTETRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEAALHKIWTRCRANYFVRHSPNQLAWHARHLLQHDLRQPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLAADRHDVIRTGLEQTITQRSWQPPQPRRQPAKLRHFTVETEVNFLPTHTDRKSFMELIALDQPGLLARVGQIFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQLEVQQRLTAALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Salmonella newport (strain SL254)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.278 kDa
Sequence
MNTLPEQHANTALPTLPDQPQNPGVWPRAELTVAGIKARIDIFQHWLGEAFDSGICAEQLIEARTEFIDQLLQRLWIEAGFGQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELLTLLWDVKLDVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLALQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNDPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPVDDEFQLRGTLIDLRDDTLFIREPQAILRMFYMMVRNSAITGIYSTTLRHLRHARRHLSQPLCYIPEARTLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLPHPELILIAALFHDIAKGRGGDHSVLGAQDVLTFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTETRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEAALHKIWTRCRANYFVRHSPNQLAWHARHLLQHDLRQPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLAADRHEVIRTGLEQTITQRSWQPPQPRRQPAKLRHFTVETEVNFLPTHTDRKSFMELIALDQPGLLARVGQIFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQLEVQQRLTAALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Salmonella paratyphi A (strain ATCC 9150 / SARB42)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.278 kDa
Sequence
MNTLPEQHANTALPTLPDQPQNPGVWPRAELTVAGIKARIDIFQHWLGEAFDSGICAEQLIEARTEFIDQLLQRLWIEAGFGQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELLTLLWDVKLDVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLALQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNDPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPVDDEFQLRGTLIDLRDDTLFIREPQAILRMFYMMVRNSAITGIYSTTLRHLRHARRHLSQPLCYIPEARTLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLPHPELILIAALFHDIAKGRGGDHSVLGAQDVLTFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTETRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEAALHKIWTRCRANYFVRHSPNQLAWHARHLLQHDLRQPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLAADRHEVIRTGLEQTITQRSWQPPQPRRQPAKLRHFTVETEVNFLPTHTDRKSFMELIALDQPGLLARVGQIFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQLEVQQRLTAALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Salmonella paratyphi A (strain AKU_12601)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.278 kDa
Sequence
MNTLPEQHANTALPTLPDQPQNPGVWPRAELTVAGIKARIDIFQHWLGEAFDSGICAEQLIEARTEFIDQLLQRLWIEAGFGQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELLTLLWDVKLDVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLALQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNDPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPVDDEFQLRGTLIDLRDDTLFIREPQAILRMFYMMVRNSAITGIYSTTLRHLRHARRHLSQPLCYIPEARTLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLPHPELILIAALFHDIAKGRGGDHSVLGAQDVLTFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTETRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEAALHKIWTRCRANYFVRHSPNQLAWHARHLLQHDLRQPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLAADRHEVIRTGLEQTITQRSWQPPQPRRQPAKLRHFTVETEVNFLPTHTDRKSFMELIALDQPGLLARVGQIFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQLEVQQRLTAALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Salmonella schwarzengrund (strain CVM19633)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.171 kDa
Sequence
MNTLPEQHANTALPTLPDQPQNPGVWPRAELTVAGIKARIDIFQHWLGEAFDSGICAEQLIEARTEFIDQLLQRLWIEAGFGQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELLTLLWDVKLDVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLALQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNDPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPVDDEFQLRGTLIDLRDDTLFIREPQAILRMFYMMVRNSAITGIYSTTLRHLRHARRHLSQPLCYIPEARTLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSLIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLPHPELILIAALFHDIAKGRGGDHSVLGAQDVLTFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTETRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEAALHKIWTRCRANYFVRHSPNQLAWHARHLLQHDLSQPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLAADRHDVIRTGLEQTITQRSWQPPQPRRQPAKLRHFTVETEVNFLPTHTDRKSFMELIALDQPGLLARVGQIFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQLEVQQRLTAALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Salmonella typhi
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.123 kDa
Sequence
MNTLPEQHANTALPTLPDQPQNPGVWPRAELTVAGIKARIDIFQHWLGEAFDSGICAEQLIEARTEFIDQLLQRLWIEAGFGQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELLTLLWDVKLDVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLALQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAECAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNDPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPVDDEFQLRGTLIDLRDDTLFIREPQAILRMFYMMVRNSAITGIYSTTLRHLRHARRHLSQPLCYIPEARTLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLPHPELILIAALFHDIAKGRGGDHSVLGAQDVLTFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTETRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEAALHKIWTRCRANYFVRHSPNQLAWHARHLLQHDLSQPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLAADRHDVIRTGLEQTITQHSWQPPQPRRQPAKLRHFTVETEVNFLPTHTDRKSFMELIALDQPGLLARVGQIFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQLEVQQRLTAALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.264 kDa
Sequence
MNTLPEQHANTALPTLPDQPQNPGVWPRAELTVAGIKARIDIFQHWLGEAFDSGICAEQLIEARTEFIDQLLQRLWIEAGFGQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELLTLLWDVKLDVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLALQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNDPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPVDDEFQLRGTLIDLRDDTLFIREPQAILRMFYMMVRNSAITGIYSTTLRHLRHARRHLSQPLCYIPEARTLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLPHPELILIAALFHDIAKGRGGDHSVLGAQDVLTFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTETRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEAALHKIWTRCRANYFVRHSPNQLAWHARHLLQHDLRQPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLAADRHDVIRTGLEQTITQRSWQPPQPRRQPAKLRHFTVETEVNFLPTHTDRKSFMELIALDQPGLLARVGQIFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQLEVQQRLTAALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Shigella boydii serotype 18 (strain CDC 3083-94 / BS512)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.423 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGNPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Shigella boydii serotype 4 (strain Sb227)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.396 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Shigella dysenteriae serotype 1 (strain Sd197)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.377 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPQARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSPELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLDLIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Shigella flexneri serotype 5b (strain 8401)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.437 kDa
Sequence
MNTLPEQYANTALSTLPGQPQNPCAWPRDELTVCGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPFDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPQARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Shigella flexneri
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.403 kDa
Sequence
MNTLPEQYANTALSTLPGQPQNPCAWPRDELTVCGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPLDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPQARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Shigella sonnei (strain Ss046)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.377 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLHYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Salmonella agona (strain SL483)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.222 kDa
Sequence
MNTLPEQHANTALPTLPDQPQNPGVWPRAELTVAGIKARIDIFQHWLGEAFDSGICAEQLIEARTEFIDQLLQRLWIEAGFGQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELLTLLWDVKLDVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLALQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNDPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPVDDEFQLRGTLIDLRDDTLFIREPQAILRMFYMMVRNSAITGIYSTTLRHLRHARRHLSQPLCYIPEARTLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLPHPELILIAALFHDIAKGRGGDHSVLGAQDVLTFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTETRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEAALHKIWTRCRANYFVRHSPNQLAWHARHLLQHDLSQPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGNPLAADRHDVIRTGLEQTITQRSWQPPQPRRQPAKLRHFTVETEVNFLPTHTDRKSFMELIALDQPGLLARVGQIFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQLEVQQRLTAALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.311 kDa
Sequence
MNTLPEQHANTALPTLPGQPQNPGAWSRDELTVSGIKAHIDIFQQWLGDAFDSGISAEQLIEARTEFIDQLLQRLWIDAGFGQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDAQAQKVGELLTLLWDVKLEVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLELQKHIFSEGFWPSEKFFAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLNEMVGFGFLTQAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYTGEGNEPVEHMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDDFQLRGTLIDLRDDDLFIRSPEAILRMFYMMVRNSTITGIYSTTLRHLRHARRHLTQPLCYIPEARSLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRQRHPLCVDLWPRLRQPELILIAALFHDIAKGRGGDHSVLGAQDVLKFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTEHRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNINEEALHQIWTRCRANYFVRHSPNQLAWHARHLLQHDLTRPLILVSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEAIRFGLEQAITQSSWQPPQPRRQPAKLRHFTVDTEVTFLPTHTDRKSFLELIALDQPGLLARVGQIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTAALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli O139:H28 (strain E24377A / ETEC)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.354 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAGGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.376 kDa
Sequence
MNPLPEQYANTALPTLPGQPQNPCAWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLIQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli O45:K1 (strain S88 / ExPEC)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.358 kDa
Sequence
MNTLPEQYANTALPTLSGQPQNPCAWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli (strain 55989 / EAEC)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.396 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli O157:H7
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.422 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPQARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVNVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEVLHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli O157:H7 (strain EC4115 / EHEC)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.422 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPQARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVNVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEVLHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli O7:K1 (strain IAI39 / ExPEC)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.373 kDa
Sequence
MNTLPEQYANTALPTLPGQPQNPCAWPRDELTVCGIKAHIDTFQRWLGDAFDNGISAEELIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDVDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIQFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Escherichia coli O81 (strain ED1a)
Length
890 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.392 kDa
Sequence
MNTLPEQYANTALPTLHGQPQNPCAWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVISRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPEARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLGKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Hydrogenovibrio crunogenus (strain XCL-2)
Length
888 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
103.724 kDa
Sequence
MATTTDKQVSPTSPSFVYNLDHEDRNTSLKSGRAVLTDFNEQQFVKFDKGCSIETLLKERTSFIDQLLKKIWEHFFSKDECEQLTLVAVGGYGRGELQPYSDIDLLILGENFIELQPKIVEFITYLWDIGFEVGHAVRNLEDCIEAGREDVTTATNLLEARWLAGNYEQFLSLQNLFNLKSFWPSHEFFQAKLEEQEKRHKRYNDTLYQLEPNIKESPGGLRDIQTILWVAKRHFGASSLQELMQHNFISLQEYKEIQAAYLYLNRIRFALHRLKKRHEDRLLFDHQQQLAELLNHDDRPEHNDSIKAVEAFMKPYYQNAHIVARLNEILLQHFKEEIYHFAEDKIEPINPRFRIINNYLDVVKENLFAKNPTALLEIFIIIENYQHLIQGIRSRTIRLIRNHLHLIDDQFRSDPINKALFIEIFRQPKGVNAAVKRMYAYGILGAYLPSFKKITGLMQFNIFHAYTVDEHTILVIRNLRRFFIKQHAYEFPTAHQIATQLCKPEILLLAGLFHDIAKGRNGAHEKLGAVDAKAFSQKHNLNKNDTDLLSWLVLRHLDFSYVAQKKDLSDPEIIQQFAEKVGTQQRLDYLYLLTLADVRSTSDEVWNDWKNQLFLQLYHNTTQALDSSSSQPRDRVKQAIFNKEKASELLKKRGLIPMHFQGFWQAFEQTDFFNRQSAAEIARITRVLFEEDHEAINIHLQPTTSRGATELIIYMHDRDYLFAQFTQIIDKLDLNIVEAKIYSGEDDMTLVIIYLLNRESTSITDPMILTEIEETLKHQLFLKDDTMPPTQPEPRRIRVFEMPTHIQFQEINEELTELSISTKDIPGLLAKIGQAFKSCKIRVHDAKINTVGEKAEDTFMISSTTNESIHTRHSQEELKQALLNNIEQ

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Length
888 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.208 kDa
Sequence
MIITSPLLDYVTSHQDIKAINQWRADVEQQLQEFYENGYSIRDIVLARSNLIDEALTFLWKHAGLDQSDLGLFAVGGYGRREMLPYSDVDIMILSENDISPEHEKQISGFISSLWDVGNFKPGTSVRSIQNCVEQATNDLTVATTLIESRLITGNPDLAKWPRRIVSQTWTDKTFFDAKMEEQAKRHAQHNNTESNLEPDIKNAPGGIRDMNQIGWIAKRHFRVNRIYDLVHLGFITEYELKVLEEAESFLWEIRHHLHLLSKRDENRLLFDHQREIAAKFGYTRAEGQPVNFAVEQFMKRYYRTAQQVSTLNEMLLAYFNESVITPRLPNYERKIEEINENFKLVDGKLAVQHHKVFSENPSAILELFYLLANHPEIEGIRARTLRLLIMAAKRIDQEFRDNPAHQALFMAIIRSPYRLYDTLVDMKRYGILGNYIPAFGQIMGLMQYDLFHIYTVDAHTLLLIRNLNRFKEPEFAQHFPVVSSVFQRLARRDIVYLAAIFHDIAKGRGGDHSELGAEDAIEFCRAHGFTERECKLVAWLIHNHLLMSLTAQKKDISDPDVIKEFAEKLGDMEHLDYLYTLTVADINATNPKLWNTWRASLMRQLYTYSRDVIRSGLGRPVDYQMLIEDTKFSASETLVNEFSLDAVEKVWQELGDEYFLKESADEIAWHTRAILQHGDNPAPIVLLRAHRQSAQDAVQIFIYTQDKPNLFATTVAVLDRMNLDVQDARIITATKAFSLDTYVVLDRFGTLLTDPEREHTVKEALIKALSQSDKYPGLMQRRIPRQLRHFDIENTVDITLNPVLQQNMVEISTLDQPGLLARVGGLFMMQGLDIHSAKIATLGERAEDIFFVTKKDGQPMTTDEAHIFSAQLKLALDEASNQIVSQH

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Length
888 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.208 kDa
Sequence
MIITSPLLDYVTSHQDIKAINQWRADVEQQLQEFYENGYSIRDIVLARSNLIDEALTFLWKHAGLDQSDLGLFAVGGYGRREMLPYSDVDIMILSENDISPEHEKQISGFISSLWDVGNFKPGTSVRSIQNCVEQATNDLTVATTLIESRLITGNPDLAKWPRRIVSQTWTDKTFFDAKMEEQAKRHAQHNNTESNLEPDIKNAPGGIRDMNQIGWIAKRHFRVNRIYDLVHLGFITEYELKVLEEAESFLWEIRHHLHLLSKRDENRLLFDHQREIAAKFGYTRAEGQPVNFAVEQFMKRYYRTAQQVSTLNEMLLAYFNESVITPRLPNYERKIEEINENFKLVDGKLAVQHHKVFSENPSAILELFYLLANHPEIEGIRARTLRLLIMAAKRIDQEFRDNPAHQALFMAIIRSPYRLYDTLVDMKRYGILGNYIPAFGQIMGLMQYDLFHIYTVDAHTLLLIRNLNRFKEPEFAQHFPVVSSVFQRLARRDIVYLAAIFHDIAKGRGGDHSELGAEDAIEFCRAHGFTERECKLVAWLIHNHLLMSLTAQKKDISDPDVIKEFAEKLGDMEHLDYLYTLTVADINATNPKLWNTWRASLMRQLYTYSRDVIRSGLGRPVDYQMLIEDTKFSASETLVNEFSLDAVEKVWQELGDEYFLKESADEIAWHTRAILQHGDNPAPIVLLRAHRQSAQDAVQIFIYTQDKPNLFATTVAVLDRMNLDVQDARIITATKAFSLDTYVVLDRFGTLLTDPEREHTVKEALIKALSQSDKYPGLMQRRIPRQLRHFDIENTVDITLNPVLQQNMVEISTLDQPGLLARVGGLFMMQGLDIHSAKIATLGERAEDIFFVTKKDGQPMTTDEAHIFSAQLKLALDEASNQIVSQH

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Acinetobacter baumannii (strain AB307-0294)
Length
887 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.102 kDa
Sequence
MINTSPLLNYVSSHHDIKAINQWRTDVEKQLQDSYENGQSIREIIKARSDLVDEALVFLWKHAELDQSKLGLFAVGGYGRREMLPYSDVDIMILSEDEISEENEKRISTFISSLWDVGNFKPGISVRTIQSCVEQAATDLTVATTLIEARLITGNTQLAKWPRRIVSQTWTDKTFYDAKMAEQAKRYHQHNNTESNLEPDIKNAPGGIRDINQIGWIAKRHFRVNRIYDLVHLGFISEFELAVLEEAESFLWEIRHHLHRLAKRDENRLLFDHQREIAAKFGYVRQEGQPVNYGVEQFMKRYYRTAQQVSTLNEMLLAYFSESVITPRLPNYERKIEVVNDHFKIVDNKLAVQHHKIFAEHPSAILELFYILANRPDIEGIRARTLRLLILAAKRINQSYRDNPEHQALFMSIIRSPYRLYDTLVAMKRYGVLGNYIPAFGQIMGLMQYDLFHIYTVDAHTLLLLRNLNRFREPEFAKEFPVVSSVFQRLARQDIVFIAALFHDIAKGRGGDHSELGAEDAIEFGRAHGFTERECKLIAWLIQNHLLMSLTAQKKDISDPDVVKDFAEKLGDMEHLDYLYTLTVADINATNPKLWNTWRASLMRQLYTHARDVIRTGLGRPVDYQMLIEDTKFAASELLVNNFALADVEKVWQELGDEYFIKESADEIAWHTQAILKHGDNPEPLVLLRAHRKAAQDAVQIFIYTRDQPNLFATTVAVLDRMNLDVQDAKIITASTAFSLDTYVVLDRFGTLLTDPEREETVKNALVKALSQPDQYPGLMQRRIPRQLRHFDIENTVDVTLNEALQQNMVEISTLDHPGLLARVGGLFMMQGLDIHSARIATLGERAEDIFFVTKKDGKPLNNEEVKLFSEKLKAALDEASNQICQH

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Acinetobacter baumannii (strain AB307-0294)
Length
887 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.102 kDa
Sequence
MINTSPLLNYVSSHHDIKAINQWRTDVEKQLQDSYENGQSIREIIKARSDLVDEALVFLWKHAELDQSKLGLFAVGGYGRREMLPYSDVDIMILSEDEISEENEKRISTFISSLWDVGNFKPGISVRTIQSCVEQAATDLTVATTLIEARLITGNTQLAKWPRRIVSQTWTDKTFYDAKMAEQAKRYHQHNNTESNLEPDIKNAPGGIRDINQIGWIAKRHFRVNRIYDLVHLGFISEFELAVLEEAESFLWEIRHHLHRLAKRDENRLLFDHQREIAAKFGYVRQEGQPVNYGVEQFMKRYYRTAQQVSTLNEMLLAYFSESVITPRLPNYERKIEVVNDHFKIVDNKLAVQHHKIFAEHPSAILELFYILANRPDIEGIRARTLRLLILAAKRINQSYRDNPEHQALFMSIIRSPYRLYDTLVAMKRYGVLGNYIPAFGQIMGLMQYDLFHIYTVDAHTLLLLRNLNRFREPEFAKEFPVVSSVFQRLARQDIVFIAALFHDIAKGRGGDHSELGAEDAIEFGRAHGFTERECKLIAWLIQNHLLMSLTAQKKDISDPDVVKDFAEKLGDMEHLDYLYTLTVADINATNPKLWNTWRASLMRQLYTHARDVIRTGLGRPVDYQMLIEDTKFAASELLVNNFALADVEKVWQELGDEYFIKESADEIAWHTQAILKHGDNPEPLVLLRAHRKAAQDAVQIFIYTRDQPNLFATTVAVLDRMNLDVQDAKIITASTAFSLDTYVVLDRFGTLLTDPEREETVKNALVKALSQPDQYPGLMQRRIPRQLRHFDIENTVDVTLNEALQQNMVEISTLDHPGLLARVGGLFMMQGLDIHSARIATLGERAEDIFFVTKKDGKPLNNEEVKLFSEKLKAALDEASNQICQH

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Acinetobacter baumannii (strain AB0057)
Length
887 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.102 kDa
Sequence
MINTSPLLNYVSSHHDIKAINQWRTDVEKQLQDSYENGQSIREIIKARSDLVDEALVFLWKHAELDQSKLGLFAVGGYGRREMLPYSDVDIMILSEDEISEENEKRISTFISSLWDVGNFKPGISVRTIQSCVEQAATDLTVATTLIEARLITGNTQLAKWPRRIVSQTWTDKTFYDAKMAEQAKRYHQHNNTESNLEPDIKNAPGGIRDINQIGWIAKRHFRVNRIYDLVHLGFISEFELAVLEEAESFLWEIRHHLHRLAKRDENRLLFDHQREIAAKFGYVRQEGQPVNYGVEQFMKRYYRTAQQVSTLNEMLLAYFSESVITPRLPNYERKIEVVNDHFKIVDNKLAVQHHKIFAEHPSAILELFYILANRPDIEGIRARTLRLLILAAKRINQSYRDNPEHQALFMSIIRSPYRLYDTLVAMKRYGVLGNYIPAFGQIMGLMQYDLFHIYTVDAHTLLLLRNLNRFREPEFAKEFPVVSSVFQRLARQDIVFIAALFHDIAKGRGGDHSELGAEDAIEFGRAHGFTERECKLIAWLIQNHLLMSLTAQKKDISDPDVVKDFAEKLGDMEHLDYLYTLTVADINATNPKLWNTWRASLMRQLYTHARDVIRTGLGRPVDYQMLIEDTKFAASELLVNNFALADVEKVWQELGDEYFIKESADEIAWHTQAILKHGDNPEPLVLLRAHRKAAQDAVQIFIYTRDQPNLFATTVAVLDRMNLDVQDAKIITASTAFSLDTYVVLDRFGTLLTDPEREETVKNALVKALSQPDQYPGLMQRRIPRQLRHFDIENTVDVTLNEALQQNMVEISTLDHPGLLARVGGLFMMQGLDIHSARIATLGERAEDIFFVTKKDGKPLNNEEVKLFSEKLKAALDEASNQICQH

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Acinetobacter baumannii (strain ACICU)
Length
887 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.117 kDa
Sequence
MINTSPLLNYVSSHHDIKAINQWRTDVEKQLQDSYENGQSIREIIKARSDLVDEALVFLWKHAELDQSKLGLFAVGGYGRREMLPYSDVDIMILSEDEISEENEKRISTFISSLWDVGNFKPGISVRTIQSCVEQAATDLTVATTLIEARLITGNTQLAKWPRRIVSQTWTDKTFYDAKMAEQAKRYHQHNNTESNLEPDIKNAPGGIRDINQIGWIAKRHFRVNRIYDLVHLGFISEFELAVLEEAESFLWEIRHHLHRLAKRDENRLLFDHQREIAAKFGYVRQEGQPVNYGVEQFMKRYYRTAQQVSTLNEMLLAYFSESVITPRLPNYERKIEVVNDHFKIVDNKLAVQHHKIFAEHPSAILELFYILANRPDIEGIRARTLRLLILAAKRINQSYRDNPEHQALFMSIIRSPYRLYDTLVAMKRYGVLGNYIPAFAQIMGLMQYDLFHIYTVDAHTLLLLRNLNRFREPEFAKEFPVVSSVFQRLARQDIVFIAALFHDIAKGRGGDHSELGAEDAIEFGRAHGFTERECKLIAWLIQNHLLMSLTAQKKDISDPDVVKDFAEKLGDMEHLDYLYTLTVADINATNPKLWNTWRASLMRQLYTHARDVIRTGLGRPVDYQMLIEDTKFAASELLVNNFALADVEKVWQELGDEYFIKESADEIAWHTQAILKHGDNPEPLVLLRAHRKAAQDAVQIFIYTRDQPNLFATTVAVLDRMNLDVQDAKIITASTAFSLDTYVVLDRFGTLLTDPEREETVKNALVKALSQPDQYPGLMQRRIPRQLRHFDIENTVDVTLNEALQQNMVEISTLDHPGLLARVGGLFMMQGLDIHSARIATLGERAEDIFFVTKKDGKPLNNEEVKLFSEKLKAALDEASNQICQH

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Acinetobacter baumannii (strain SDF)
Length
887 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.102 kDa
Sequence
MINTSPLLNYVSSHHDIKAINQWRTDVEKQLQDSYENGQSIREIIKARSDLVDEALVFLWKHAELDQSKLGLFAVGGYGRREMLPYSDVDIMILSEDEISEENEKRISTFISSLWDVGNFKPGISVRTIQSCVEQAATDLTVATTLIEARLITGNTQLAKWPRRIVSQTWTDKTFYDAKMAEQAKRYHQHNNTESNLEPDIKNAPGGIRDINQIGWIAKRHFRVNRIYDLVHLGFISEFELAVLEEAESFLWEIRHHLHRLAKRDENRLLFDHQREIAAKFGYVRQEGQPVNYGVEQFMKRYYRTAQQVSTLNEMLLAYFSESVITPRLPNYERKIEVVNDHFKIVDNKIAVQHHKIFAEHPSAILELFYILANRPDIEGIRARTLRLLILAAKRINQSYRDNPEHQALFMSIIRSPYRLYDTLVAMKRYGVLGNYIPAFGQIMGLMQYDLFHIYTVDAHTLLLLRNLNRFREPEFAKEFPVVSSVFQRLARQDIVFIAALFHDIAKGRGGDHSELGAEDAIEFGRAHGFTERECKLIAWLIQNHLLMSLTAQKKDISDPDVVKDFAEKLGDMEHLDYLYTLTVADINATNPKLWNTWRASLMRQLYTHARDVIRTGLGRPVDYQMLIEDTKFAASELLVNNFALADVEKVWQELGDEYFIKESADEIAWHTQAILKHGDNPEPLVLLRAHRKAAQDAVQIFIYTRDQPNLFATTVAVLDRMNLDVQDAKIITASTAFSLDTYVVLDRFGTLLTDPEREETVKNALVKALSQPDQYPGLMQRRIPRQLRHFDIENTVDVTLNEALQQNMVEISTLDHPGLLARVGGLFMMQGLDIHSARIATLGERAEDIFFVTKKDGKPLNNEEVKLFSEKLKAALDEASNQICQH

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377)
Length
887 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.126 kDa
Sequence
MINTSPLLNYVSSHHDIKAINQWRTDVEKQLQDSYENGQSIREIIKARSDLVDEALVFLWKHAELDQSKLGLFAVGGYGRREMLPYSDVDIMILSEDEISEENEKRISTFISSLWDVGNFKPGISVRTIQSCVEQAATDLTVATTLIEARLITGNTQLAKWPRRIVSQTWTDKTFYDAKMAEQAKRYHQHNNTESNLEPDIKNAPGGIRDINQIGWIAKRHFRVNRIYDLVHLGFISEFELAVLEEAESFLWEIRHHLHRLAKRDENRLLFDHQREIAAKFGYVRQEGQPVNYGVEQFMKRYYRTAQQVSTLNEMLLAYFSESVITPRLPNYERKIEVVNDHFKIVDNKLAVQHHKIFAEHPSAILELFYILANRPDIEGIRARTLRLLILAAKRINQSYRDNPEHQALFMSIIRSPYRLYDTLVAMKRYGVLGNYIPAFGQIMGLMQYDLFHIYTVDAHTLLLLRNLNRFREPEFAKEFPVVSSVFQRLARQDIVFIAALFHDIAKGRGGDHSELGAEDAIEFGRAHGFTERECKLIAWLIQNHLLMSLTAQKKDISDPDVVKDFAEKLGDMEHLDYLYTLTVADINATNPKLWNTWRASLMRQLYTHARDVIRTGLGRPVDYQMLIEDTKFAASELLVNNFALADVEKVWQELGDEYFIKESADEIAWHTQAILKHGDNPEPLVLLRAHRKAAQDAVQIFIYTRDQPNLFATTVAVLDRMNLDVQDAKIITASTAFSLDTYVVLDRFGTLLTDPEREETVKNALVKALSQPDQYPGLMQRRIPRQLRHFDIENTVDVTLNEALQQNMVEISTLDHPGLLARVGGLFMMQGLDIHSARIATLGERAEDIFFVTKKDGKPLNHEEVKLFSEKLKAALDEASNQICQH

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Acinetobacter baumannii (strain AYE)
Length
887 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.102 kDa
Sequence
MINTSPLLNYVSSHHDIKAINQWRTDVEKQLQDSYENGQSIREIIKARSDLVDEALVFLWKHAELDQSKLGLFAVGGYGRREMLPYSDVDIMILSEDEISEENEKRISTFISSLWDVGNFKPGISVRTIQSCVEQAATDLTVATTLIEARLITGNTQLAKWPRRIVSQTWTDKTFYDAKMAEQAKRYHQHNNTESNLEPDIKNAPGGIRDINQIGWIAKRHFRVNRIYDLVHLGFISEFELAVLEEAESFLWEIRHHLHRLAKRDENRLLFDHQREIAAKFGYVRQEGQPVNYGVEQFMKRYYRTAQQVSTLNEMLLAYFSESVITPRLPNYERKIEVVNDHFKIVDNKLAVQHHKIFAEHPSAILELFYILANRPDIEGIRARTLRLLILAAKRINQSYRDNPEHQALFMSIIRSPYRLYDTLVAMKRYGVLGNYIPAFGQIMGLMQYDLFHIYTVDAHTLLLLRNLNRFREPEFAKEFPVVSSVFQRLARQDIVFIAALFHDIAKGRGGDHSELGAEDAIEFGRAHGFTERECKLIAWLIQNHLLMSLTAQKKDISDPDVVKDFAEKLGDMEHLDYLYTLTVADINATNPKLWNTWRASLMRQLYTHARDVIRTGLGRPVDYQMLIEDTKFAASELLVNNFALADVEKVWQELGDEYFIKESADEIAWHTQAILKHGDNPEPLVLLRAHRKAAQDAVQIFIYTRDQPNLFATTVAVLDRMNLDVQDAKIITASTAFSLDTYVVLDRFGTLLTDPEREETVKNALVKALSQPDQYPGLMQRRIPRQLRHFDIENTVDVTLNEALQQNMVEISTLDHPGLLARVGGLFMMQGLDIHSARIATLGERAEDIFFVTKKDGKPLNNEEVKLFSEKLKAALDEASNQICQH

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Klebsiella oxytoca
Length
887 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism (Probable).
Similarity
Belongs to the GlnD family.
Mass
102.344 kDa
Sequence
MSNSLSNTVPPDLSAQPENPGEWPKSDFNCATIKALIDAFQRWLGEAFDSGIAAERLIEARTEFIDQLLQRLWVEYGFGSINDIALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGERLALLWDIKLEVGHSVRTLEECLLEGLSDLSVATNLIESRLLIGDVALFLELQKHIFSDGFWPSEKFFAAKVEEQNDRHQRYHGTSYNLEPDVKSSPGGLRDIHTLQWIARRHFGATSLDEMVGFGFLTEAERNELNECLHQLWRIRFALHLELNRYDNRLLFDRQFSVARRLRYEGESNQPIEHMMKDFFRVTRRVSELNQMLIQLFEEAILALTEDEKPRPIDDDFQLRGTLIDLRDDTLFIREPQAILRMFYTMVRNSSITGIYSTTVRHLRHARRHLTQPLCYIPEARTLFLSMLRHQGGLSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLLKLESFAKEETRSRHPLWLELWPRLTHPELILIAALFHDIAKGAGGDHSILGAQDVLKFAELHGLNCAQTQLVAWLVRHQLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLHYLVCLTVADICATNENLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMENINEQALHQIWNRCRANYFVRHTPNQLAWHARNLLKHDLSKPMILLSSHATRGGTEIFIWSPDRPYLFAAVSAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRTQMIRVGLEQTLSQRSWQPPAPRRQAAKLRHFSVPTEVNFLPTHTDRKSFLELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVQQRLTEALNPNDKG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71)
Length
887 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
101.51 kDa
Sequence
MKGLNAKPFSHEAVRQKLLSGRESLQRRYHQNRNGAALLRDHSRLVDGILRQVWHEMNMPGSTALLAVGGYGRRQLFPYSDIDLVVLLPDKGDAAEAMDNELGTRLEHWVGLLWDIGLDIGHSVRTVKECGEEAANDITVQTSLLEARLLGGNSDLFDRFLQVMETMLAPRKFFVDKQLEQQQRHKRYQDAPYKLEPNIKESPGGLRDLQNVLWISRAAGFGKTWSELAKKGFIIRREARLIQRQQTVLQDLRIRLHYLGGRREDRLLFDYQNPLAEELGIAAKPPRRPGEMLMQRYYRAARSVTQVNTILLLTLHAEIFPDEEAVTTIINERFQKRGDLLEICEEDIFERDPGAILESVLLLQQNPDLKGRSFATLRAMWRSAPLITASFRREPRHCAMFMEILRQPRGLTRELRLMNRYGILGRYIPAFGRIIGQMQHDLFHVYTVDEHILMVVRNLRRFMAPEFAYEYPLCSRLINEFERPELLYLAGLFHDIAKGRQGDHSLLGKVDARRFCERHRMPAEDTELVVWLVENHLHMSATAQKKDIADAEVIADFAASMRDERHLIALYLLTVSDIRGTSPKVWNAWKGKLLEDLFHRTRQYLCGETALTDISLENRKNKVLQLLHPDDAAMRAYERFWSGLDSSYLMMHDPREIAWHTQHLSQRMKSPAPIVKTRAAETGAGVEVLVYTADQKDLFARICSFFDGIDYNIVQAKIHTTREGYALDSFLVLDPFNVANHDPREFQFIEQELTQQLEQQALMATPVKGRLSRHLRHFPITPQVSIEPDDSGAYYVLSITAGDQSGLLSRIAQVLVRFGLNVHSARINTLGERAEDTFLVTGSILSNSRSVIQLEANLIKVLHTSPQPETPGKAPGKPSAGDRIIPR

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Photorhabdus luminescens subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)
Length
882 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
102.232 kDa
Sequence
MSADIATIQAPIPPLSPADFSSEDLRYPVLKQHLEEFQLWLEHAFKAGISAEALISARSDYIDQLLQQLWYAYRFDKISSLSLIAVGGYGRRELHPLSDIDVLILSEQPLTPPQAQNVGQFITLLWDIRLEVGHSVRTLEECLLEGLSDLTIATNLIESRLICGDSSIFLRLQRHTFSDGFWPSTEFFDAKIVEQHERHQRYHSTSYNLEPDIKSSPGGLRDIHTLLWVARRHFGATSIDEMVDFGFLTAEERNELNECQSFLWRIRFALHLVVNRYDNRLLFDRQFSIAQLLGYHGERNQPVERMMKDFYRMTRRVSELNNMLLQLFDEAILALETNEKSRSLDSEFQLRGQLIDLIDETLFIKEPAAIMRMFYRMAEHEEVQGIYSTTLRHLRYARRNLSQPLCELPEARQIFMDILRHPRAVESAFVPMHRHSVLGAYTPLWGNIVGQMQFDLFHAYTVDEHTIRVLRKLESFANENNRPAHPLCVELYPRLPQPELLHLAALFHDIAKGRTGDHSELGADDALAFSLKHGLNSREADLVAWLVRHHLLMSVTAQRRDIQDPEIIKQFTHQILNETRLRYLICLTVADICATNVNLWNSWKQSLLRELYFSTENQLRQGNTPDFRERIRHNRFQALALLRQDNINEQKLHQLWSRCHADYFLRHTPKQLAWHAHHLVQHDSQESLILISTKPTRGGTEIFIWSVDRPSLFAAVVGELDRRNLSVHHAQIFTNRDGMTMDTFVVLEPNGHPLASDRHEIIRNALLQVVLAPHTKTPKTRKLPTKLRHFNVPTKVTFLPTHNERRTYMELFALDQPGLLARVGNIFAEMGVSLHGAHITTIGERVEDFFVLADKDHKALNKKVREELSERLTATLNPKDKI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
Length
879 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
101.332 kDa
Sequence
MANVQEDKDFHGRWPDRTLQPCLKDYKALLESYQNWSAARFVTADIDELVHHRATFFDQLISQLWQQFQLEDEPASILAVGGYGRETLHPGSDIDLLILVGPENAEAEAKLSEKLGQFVTFLWDLHLDIGHSVRTIEDCFAQSENDITIATNLIESRYLSGAESLYNEFHQQLLNDFPWSSRDFYQAKLDEQKQRHQQYHSTSYNLEPNIKSSPGGLRDIQTVGWIAKRHFRTHSDENLVEYGYMTADEFVELRDCMNWLWRIRFALHLEAGKREDRLLFDFQPGVAVRLGYGNDGKASVETMMKDYFKVVLRVSELNQMLLQFFHQAILGTQDLQHAEHISDDFAVANKLLTARHDNVFDNHCNIIRAFVCIAEHPQIQGIHSNTIRLLRNARAQLSEPLSHDPECRDLFNQLIQHPRGCGLSFALMHHHSVLASYLSQWQQIVGQMQFDLFHAYTVDEHTFRLVRNLYRFSDEDYQDQFPLCEKLVAQMDRRYCLYLAGIFHDIAKGRGGDHSELGEMDARNFCHQHGYSEEDAELVAWLVRHHLTMSVTAQKRDIHDPEVIQDFANQVSTPERLDYLYCLTVADIRATNQSLWNNWKATLLEELYNATSYLLQQDSNKPTLDIRQKINENKASAMALLLSAGFEKAEILALWGRFTADYFFRHTAEQISWHSQHILNLPSEQLPLILIGDENNYGTTELFIYHHEEGHLFASVAGVLDSQQLNILDAQILATRDGFVMDTFVVLQRDGKPLTEPHRIEEVKQQLLDVLHKRIPVPSTKRPLSRRMKNFSVATEVTFIPSKHHGRTTFELVTLDRPGLIAKLAAILQQQNVILLAAKITTIGEQAEDLFIVTTEQQTALSDKQKKTLKAKIIKDLEF

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Colwellia psychrerythraea (strain 34H / ATCC BAA-681)
Length
878 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
101.844 kDa
Sequence
MTSHPVSVHIVPSHFINQLAISADFLSTRDICQLSQSFNTWLKDVFIENDINDLLSARAVFVDAILKKLWCQHHLDEFQITLIAVGGYGRGELHPQSDVDILLLTQEEVDLELEEKISSFITQLWDIKLDIGHSVRSIKECLKQAVKEVTVATNLMEMRQVAGNETLTQQLTPLLSEDVFWTSEKFFIAKCKEQEARHQQYRGAAYTLEPNLKANPGGLRDIQTIAWVAKRHFSADSLEELVEHDYLYPNEFFELLESQDYLWRMRFALHFVAGRSENRLLFDYQADVAKMMGFGDEGKAPVERMMKRFFRIIARVTELNTMLLQHFEQAIIKKPELSNISIINQDFELVDKLINTRNDRIFMRPVKMIEMFLIIAQEPGIKGIHSHTMRLMRNARRRLISGLIDYAECRRMFMAIIRHPRGLGLALTLMHRHSILSSYLPLWRNIAGQMQFDLFHAYSVDEHSYRVIKNLHQFSQKEHNHKFPLCSKIVQKIRKPEVLYLAGFFHDIGKGRGGDHAKLGAVDALTFCLSHQLSKHDSNMVAWLVEHHLLMSVTAQRRDINDENVIRTFGEIVRDEAHLNYLYCLTVADMRGTNESLWNNWKANLLEELYFNTLSAFRHGLEKPVEVRSKIRENQQQALALLNENNVDEQSIKALWREFRIDYFLRYSPEQIARQCQNIVEHDREKPLVLISPIPYRGGTEVFIFTKEKNNTFASTVSFLVTKKLSIHDAKIITTKTGYTVNTFVVLDSRNKPLRERFYTKEMSQALVDRLQQVNICELPEPKLARHMKKFKVPLRVNFIKIHAKNRTMIEIIALDRPGLLSNISQVFLEARVNIHSAKITTFGEKADDVFTISTEEDDALTTQEKEALALRLTQEID

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Length
877 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
99.886 kDa
Sequence
MDGPNSDRAHDRHAFDRVAACKARIQHNTAELAERFRTGTPVADLIRERTAFIDHLLSEAWDRRIGRGATDVALVAVGGYGRGELLLHSDVDLLILLDEAAPSSRKQDLSDFLRLLWDIGLKPGHSVRSPAECAEAARTDQTIITNLLEGRLLVGSAALWEAVRSETAPERMWSSAAFFEAKMAEQRIRYSKYHNTAYNLEPNVKEGPGGLRDIQLIGWIIRRHSDARGLQDLVAHGWLTDAEYRELKEAQAFLWRIRFALHALTGRCEDRLLFDYQRELAGLFGYRGETSNEVVEGFMQDYFRTVTGVERLNELLLQLFNEAVLHRDDAFSPTPVNDHFQAVNDYLEAVHPAVFREHPLALLEVFLILQKNSALEGVRAATIRLIRQHIHLIDDAFRNDPEACRLFMDILRQPGGVTHQLRRMNRYGVLAAYLPEFGRVVGRMQYDLFHVYTVDEHTLFVVRNLRRFALEEFQQENPLCYELFQLIEKPELLYIAALMHDIAKGSDGDHSEVGERIAEEFCRRHRIGPRETLLVKWLVRHHLVMSMTAQRKDLSDPEVIHEFAQIVRNQNTLNHLYLLTVADIRATNPSLWNSWKGALLQELYTSTSWTLRRGLDTPPDYAEQISAAKDEARTLLQRFGLAEDAITAVWENIGDDYFLRFLPEEIAWHTTAIAACRPEHLPLVLLRPESLRGSVEVFIYERNRDFLFAQTTAVLDQLGLTVLDAKIIASRQGFALLSFNVLERSGTAPEGLFRLVQICDRLKEALSGGGAPPPAVSRLATRQIRHFTVPTKVFFHDDPQNRFSILELIATDRPGLLSKVGQAFMRTGIRLHNAKISTVGSRAEDIFFITDREDRPLDGEADRAALRRVLIEFVGDQ

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Length
876 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
101.542 kDa
Sequence
MPYQSPITFQEPQLTVESLKQQLESFTEYQKQEFFDHHPVTDLVLGRSEYMDLLLHRLWQFFGFDELVEVSLVAVGGYGRGELHPLSDIDLLVLSQQPLSEQVANKISQFLTLLWDLKLEIGHAVRTVEQCAEIGKADLTVATNLQEARLLCGCEETFHRLKMVIHSESFWPSEIFYQAKVREQKERHARYHDTTYNLEPDIKSTPGGLRDIHTLSWVARRHFGATSLYEMSRFGFLTDAEYRELVECQDFLWRVRFALHIELKRYDNRLTFAHQVQVARHLGYFGEGNRGIEMMMKEFFRTLRRVAELNKMLLKIFDKAILNNGEEAEAVIIDDDFQRRGNMIEARKPALFQARPETILDMFLHMASDSTIESVAPATMRQLRTARRRLNKFLHTLPAAREKFIELVRHPNALHKAFSQMHKLGVLAAYLPQWNQIVGQMQFDLFHVYTVDEHSIRLLKHIHLFSDANNHDRHPICCEIYPKIQKKELLILAAIFHDIGKGRGGDHSEIGADEAFDFCIEHGLSKPEAKLVAWLVKNHLLMSVTAQRRDIYDPDVIIEFAKKVRDEERLEYLVCLTVADICATNPELWNSWKRTLLAELFYSTQRALRRGLENPVDVRERIRHNQQMASALLRKEGFSSREIEVLWQRFKADYFLRHTHKQIAWHCTHLLRHEDSSKPLVLLSKKATRGGTEVFIYTKDQAALFATVVAELDRRNLNVHDAQIMASKDGYVLDTFMVLDQNGQAIEEDRHQALIRHLVHVLEDGRPTTQKARRIPRNLQHFKVKTQVDFLPTKSKKRTLMEFVALDTPGLLATVGATFAELNLDLHAAKITTIGERAEDLFILTNAQGTRLNEEEEQHLREKLIEHVAELAPSAQ

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Length
876 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
101.542 kDa
Sequence
MPYQSPITFQEPQLTVESLKQQLESFTEYQKQEFFDHHPVTDLVLGRSEYMDLLLHRLWQFFGFDELVEVSLVAVGGYGRGELHPLSDIDLLVLSQQPLSEQVANKISQFLTLLWDLKLEIGHAVRTVEQCAEIGKADLTVATNLQEARLLCGCEETFHRLKMVIHSESFWPSEIFYQAKVREQKERHARYHDTTYNLEPDIKSTPGGLRDIHTLSWVARRHFGATSLYEMSRFGFLTDAEYRELVECQDFLWRVRFALHIELKRYDNRLTFAHQVQVARHLGYFGEGNRGIEMMMKEFFRTLRRVAELNKMLLKIFDKAILNNGEEAEAVIIDDDFQRRGNMIEARKPALFQARPETILDMFLHMASDSTIESVAPATMRQLRTARRRLNKFLHTLPAAREKFIELVRHPNALHKAFSQMHKLGVLAAYLPQWNQIVGQMQFDLFHVYTVDEHSIRLLKHIHLFSDANNHDRHPICCEIYPKIQKKELLILAAIFHDIGKGRGGDHSEIGADEAFDFCIEHGLSKPEAKLVAWLVKNHLLMSVTAQRRDIYDPDVIIEFAKKVRDEERLEYLVCLTVADICATNPELWNSWKRTLLAELFYSTQRALRRGLENPVDVRERIRHNQQMASALLRKEGFSSREIEVLWQRFKADYFLRHTHKQIAWHCTHLLRHEDSSKPLVLLSKKATRGGTEVFIYTKDQAALFATVVAELDRRNLNVHDAQIMASKDGYVLDTFMVLDQNGQAIEEDRHQALIRHLVHVLEDGRPTTQKARRIPRNLQHFKVKTQVDFLPTKSKKRTLMEFVALDTPGLLATVGATFAELNLDLHAAKITTIGERAEDLFILTNAQGTRLNEEEEQHLREKLIEHVAELAPSAQ

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Mannheimia succiniciproducens (strain MBEL55E)
Length
875 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.522 kDa
Sequence
MIGHNNFIIQSVILRFFMFQSVEGLLTPGLIKQQKEQLKQTELENFAQADVNSLISHRTLFCDNFLIRLWRQFSLHEVTDLALIAVGGYGRREIFPLSDLDFLILTEQPMPADLAKKVEEFIQFVWDCGFDVGASVRTLEDCDSQGRADITIATNLLESRLLTGNETLFDKLSSIVGREDFWPRKTFFEAKIQEKKQRYQRYNNTSYNLEPDIKYNPGGLRDLHLIYWIALRHSNALSLEEILQSGFIYPEEYAELERNQQFLFKVRFALHLILKRYDNRLLFDRQVKVSELLGYQGEGNQGVETMMKAFFQSLQAISLASDILAKHYKEHFVDENGEEECQVLDDNFQMINNAIFLVREDCFVQQPDTILDLFSYLIIRPQAELHSSTLRLLHLALGQLNGYLSELPAAREKFLRLLTQPRGIERALIPMHKYGVLTAYIPEWKGIEGLMQFDLFHIYTVDEHTMRVLAKLETFLSEETAEAHPLCVKLFPSLPDRALIYIAALFHDIAKGRGGNHADLGAVDVGRFAAQHGFDCREIETMKWLVKQHLFMSVTAQRRDIHDPEVVMNFAAEVQNQVRLNYLVCLTVADICATNTTLWNSWKRSLFASLYQYTNQQFNQGMDNLLDNQEQEEQNKALALEILQSQGFTEDVQSLWKRCPGDYFLRNTPKELAWHAVLLAGVETELLVKISNRFSAGGTEVFIYCKDRPNLFLKVVAAIGNKKLSIHDAQIITSLDGYAFDSFIVTELDGSLLKFDRRRVLEKAIINSLNSNELTKLQGSENHKLQHFNVKTEVRFLNTEKTTHTEMELFTLDKAGLLADVSLVFSELNLSIQNAKITTIGEKAQDFFILTNAKGEALSERERQSLSEKLQARLD

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Vibrio campbellii (strain ATCC BAA-1116 / BB120)
Length
874 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.71 kDa
Sequence
MTLQSPLTFRDEQINIGELKQELEKFSSYQKEEFLQHHPVTNLVLSRAEYMDLLLNRLWQHFGFKDIHNISLVAVGGYGRGELHPLSDIDILILSNNKLPNALEAKISEFITLLWDLRLEVGHAVRTVDECAEIGRADLTVATNLQEARLLCGSEDTFQALKKVVLSDSFWPSETFYRAKIQEQRERHARYHDTTYNLEPDIKSTPGGLRDIHTLSWVARRHFGATSLLEMSRYGFLTDAEYRELVECQDILWRVRFALHIELRRYDNRLTFAHQAQVAEHLGYVGEGNRGVEMMMKEFYRTLRRVAELNKMLLKLFDQAIINGGASEDAEIIDEDFQRRGALIEARKPALFQARPETILDMFLHIANDSSIEGVSPPTLRQLRTARRRLNKFLHTIPEAREKFMALCRHPNALHKAFSLMHKLGVLAAYLPQWSQIVGQMQFDLFHVYTVDEHSIRLLKHINTFSYAENHSKHPICCEVYPRIQKKELLILAAIFHDIGKGRGGDHSVIGEGEAYDFCIEHGLSKPEAKLVSWLVRHHLLMSVTAQRRDIYDPDVITEFAKQVRDEEYLEYLVCLTVADICATNPELWNSWKRTLLAELFYSTQRALRRGLENPVDVRERIRHNQQMASAQLRKEGFSAREIEVLWQRFKADYFLRHTHKQIAWHCENLLRMEDTSKPLVLISKKATRGGTEVFVYSPDQPALFATVVAELDRRNFNVHDAQIMTSKDGYVLDTFMVLDQHGKAIEEGRHSAVTKHITHVLEDGRPTKIKTRRTPNKLQHFNVKTKVDFLPTKSKKRTLMEFVALDTPGLLAKVGRTFADLGINLHAAKITTIGERAEDLFILTSEAGGRLSEEQQTELREKLIEKLSDSVSA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Length
874 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.247 kDa
Sequence
MPLQSPLTFSDEQINIGELKQELEKFSSTQKQEFLNHHPVTSLVLARAEYMDLLLTRLWQYFGFNDIYNISLVAVGGYGRGELHPLSDIDILVLSNNKLPTALEAKISEFITLLWDLKLEVGHAVRTVNECAQIGRDDLTVATNLQEARLLCGSEDTFQALKKVVLSDSFWPSETFYRAKIQEQRERHARYHDTTYNLEPDIKSTPGGLRDIHTLSWVARRHFGATSLLEMSRYGFLTDAEYRELVECQDFLWRVRFALHIELRRYDNRLTFAHQAQVAENLGYVGEGNRGVEMMMKEFYRTLRRVAELNKMLLKLFDQAIINGGATENAEILDADFQRRGSLIEARKPALFQARPETILDMFLHIANDSTIEGVSPPTLRQLRTARRRLNKFLHTIPAAREKFLALCRHPNALHKAFSLMHRLGVMAAYLPQWSQIVGQMQFDLFHAYTVDEHSIRLLKHINTFNNPDNHAKHPICCDIYPRMQKKELLIIAAIFHDIGKGRGGDHSVIGEGEAYDFCIEHGLSKPEAKLVGWLVRHHLLMSVTAQRRDIYDPDVITEFAKQVRDEESLEYLVCLTVADICATNPELWNAWKRTLLAELFYSTQRALRRGLENPVDVRERIRHNQQMASALLRKEGFSARQIEVLWQRFKADYFLRHTHTQIAWHCAHLLRMDDPNKPLVLISKKATRGGTEVFVYTKDQPALFATVVAELDRRNFNVHDAQIMTSKDGHVIDTFMVLDQHGEAIDESRHAAVIKHLTHVLEAGRPTKIKTRRTPNKLQHFNVKTKVDFLPTKGKKHTLMEFVALDTPGLLAKVGRTFADLNINLHGAKITTIGERAEDLFILTSEAGGRLSEEQQNELRDKLIEKLSDAVTA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Vibrio campbellii (strain ATCC BAA-1116 / BB120)
Length
874 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.71 kDa
Sequence
MTLQSPLTFRDEQINIGELKQELEKFSSYQKEEFLQHHPVTNLVLSRAEYMDLLLNRLWQHFGFKDIHNISLVAVGGYGRGELHPLSDIDILILSNNKLPNALEAKISEFITLLWDLRLEVGHAVRTVDECAEIGRADLTVATNLQEARLLCGSEDTFQALKKVVLSDSFWPSETFYRAKIQEQRERHARYHDTTYNLEPDIKSTPGGLRDIHTLSWVARRHFGATSLLEMSRYGFLTDAEYRELVECQDILWRVRFALHIELRRYDNRLTFAHQAQVAEHLGYVGEGNRGVEMMMKEFYRTLRRVAELNKMLLKLFDQAIINGGASEDAEIIDEDFQRRGALIEARKPALFQARPETILDMFLHIANDSSIEGVSPPTLRQLRTARRRLNKFLHTIPEAREKFMALCRHPNALHKAFSLMHKLGVLAAYLPQWSQIVGQMQFDLFHVYTVDEHSIRLLKHINTFSYAENHSKHPICCEVYPRIQKKELLILAAIFHDIGKGRGGDHSVIGEGEAYDFCIEHGLSKPEAKLVSWLVRHHLLMSVTAQRRDIYDPDVITEFAKQVRDEEYLEYLVCLTVADICATNPELWNSWKRTLLAELFYSTQRALRRGLENPVDVRERIRHNQQMASAQLRKEGFSAREIEVLWQRFKADYFLRHTHKQIAWHCENLLRMEDTSKPLVLISKKATRGGTEVFVYSPDQPALFATVVAELDRRNFNVHDAQIMTSKDGYVLDTFMVLDQHGKAIEEGRHSAVTKHITHVLEDGRPTKIKTRRTPNKLQHFNVKTKVDFLPTKSKKRTLMEFVALDTPGLLAKVGRTFADLGINLHAAKITTIGERAEDLFILTSEAGGRLSEEQQTELREKLIEKLSDSVSA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Length
874 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.247 kDa
Sequence
MPLQSPLTFSDEQINIGELKQELEKFSSTQKQEFLNHHPVTSLVLARAEYMDLLLTRLWQYFGFNDIYNISLVAVGGYGRGELHPLSDIDILVLSNNKLPTALEAKISEFITLLWDLKLEVGHAVRTVNECAQIGRDDLTVATNLQEARLLCGSEDTFQALKKVVLSDSFWPSETFYRAKIQEQRERHARYHDTTYNLEPDIKSTPGGLRDIHTLSWVARRHFGATSLLEMSRYGFLTDAEYRELVECQDFLWRVRFALHIELRRYDNRLTFAHQAQVAENLGYVGEGNRGVEMMMKEFYRTLRRVAELNKMLLKLFDQAIINGGATENAEILDADFQRRGSLIEARKPALFQARPETILDMFLHIANDSTIEGVSPPTLRQLRTARRRLNKFLHTIPAAREKFLALCRHPNALHKAFSLMHRLGVMAAYLPQWSQIVGQMQFDLFHAYTVDEHSIRLLKHINTFNNPDNHAKHPICCDIYPRMQKKELLIIAAIFHDIGKGRGGDHSVIGEGEAYDFCIEHGLSKPEAKLVGWLVRHHLLMSVTAQRRDIYDPDVITEFAKQVRDEESLEYLVCLTVADICATNPELWNAWKRTLLAELFYSTQRALRRGLENPVDVRERIRHNQQMASALLRKEGFSARQIEVLWQRFKADYFLRHTHTQIAWHCAHLLRMDDPNKPLVLISKKATRGGTEVFVYTKDQPALFATVVAELDRRNFNVHDAQIMTSKDGHVIDTFMVLDQHGEAIDESRHAAVIKHLTHVLEAGRPTKIKTRRTPNKLQHFNVKTKVDFLPTKGKKHTLMEFVALDTPGLLAKVGRTFADLNINLHGAKITTIGERAEDLFILTSEAGGRLSEEQQNELRDKLIEKLSDAVTA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Photobacterium profundum (strain SS9)
Length
874 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.797 kDa
Sequence
MIDTSTITNPQTLPVEAITQENLRNTLEQFAEQQKQQFIQHRPVTDLVLSRSTFIDKLLIRLWEHYEVNQYPDIALVAVGGYGRGELHPLSDVDILILSAQPLSDETGRIVSKFLTFLWDLRLEVGHSVRTIDDCIEIGNDDLTVATNLTEARILCGSEDVFQCLQERINAGNFWPSEDFYRAKLEEQKTRHARYHDTTYNLEPDIKSSPGGLRDIHTLSWVARRHFGATSLLEMSRFGFLTDAEYRELVECQDSLWRIRFALHIELRRYDNRLTFSHQPSVAENLGYTGEGNRGVEMMMKEFYRTLRRVLELNKMLLQLFDQAILDNGKTVETIQLSDDFQIRGHLIEATKPALFQARPETILDMFLHIAQNGDIEGIAAPTLRQLRTARQRLNVFLVDIPEAREKFMELVRQPNTLQKAFRLMHRHGVLSAYLPQWSQIVGQMQFDLFHVYTVDEHSVRLIKNLNKFNDPENRERHPICCEVYPRIIKKELLTIAAIFHDIAKGRGGDHSELGAIEARKFCIQHGLSRPETNLIAWLVQKHLLMSVTAQRRDIYDPEVVAEFAKEVRDEERLDYLICLTVADICATNQELWNSWKRTLLAELYYSTQKALRRGLENTPDVRDRIRHNQQLSSAILRGKGFAPREIEVLWKRFKADYFLRHTHKQLAWHAEALLTHDHDKPLILLSKKATRGGTEVFVYNKDKAKLFAIVVSELDKKNLSVHDAQIMNSKDGYTLDTFMVLDPSGKTIPENRHNTIRRALVNALTKMKSERKNKRAPRKLMHFNVKTQVDFLPTKTGKKTTMELIALDTPGLLARIGAVFAKQKVSLQAAKITTIGERAEDFFILVNEHGSPLTEEHQQALKEALIIKLTPQD

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Vibrio tasmaniensis (strain LGP32)
Length
873 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.638 kDa
Sequence
MPYQCPITFNDEQLEICELKNQLEIFTQYQKSEFLNHHPVTDLVLLRSEYMDLLLNRLWEHFGFSKLPHIALVAVGGYGRGELHPLSDIDILIVSQRTLPSALGEKVSQFITLLWDLKLEVGHAVRTIAECIEIGSDDLTVATNLQESRLLCGSEDTFQELKLKIHSDSFWPSETFYKAKIQEQRERHARYHDTTYNLEPDIKSTPGGLRDIHTLSWVARRHFGATSLLEMSKYGFLTDAEYRELVECQDFLWRVRFALHIELRRYDNRLTFAHQAQVAEHLGYTGEGNRGVEMMMKEFYRTLRRVAELNKMLLKLFDQAIINGGQTQEAEILDNDFQRRGSLIEARKPALFQARPETILDMFIHIANDSTIEGVSPPTLRQLRTARRRLNRFLHTIPEARDKFMDLVRHPNALHKAFSLMHKLGVLSAYLPQWSQIVGQMQFDLFHVYTVDEHSIRLLKHINRFSQVENHDKHPICCEVYPRVQKKELLILAAIFHDIGKGRGGDHSEIGAVEAYSFCIEHGLSKPEAKQVAWLVQNHLLMSVTAQRRDIYDPDVITEFAKKVRDEESLELLVCLTVADICATNPELWNSWKRTLLAELFHSTQRALRRGLENPVDVRDRIRHNQQMASALLRKEGFSAREIEVLWQRFKADYFLRHTHTQIAWHCEHLLRLEDPSQPLVLISKKATRGGTEVFVYCKDQAALFATVVAELDRRNFNVHDAQVMVSKDGHVLDTFIVLDQHGEAIDEARHKAVAKHLTHVLADGRPTKIKTRRTPRNLQHFKVKTRVEFLPTKSKKRTLMELRALDTPGLLAQVGATFAELDINLHGAKITTIGERAEDLFILTSDAGGRLSEEQEQALRERLTEHVSELAP

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Vibrio vulnificus (strain CMCP6)
Length
873 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
101.03 kDa
Sequence
MAFQSPLTFNDEQLTVAQLKSQLDLFANAQKQAFLNHHPVTDLVLSRAEYMDLLLTRLWRYYGFSEIHNISLVAVGGYGRGELHPLSDIDILVLSKHKLPGELETKLSEFITLLWDLRLEVGHAVRTVEECAAIGREDLTVATNLQEARLLCGSENTFQDLKKVVLSDSFWPSETFYRAKIQEQRERHARYHDTTYNLEPDIKSTPGGLRDIHTLSWVARRHFGATSLLEMSRYGFLTDAEYRELVECQDFLWRVRFALHIELKRYDNRLTFAHQIQVAEHLGFKGEGNRGIEMMMKEFYRTLRRVAELNKMLLKLFDQAIINGGETEPAVIINEDFQRRGRLIEARKPALFQARPETILDMFLHIANDSTIDSVSPPTLRQLRTARRRLNKFLHTIPEAREKFMELVRHPNALHRAFSLMHKLGVLAAYLPQWSQIVGQMQFDLFHVYTVDEHSVRLLNHINTFSYAKNHDKHPICCEVYPRLQKKELLLLAAIFHDIGKGRGGDHSEIGEKEAYDFCIEHGLSKPEAKLVSWLVRHHLLMSVTAQRRDIYDPEVITEFAKQVRDEERLEYLVCLTVADICATNPELWNSWKRTLLAELFYSTQRALRRGLENPVDVRERIRHNQQLASALLRKEGFTAREIEVLWQRFKADYFLRHTHKQIAWHCEHILRMDNPEQPLVLMSKKATRGGTEVFVYTKDQHALFATVVAELDRRNFNVHDAQIMSSKDGYVLDTFMVLDQHGQAIDVDNHKAVIKHLMHVLADGRPTKVKTRRTPYKLQHFKVKTKVDFLPTKSKKRTLMELVALDTPGLLAITGATFADMGFNLHGAKITTIGERAEDLFILTSENGGRLSEEQELQLREKLIHNIAELAP

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Vibrio vulnificus (strain YJ016)
Length
873 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
101.06 kDa
Sequence
MAFQSPLTFNDEQLTVAQLKSQLDLFANAQKQAFLNHHPVTDLVLSRAEYMDLLLTRLWRYYGFSEIHNISLVAVGGYGRGELHPLSDIDILVLSKHKLPGELETKLSEFITLLWDLRLEVGHAVRTVEECAAIGREDLTVATNLQEARLLCGSENTFQDLKKVVLSDSFWPSETFYRAKIQEQRERHARYHDTTYNLEPDIKSTPGGLRDIHTLSWVARRHFGATSLLEMSRYGFLTDAEYRELVECQDFLWRVRFALHIELKRYDNRLTFAHQIQVAEHLGFKGEGNRGIEMMMKEFYRTLRRVAELNKMLLKLFDQAIINGGETEPAVIINEDFQRRGRLIEARKPALFQARPETILDMFLHIANDSTIDSVSPPTLRQLRTARRRLNKFLHTIPEAREKFMELVRHPNALHRAFSLMHKLGVLAAYLPQWSQIVGQMQFDLFHVYTVDEHSVRLLNHINTFSYAKNHDKHPICCEVYPRLQKKELLLLAAIFHDIGKGRGGDHSEIGEKEAYDFCIEHGLSKPEAKLVSWLVRHHLLMSVTAQRRDIYDPEVITEFAKQVRDEERLEYLVCLTVADICATNPELWNSWKRTLLAELFYSTQRALRRGLENPVDVRERIRHNQQLASALLRKEGFTAREIEVLWQRFKADYFLRHTHKQIAWHCEHILRMDNPEQPLVLMSKKATRGGTEVFVYTKDQHALFATVVAELDRRNFNVHDAQIMSSKDGYVLDTFMVLDQHGQAIDVDNHKAVIKHLMHVLTDGRPTKVKTRRTPYKLQHFKVKTKVDFLPTKSKKRTLMELVALDTPGLLAITGATFADMGFNLHGAKITTIGERAEDLFILTSENGGRLSEEQELQLREKLIHNIAELAP

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Vibrio tasmaniensis (strain LGP32)
Length
873 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.638 kDa
Sequence
MPYQCPITFNDEQLEICELKNQLEIFTQYQKSEFLNHHPVTDLVLLRSEYMDLLLNRLWEHFGFSKLPHIALVAVGGYGRGELHPLSDIDILIVSQRTLPSALGEKVSQFITLLWDLKLEVGHAVRTIAECIEIGSDDLTVATNLQESRLLCGSEDTFQELKLKIHSDSFWPSETFYKAKIQEQRERHARYHDTTYNLEPDIKSTPGGLRDIHTLSWVARRHFGATSLLEMSKYGFLTDAEYRELVECQDFLWRVRFALHIELRRYDNRLTFAHQAQVAEHLGYTGEGNRGVEMMMKEFYRTLRRVAELNKMLLKLFDQAIINGGQTQEAEILDNDFQRRGSLIEARKPALFQARPETILDMFIHIANDSTIEGVSPPTLRQLRTARRRLNRFLHTIPEARDKFMDLVRHPNALHKAFSLMHKLGVLSAYLPQWSQIVGQMQFDLFHVYTVDEHSIRLLKHINRFSQVENHDKHPICCEVYPRVQKKELLILAAIFHDIGKGRGGDHSEIGAVEAYSFCIEHGLSKPEAKQVAWLVQNHLLMSVTAQRRDIYDPDVITEFAKKVRDEESLELLVCLTVADICATNPELWNSWKRTLLAELFHSTQRALRRGLENPVDVRDRIRHNQQMASALLRKEGFSAREIEVLWQRFKADYFLRHTHTQIAWHCEHLLRLEDPSQPLVLISKKATRGGTEVFVYCKDQAALFATVVAELDRRNFNVHDAQVMVSKDGHVLDTFIVLDQHGEAIDEARHKAVAKHLTHVLADGRPTKIKTRRTPRNLQHFKVKTRVEFLPTKSKKRTLMELRALDTPGLLAQVGATFAELDINLHGAKITTIGERAEDLFILTSDAGGRLSEEQEQALRERLTEHVSELAP

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Vibrio vulnificus (strain CMCP6)
Length
873 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
101.03 kDa
Sequence
MAFQSPLTFNDEQLTVAQLKSQLDLFANAQKQAFLNHHPVTDLVLSRAEYMDLLLTRLWRYYGFSEIHNISLVAVGGYGRGELHPLSDIDILVLSKHKLPGELETKLSEFITLLWDLRLEVGHAVRTVEECAAIGREDLTVATNLQEARLLCGSENTFQDLKKVVLSDSFWPSETFYRAKIQEQRERHARYHDTTYNLEPDIKSTPGGLRDIHTLSWVARRHFGATSLLEMSRYGFLTDAEYRELVECQDFLWRVRFALHIELKRYDNRLTFAHQIQVAEHLGFKGEGNRGIEMMMKEFYRTLRRVAELNKMLLKLFDQAIINGGETEPAVIINEDFQRRGRLIEARKPALFQARPETILDMFLHIANDSTIDSVSPPTLRQLRTARRRLNKFLHTIPEAREKFMELVRHPNALHRAFSLMHKLGVLAAYLPQWSQIVGQMQFDLFHVYTVDEHSVRLLNHINTFSYAKNHDKHPICCEVYPRLQKKELLLLAAIFHDIGKGRGGDHSEIGEKEAYDFCIEHGLSKPEAKLVSWLVRHHLLMSVTAQRRDIYDPEVITEFAKQVRDEERLEYLVCLTVADICATNPELWNSWKRTLLAELFYSTQRALRRGLENPVDVRERIRHNQQLASALLRKEGFTAREIEVLWQRFKADYFLRHTHKQIAWHCEHILRMDNPEQPLVLMSKKATRGGTEVFVYTKDQHALFATVVAELDRRNFNVHDAQIMSSKDGYVLDTFMVLDQHGQAIDVDNHKAVIKHLMHVLADGRPTKVKTRRTPYKLQHFKVKTKVDFLPTKSKKRTLMELVALDTPGLLAITGATFADMGFNLHGAKITTIGERAEDLFILTSENGGRLSEEQELQLREKLIHNIAELAP

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Vibrio vulnificus (strain YJ016)
Length
873 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
101.06 kDa
Sequence
MAFQSPLTFNDEQLTVAQLKSQLDLFANAQKQAFLNHHPVTDLVLSRAEYMDLLLTRLWRYYGFSEIHNISLVAVGGYGRGELHPLSDIDILVLSKHKLPGELETKLSEFITLLWDLRLEVGHAVRTVEECAAIGREDLTVATNLQEARLLCGSENTFQDLKKVVLSDSFWPSETFYRAKIQEQRERHARYHDTTYNLEPDIKSTPGGLRDIHTLSWVARRHFGATSLLEMSRYGFLTDAEYRELVECQDFLWRVRFALHIELKRYDNRLTFAHQIQVAEHLGFKGEGNRGIEMMMKEFYRTLRRVAELNKMLLKLFDQAIINGGETEPAVIINEDFQRRGRLIEARKPALFQARPETILDMFLHIANDSTIDSVSPPTLRQLRTARRRLNKFLHTIPEAREKFMELVRHPNALHRAFSLMHKLGVLAAYLPQWSQIVGQMQFDLFHVYTVDEHSVRLLNHINTFSYAKNHDKHPICCEVYPRLQKKELLLLAAIFHDIGKGRGGDHSEIGEKEAYDFCIEHGLSKPEAKLVSWLVRHHLLMSVTAQRRDIYDPEVITEFAKQVRDEERLEYLVCLTVADICATNPELWNSWKRTLLAELFYSTQRALRRGLENPVDVRERIRHNQQLASALLRKEGFTAREIEVLWQRFKADYFLRHTHKQIAWHCEHILRMDNPEQPLVLMSKKATRGGTEVFVYTKDQHALFATVVAELDRRNFNVHDAQIMSSKDGYVLDTFMVLDQHGQAIDVDNHKAVIKHLMHVLTDGRPTKVKTRRTPYKLQHFKVKTKVDFLPTKSKKRTLMELVALDTPGLLAITGATFADMGFNLHGAKITTIGERAEDLFILTSENGGRLSEEQELQLREKLIHNIAELAP

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Aliivibrio fischeri (strain ATCC 700601 / ES114)
Length
873 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.599 kDa
Sequence
MKYLSPLSLSDTQLNITELKQQLTLFSQYQINAFHQHKAVSDLVLERSHYFDQLLSRLWQFFKFDDIANTSLIAVGGYGRSELHPLSDIDILILTENNTNDAFCQKVGELVTLLWDLKLEVGHSVRSIAECIEIGQNDLTVATNLQEARYISGNKELSHQLKLKIHSDSFWPSELFYQAKIDEQKKRHSRYHDTTYNLEPDIKSSPGGLRDIHTLSWIARRHFGATSLLEMSQAGFLTDAEYRELLECQEFLWRVRFALHIELKRYDNRLTFGHQASVAEHLGFIGEGNRGVERMMKEFYRTLRRVAELNSMLLKIFDQAILHQGEQDDAIIIDDDFQRRGRLIEARKPALFQARPDTILDMFLLMANDSTIDGVAPPTMRQLRTARRRLNRFLCEIPEAKEKFLQLTQHPNALNNAFSSMHKLGVLSAYLPQWSHIVGQMQFDLFHAYTVDEHSIRLLKHINKFSDTTNRDKHPICCEIFPKIMKKELLIIAAIFHDIAKGRGGDHSELGAVDAYDFCISHGLSKPEANLVSWLVKSHLLMSVTAQRRDIYDPDVITEFAKQVRDEERLDYLVCLTVADICATNPDLWNSWKRSLIADLYNATQRALRRGLENPPDLRDRIRHNQQMASAQLRSEGFTQWEVDALWRRFKADYFLRHTHKQIAWHASHLLRHQDKEKSLILISKNASRGGTEIFVYSKDQPHLFATVAAELDRRSITIYDAQVMSSKDGYALDTFMVLDQNDDPIDEERQQRLIDQLYDVKLNDQATHIKTRRPPRQLQHFNVKTRMEFLPTKTGKRTLMEFVALDTPGLLATVGATFAQLGINLHAAKITTIGERAEDLFILTSDVGGRLDDEKQAELELALVKNVARLSS

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Aliivibrio fischeri (strain MJ11)
Length
873 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.653 kDa
Sequence
MKYLSPLSLSDTQLNITELKQQLTLFSQYQINAFHQHKAVSDLVFERSHYFDQLLSRLWQFFKFDDIANTSLIAVGGYGRSELHPLSDIDILILTENNTNDTFCQKVGELVTLLWDLKLEIGHSVRSIAECIEIGQNDLTVATNLQEARYICGNKELSHQLKLKIHSDSFWPSESFYQAKIDEQKKRHSRYHDTTYNLEPDIKSSPGGLRDIHTLSWIARRHFGATSLLEMSQAGFLTDAEYRELLECQEFLWRVRFALHIELKRYDNRLTFGHQASVAEHLGFIGEGNRGVERMMKEFYRTLRRVAELNSMLLKIFDQAILHQGEQDDAIIIDDDFQRRGRLIEARKPALFQARPDTILDMFLLMANDSTIDGVAPPTMRQLRTARRRLNRFLCEIPEAKEKFLQLTQHPNALNNAFSSMHKLGVLSAYLPQWSHIVGQMQFDLFHAYTVDEHSIRLLKHINKFSDTTNRDKHPICCEIFPKIMKKELLIIAAIFHDIAKGRGGDHSELGAVDAYDFCISHGLSKPEANLVSWLVKSHLLMSVTAQRRDIYDPDVITEFAKQVRDEERLDYLVCLTVADICATNPDLWNSWKRSLIADLYNATQRALRRGLENPPDLRDRIRHNQQMASAQLRSEGFTQWEVDALWRRFKADYFLRHTHKQIAWHASHLLRHQDKEKSLILISKNASRGGTEIFVYSKDQPHLFATVAAELDRRSITIYDAQVMSSKDGYALDTFMVLDQNDDPIDEERQQRLIDQLYDVKLNDQATHIKTRRPPRQLQHFNVKTRMEFLPTKTGKRTLMEFVALDTPGLLATVGATFAQLGINLHAAKITTIGERAEDLFILTSDVGGRLDDDKQAELEIALVKNVARLSS

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pseudoalteromonas haloplanktis (strain TAC 125)
Length
872 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
101.049 kDa
Sequence
MALPNKVKKLLSDAEQLSDYRDCSSYFYKWLFNEFSKQPVGNLINARAEFIDRLLIKLFHVYDLAHEPDLALIAVGGYGRGELHPYSDIDFLLLVTQQPNAEISEKIGQFVTMLWDLNLEIGHSVRTIAQAIEQKREDVTFATSLLESRLIFGNHIEFEKLKNHIIDTPVWRSNEFFLAKVQEQHLRHRKCHGTAYNLEPNIKENPGGLRDLQTIIWVAKKHFRAETLQELISHGYLTHEEFQELSECLENLWNIRFALHLAAGRSENRLLFDHQPQAAEILGFGSDGKSSVERMMKRLFRIMSRVRELNLMLLAYFEQSISPKHHQPIIQELDRNFERIGNQIKVKSPSVFFRRDQLFMLFEHIADNPEITHIYPSTIRTIRQVRRRLLGDLQDYAACREAFLRLIKHPNGMGRAFTLMHKHGMLAAYLPQWRNIFGQMQFDLFHAYTVDEHTHRLINNIYQYFDKTGVSEFPICSEIVTRMDKPELLYLAGIFHDIAKGRGGDHSELGAVDALAFAKLHAFSVADGKLIAWLVSNHLLMSVTAQRKDINDPGVIKDFATRVKTERQLDYLYCLTVADIRATNDNLWNDWKNTLLRELYLHTQHALRLGLENPMDQRDQIRDKKHQAKQRLLNLGYMEDQIDLIWSRFKANYFTAFSEQQISWHSQHLVNSEDLSQPSVIVSNKAMHGGTQVFVYSPYSGPLFARLVSVIGSKKAQIQHAQVLTTKDGYVLFNFVILEVNGEPIASGRAQSIKRALEQALFEPRKKIRFKKNRSQRFKDFNIKPKIVLRPHPRKDRSLIEIQAIDIPGLLTKIAEVFQAHLLHIHAARITTVGQRAEDFFVVSNNEYQALTDEEQAKIHQALRKKLNAETE

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Xanthomonas axonopodis pv. citri (strain 306)
Length
869 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.37 kDa
Sequence
MTDTPAERPDPGVAGDADWAAQARPLLVHVDMRLCKRFDQGEPIERLVALRARAVDQLMRNAWMRCIPADSGLSLHAVGGYGRGELFPRSDVDVLVLGDTAAQQQHEQALARLFALLWDVGLPISHAVRSPAQCTAAAADQTVLTALIESRALVADAQARAALATAIAPPQVWPPRDFFQAKREELLARHQRFGDTADNLEPDIKDGPGGLRDLQTLGWMALRAFGVKDLEALVGLGHVGFDEAAALRREREELARLRFGLHIVANRPEERLRFDYQKTLAERLGFADDPESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQFDGEATPEPLGGGFSLRRGYLAADTESWPDGDVLQVFALFAQWAAHREVRGLHSLTARALAEVLRDLPAYEVADATARERFMALLRGPRAVETLNRMARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADEHFSIAHEVWPRLRKPELLLLAGLFHDIAKGRGGDHSELGAVDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGLEHPPPREERLREARESARTLMQAQGHDDVTIDRQFAGMPDENFLRFRPEQLAWQAASLIEVEIGQTLVKARRAVPDNDALEVFVYSPDRDGLFAAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPQETYADGDPQRLAATLRQVLAGDLQKVRPARRAVPRQLRHFRFAPRVEFSESAGGRRTRISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHDRPLSESARQALRDALCACLDPV

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Xanthomonas campestris pv. vesicatoria (strain 85-10)
Length
869 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.326 kDa
Sequence
MTDTPAERPDPGVAGDADWAAQARPLLVHADMRLCKRFDQGEPIERLVALRARAVDQLMRNAWMRCIPADSGLSLHAVGGYGRGELFPRSDVDVLVLGDTAAQQQHEQALARLFALLWDVGLPISHAVRSPAQCTAAAADQTVLTALIESRALVADGQARAALATAIAPPQVWPPRDFFQAKREELLARHQRFGDTADNLEPDIKDGPGGLRDLQTLGWMALRAFGVKDLEALVGLGHVGFDEAAALRREREELARLRFGLHIVANRPEERLRFDYQKTLAERLGFADDPESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQFDGEATPEPLGGGFSLRRGYLAADAESWPDGDVLQVFALFAQWAAHREVRGLHSLTARALAEVLRDLPAYDIADATARERFMALLRGPRAVETLNRMARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSIAHEVWPRLRKPELLLLAGLFHDIAKGRGGDHSELGAVDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGLEHPPPREERLREARESARTLMQAQGHDDVTIDRQFAGMPDENFLRFRPEQLAWQAASLIEVEIGQTLVKARRAVPDNDALEVFVYSPDRDGLFAAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPQETYADGDPQRLAATLRQVLAGDLHKVRPARRAVPRQLRHFRFAPRVEFSESAGGRRTRISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHDRPLSESARQALRDALCACLDPV

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Xanthomonas campestris pv. campestris (strain 8004)
Length
869 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.246 kDa
Sequence
MTATPADRPDPGVAGDADWAAEARPLLVHADMRLCKRFDQGEPTERLLALRARAVDQLMRNAWTRCIPADAGLSLHAVGGYGRGELFPRSDVDLLVLGETAAQQRHEQALARLFALLWDVGLPISHAVRSPAQCTSAAADQTVLTALIESRPLVADAQARAALAAAIAPQQVWPPRAFFQAKREELHARHQRFGDTADNLEPDIKDGPGGLRDLQTLGWMALRAFGVKDLEALVGLGHVGMDEAAALRREREELARLRYGLHLVANRPEERLRFDYQKTLAERLGFADDPESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQFDGEAVPVQLDAGFSLRRGYLTADADTWPDGDVVQVFALFAQWAAHREVRGLHSLTARALAEVLRDLPAYDVADAIARDRFMALLRGPRAVETLNRMARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSITHEVWPRLRKPELLLLAGLFHDIAKGRGGDHSELGAVDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGLEHPPPREERLREARESARTLMQAQGHDDATIDRQFAGMPDENFLRFRPEQLAWQAASLIEVQIGQTLVKARRAVPDNDALEVFVYSPDRDGLFSAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPQDSSADGDPQRLAAALRQVLAGDLLKVRPSRRAVPRQLRHFRFAPRVEFSESAGGRRTRISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHDRPLPDAARQALRDALCACLDPT

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Xanthomonas campestris pv. campestris (strain B100)
Length
869 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.315 kDa
Sequence
MTATPADRPDPGVAGDADWAAEARPLLVHADMRLCKRFDQGEPTERLLALRARAVDQLMRNAWARCIPADARLSLHAVGGYGRGELFPRSDVDLLVLGETAAQQRHEQALARLFALLWDVGLPISHAVRSPAQCTSAAADQTVLTALIESRPLVADAQARAALAAAIAPQQVWPPRAFFQAKREELHARHQRFGDTADNLEPDIKDGPGGLRDLQTLGWMALRAFGVKDLEALVGLGHVGMDEAAALRREREELARLRYGLHLVANRPEERLRFDYQKTLAERLGFADDPESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQFDGEAVPVQLDAGFSLRRGYLTADADTWPDGDVVQVFALFAQWAAHREVRGLHSLTARALAEVLRDLPAYDVADAIARDRFMALLRGPRAVETLNRMARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSITHEVWPRLRKPELLLLAGLFHDIAKGRGGDHSELGAVDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGLEHPPPREERLREARESARTLMQAQGHDDATIDRQFAGMPDENFLRFRPEQLAWQAASLIEVQIGQTLVKARRAVPDNDALEVFVYSPDRDGLFSAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPQDSSADGDPQRLAAALRQVLAGDLLKVRPSRRAVPRQLRHFRFAPRVEFSESAGGRRTRISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHDRPLPDAARQALRDALCACLDPT

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Length
869 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.246 kDa
Sequence
MTATPADRPDPGVAGDADWAAEARPLLVHADMRLCKRFDQGEPTERLLALRARAVDQLMRNAWTRCIPADAGLSLHAVGGYGRGELFPRSDVDLLVLGETAAQQRHEQALARLFALLWDVGLPISHAVRSPAQCTSAAADQTVLTALIESRPLVADAQARAALAAAIAPQQVWPPRAFFQAKREELHARHQRFGDTADNLEPDIKDGPGGLRDLQTLGWMALRAFGVKDLEALVGLGHVGMDEAAALRREREELARLRYGLHLVANRPEERLRFDYQKTLAERLGFADDPESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQFDGEAVPVQLDAGFSLRRGYLTADADTWPDGDVVQVFALFAQWAAHREVRGLHSLTARALAEVLRDLPAYDVADAIARDRFMALLRGPRAVETLNRMARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSITHEVWPRLRKPELLLLAGLFHDIAKGRGGDHSELGAVDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGLEHPPPREERLREARESARTLMQAQGHDDATIDRQFAGMPDENFLRFRPEQLAWQAASLIEVQIGQTLVKARRAVPDNDALEVFVYSPDRDGLFSAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPQDSSADGDPQRLAAALRQVLAGDLLKVRPSRRAVPRQLRHFRFAPRVEFSESAGGRRTRISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHDRPLPDAARQALRDALCACLDPT

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Xanthomonas oryzae pv. oryzae (strain MAFF 311018)
Length
869 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.35 kDa
Sequence
MTDAPAERPDPSVAGDADWAAQARPLLVHADMRLRKRFDQGEPIERLVALRARAVDQLMRNAWTRCIPADSGLSLHAVGGYGRGELFPRSDVDVLVLGDSVAQQRHEQHLSRLFALLWDVGLPISHAVRSPTQCMVAAADQTVLTALIESRALVADAAARAALAAAIAPQRVWPPRDFFQAKREELLARHQRFGDTADNLEPDIKDGPGGLRDLQTLGCMALRAFGVKDVEALVGLGHVGCDEAAALRREREELARLRFGLHIVANRPEERLRFDYQKTLAERLGFADDLESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQFDGEATPESLGGGFSLRRGYLAADSDSWPGDDVLQVFALFVHWAAHREVRGLHSLTARALAEVLREFPAYDVADATARELFMALLRGTRAVETLNRMARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSIAHEVWPRLRKPELLLLAGLFHDIAKGRGGDHSELGAVDTRAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGVEHPPPREERLREARESARALMQAQGHDDATIDRQFAGMPDENFLRFRPEQLAWQAASLIEVEIAQTLVKARRAVPDNDALEVFVYSPDRDGLFAAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPRDTYADGDPQRLAATLRQVLAGDLQQVRPARRAVPGQLRHFRFAPRVEFSESADGRRTRISLVAPDRPGLLADVAHVLRVQHLRVHDARIATFGERAEDQFQITDEHDRPLSESARQALRDALCACLDPV

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)
Length
869 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.35 kDa
Sequence
MTDAPAERPDPSVAGDADWAAQARPLLVHADMRLRKRFDQGEPIERLVALRARAVDQLMRNAWTRCIPADSGLSLHAVGGYGRGELFPRSDVDVLVLGDSVAQQRHEQHLSRLFALLWDVGLPISHAVRSPTQCMVAAADQTVLTALIESRALVADAAARAALAAAIAPQRVWPPRDFFQAKREELLARHQRFGDTADNLEPDIKDGPGGLRDLQTLGCMALRAFGVKDVEALVGLGHVGCDEAAALRREREELARLRFGLHIVANRPEERLRFDYQKTLAERLGFADDLESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQFDGEATPESLGGGFSLRRGYLAADSDSWPGDDVLQVFALFVHWAAHREVRGLHSLTARALAEVLREFPAYDVADATARELFMALLRGTRAVETLNRMARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSIAHEVWPRLRKPELLLLAGLFHDIAKGRGGDHSELGAVDTRAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGVEHPPPREERLREARESARALMQAQGHDDATIDRQFAGMPDENFLRFRPEQLAWQAASLIEVEIAQTLVKARRAVPDNDALEVFVYSPDRDGLFAAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPRDTYADGDPQRLAATLRQVLAGDLQQVRPARRAVPGQLRHFRFAPRVEFSESADGRRTRISLVAPDRPGLLADVAHVLRVQHLRVHDARIATFGERAEDQFQITDEHDRPLSESARQALRDALCACLDPV

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Xanthomonas axonopodis pv. citri (strain 306)
Length
869 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.37 kDa
Sequence
MTDTPAERPDPGVAGDADWAAQARPLLVHVDMRLCKRFDQGEPIERLVALRARAVDQLMRNAWMRCIPADSGLSLHAVGGYGRGELFPRSDVDVLVLGDTAAQQQHEQALARLFALLWDVGLPISHAVRSPAQCTAAAADQTVLTALIESRALVADAQARAALATAIAPPQVWPPRDFFQAKREELLARHQRFGDTADNLEPDIKDGPGGLRDLQTLGWMALRAFGVKDLEALVGLGHVGFDEAAALRREREELARLRFGLHIVANRPEERLRFDYQKTLAERLGFADDPESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQFDGEATPEPLGGGFSLRRGYLAADTESWPDGDVLQVFALFAQWAAHREVRGLHSLTARALAEVLRDLPAYEVADATARERFMALLRGPRAVETLNRMARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADEHFSIAHEVWPRLRKPELLLLAGLFHDIAKGRGGDHSELGAVDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGLEHPPPREERLREARESARTLMQAQGHDDVTIDRQFAGMPDENFLRFRPEQLAWQAASLIEVEIGQTLVKARRAVPDNDALEVFVYSPDRDGLFAAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPQETYADGDPQRLAATLRQVLAGDLQKVRPARRAVPRQLRHFRFAPRVEFSESAGGRRTRISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHDRPLSESARQALRDALCACLDPV

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Xanthomonas campestris pv. vesicatoria (strain 85-10)
Length
869 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.326 kDa
Sequence
MTDTPAERPDPGVAGDADWAAQARPLLVHADMRLCKRFDQGEPIERLVALRARAVDQLMRNAWMRCIPADSGLSLHAVGGYGRGELFPRSDVDVLVLGDTAAQQQHEQALARLFALLWDVGLPISHAVRSPAQCTAAAADQTVLTALIESRALVADGQARAALATAIAPPQVWPPRDFFQAKREELLARHQRFGDTADNLEPDIKDGPGGLRDLQTLGWMALRAFGVKDLEALVGLGHVGFDEAAALRREREELARLRFGLHIVANRPEERLRFDYQKTLAERLGFADDPESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQFDGEATPEPLGGGFSLRRGYLAADAESWPDGDVLQVFALFAQWAAHREVRGLHSLTARALAEVLRDLPAYDIADATARERFMALLRGPRAVETLNRMARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSIAHEVWPRLRKPELLLLAGLFHDIAKGRGGDHSELGAVDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGLEHPPPREERLREARESARTLMQAQGHDDVTIDRQFAGMPDENFLRFRPEQLAWQAASLIEVEIGQTLVKARRAVPDNDALEVFVYSPDRDGLFAAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPQETYADGDPQRLAATLRQVLAGDLHKVRPARRAVPRQLRHFRFAPRVEFSESAGGRRTRISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHDRPLSESARQALRDALCACLDPV

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Xanthomonas campestris pv. campestris (strain 8004)
Length
869 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.246 kDa
Sequence
MTATPADRPDPGVAGDADWAAEARPLLVHADMRLCKRFDQGEPTERLLALRARAVDQLMRNAWTRCIPADAGLSLHAVGGYGRGELFPRSDVDLLVLGETAAQQRHEQALARLFALLWDVGLPISHAVRSPAQCTSAAADQTVLTALIESRPLVADAQARAALAAAIAPQQVWPPRAFFQAKREELHARHQRFGDTADNLEPDIKDGPGGLRDLQTLGWMALRAFGVKDLEALVGLGHVGMDEAAALRREREELARLRYGLHLVANRPEERLRFDYQKTLAERLGFADDPESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQFDGEAVPVQLDAGFSLRRGYLTADADTWPDGDVVQVFALFAQWAAHREVRGLHSLTARALAEVLRDLPAYDVADAIARDRFMALLRGPRAVETLNRMARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSITHEVWPRLRKPELLLLAGLFHDIAKGRGGDHSELGAVDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGLEHPPPREERLREARESARTLMQAQGHDDATIDRQFAGMPDENFLRFRPEQLAWQAASLIEVQIGQTLVKARRAVPDNDALEVFVYSPDRDGLFSAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPQDSSADGDPQRLAAALRQVLAGDLLKVRPSRRAVPRQLRHFRFAPRVEFSESAGGRRTRISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHDRPLPDAARQALRDALCACLDPT

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Xanthomonas campestris pv. campestris (strain B100)
Length
869 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.315 kDa
Sequence
MTATPADRPDPGVAGDADWAAEARPLLVHADMRLCKRFDQGEPTERLLALRARAVDQLMRNAWARCIPADARLSLHAVGGYGRGELFPRSDVDLLVLGETAAQQRHEQALARLFALLWDVGLPISHAVRSPAQCTSAAADQTVLTALIESRPLVADAQARAALAAAIAPQQVWPPRAFFQAKREELHARHQRFGDTADNLEPDIKDGPGGLRDLQTLGWMALRAFGVKDLEALVGLGHVGMDEAAALRREREELARLRYGLHLVANRPEERLRFDYQKTLAERLGFADDPESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQFDGEAVPVQLDAGFSLRRGYLTADADTWPDGDVVQVFALFAQWAAHREVRGLHSLTARALAEVLRDLPAYDVADAIARDRFMALLRGPRAVETLNRMARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSITHEVWPRLRKPELLLLAGLFHDIAKGRGGDHSELGAVDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGLEHPPPREERLREARESARTLMQAQGHDDATIDRQFAGMPDENFLRFRPEQLAWQAASLIEVQIGQTLVKARRAVPDNDALEVFVYSPDRDGLFSAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPQDSSADGDPQRLAAALRQVLAGDLLKVRPSRRAVPRQLRHFRFAPRVEFSESAGGRRTRISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHDRPLPDAARQALRDALCACLDPT

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Length
869 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.246 kDa
Sequence
MTATPADRPDPGVAGDADWAAEARPLLVHADMRLCKRFDQGEPTERLLALRARAVDQLMRNAWTRCIPADAGLSLHAVGGYGRGELFPRSDVDLLVLGETAAQQRHEQALARLFALLWDVGLPISHAVRSPAQCTSAAADQTVLTALIESRPLVADAQARAALAAAIAPQQVWPPRAFFQAKREELHARHQRFGDTADNLEPDIKDGPGGLRDLQTLGWMALRAFGVKDLEALVGLGHVGMDEAAALRREREELARLRYGLHLVANRPEERLRFDYQKTLAERLGFADDPESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQFDGEAVPVQLDAGFSLRRGYLTADADTWPDGDVVQVFALFAQWAAHREVRGLHSLTARALAEVLRDLPAYDVADAIARDRFMALLRGPRAVETLNRMARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSITHEVWPRLRKPELLLLAGLFHDIAKGRGGDHSELGAVDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGLEHPPPREERLREARESARTLMQAQGHDDATIDRQFAGMPDENFLRFRPEQLAWQAASLIEVQIGQTLVKARRAVPDNDALEVFVYSPDRDGLFSAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPQDSSADGDPQRLAAALRQVLAGDLLKVRPSRRAVPRQLRHFRFAPRVEFSESAGGRRTRISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHDRPLPDAARQALRDALCACLDPT

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Xanthomonas oryzae pv. oryzae (strain MAFF 311018)
Length
869 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.35 kDa
Sequence
MTDAPAERPDPSVAGDADWAAQARPLLVHADMRLRKRFDQGEPIERLVALRARAVDQLMRNAWTRCIPADSGLSLHAVGGYGRGELFPRSDVDVLVLGDSVAQQRHEQHLSRLFALLWDVGLPISHAVRSPTQCMVAAADQTVLTALIESRALVADAAARAALAAAIAPQRVWPPRDFFQAKREELLARHQRFGDTADNLEPDIKDGPGGLRDLQTLGCMALRAFGVKDVEALVGLGHVGCDEAAALRREREELARLRFGLHIVANRPEERLRFDYQKTLAERLGFADDLESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQFDGEATPESLGGGFSLRRGYLAADSDSWPGDDVLQVFALFVHWAAHREVRGLHSLTARALAEVLREFPAYDVADATARELFMALLRGTRAVETLNRMARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSIAHEVWPRLRKPELLLLAGLFHDIAKGRGGDHSELGAVDTRAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGVEHPPPREERLREARESARALMQAQGHDDATIDRQFAGMPDENFLRFRPEQLAWQAASLIEVEIAQTLVKARRAVPDNDALEVFVYSPDRDGLFAAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPRDTYADGDPQRLAATLRQVLAGDLQQVRPARRAVPGQLRHFRFAPRVEFSESADGRRTRISLVAPDRPGLLADVAHVLRVQHLRVHDARIATFGERAEDQFQITDEHDRPLSESARQALRDALCACLDPV

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)
Length
869 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.35 kDa
Sequence
MTDAPAERPDPSVAGDADWAAQARPLLVHADMRLRKRFDQGEPIERLVALRARAVDQLMRNAWTRCIPADSGLSLHAVGGYGRGELFPRSDVDVLVLGDSVAQQRHEQHLSRLFALLWDVGLPISHAVRSPTQCMVAAADQTVLTALIESRALVADAAARAALAAAIAPQRVWPPRDFFQAKREELLARHQRFGDTADNLEPDIKDGPGGLRDLQTLGCMALRAFGVKDVEALVGLGHVGCDEAAALRREREELARLRFGLHIVANRPEERLRFDYQKTLAERLGFADDLESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQFDGEATPESLGGGFSLRRGYLAADSDSWPGDDVLQVFALFVHWAAHREVRGLHSLTARALAEVLREFPAYDVADATARELFMALLRGTRAVETLNRMARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSIAHEVWPRLRKPELLLLAGLFHDIAKGRGGDHSELGAVDTRAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGVEHPPPREERLREARESARALMQAQGHDDATIDRQFAGMPDENFLRFRPEQLAWQAASLIEVEIAQTLVKARRAVPDNDALEVFVYSPDRDGLFAAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPRDTYADGDPQRLAATLRQVLAGDLQQVRPARRAVPGQLRHFRFAPRVEFSESADGRRTRISLVAPDRPGLLADVAHVLRVQHLRVHDARIATFGERAEDQFQITDEHDRPLSESARQALRDALCACLDPV

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Cupriavidus necator (strain JMP 134 / LMG 1197)
Length
869 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
98.722 kDa
Sequence
MPTNLPALPMDTTPELLLAARVRDQLKADKQALFADFDLSSHVGTLVTRLRRAVDAALAEAWRGLDMPADAALVAVGGYGRGELFPYSDVDVLLLLRAEPDADTVSRLERFIGMCWDLGLEIGSSVRTVEDCIREARADITIQTSLLEARLLTGNRKLFEALRTQHQADLDPAAFFQAKLLEMRQRHAKYQDTPYALEPNCKESPGGLRDLQVILWMTKAAGLGDSWKELFERGLLTQREAQELSRNERLLKTIRARLHLVAGRRQDVLVFDLQTALAESFGYRQNANKRASEQLMRRYFWAAKAVTQLNSVLLLNIEALLFPSESQVTRVINERFVERQGMLEITSDSLYEDDPHAILETFLLYERTPGIKGLSPRTLRGLYNARTVMDARWRSDPENRRLFLAILQEPQGITHALRLMNQTSVLGRYLINFRRIVGQMQHDLFHVYTVDQHILMVVRNMRRFAIVEHTHEFPFCSQLMASFDKPWVLSVAALFHDIAKGRGGDHSKLGTVDARRFCKQHGIGREDADLICWLVEHHLTMSHVAQKQDLTDPDVVHAFARVVGDERHLTALYLLTVADVRGTSPKVWNAWKGKLLEDLYRITLRVLGGARVDPHSIWAQRQEETISQLRLKAFDPELGKPLWAQLDVAFFLRHDSRDIAWLTRHLFNKVDSPVPVVKARISPAGEGLQVAVYVKDQPDLFARICGYFERKAFSIQDAKIHTTRHGYALDTFQVTDPGLADDGGNYRDILALVEHELGDRLQQQAALPEPSQGRLSRQSRSFPIKPRVDLRPDERGQYYLLSLSANDRTGLLYAITRVLAKHRVSVHTARINTLGERVEDVFLVDGSRLAADNRLQIQLEQDLLAALEI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
Length
865 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
98.483 kDa
Sequence
MPHVDLNPLKQRMQAARAAAVAQFRQHPRPDMLLTELRRIVDQALRELVKLCPLPAGATLAAVGGYGRGELYPHSDVDLLILLPQPPSAADARAVEALVAALWDLGLEPGHSVRTLEDCEREARGDITVETALLESRWLAGSRTLMKRLDSAMQARLDAAVFFQAKRVEMQQRHARYQDTPYALEPNCKESPGGLRDLQVILWMARAAGFGHSWREVAQAGLLTSSEARDLRRAEQAFKRLRIELHLLTGRREDRVLFDLQPGLAAVYGIASTATRRASELLMQRYYWAARLVTQLNVILVQNIEERLFPRPDSDARLIDDDFRNLRERLDIVREDGFERNPTLLLRAFLVMQQHPELIGMSARTLRAIWHSRHRIDAQFRRNPVNRKLFLQILQQPRGIVHELRRMTMLNILPRYLPVFRRIVGQMQHDLFHVYTVDQHTLAVVRNLRRFTMPEHAQEYPLASQLIAGLDRHWLLYVAALFHDIAKGRGGDHSELGAREVRRFAQDHGLDPADAELVEFLVRHHLLMSAVAQKRDLSDPQVVRDFAAQVGDERRLAALYLLTVADIRGTSPRVWNAWKGKLLEDLFRLTLAALGGAHADAHTVLTERKDEAARLTRLAGLRDDAREAFWNQLDIAYFLRHDASEIAWHTRHLYYQVAPDEPVVRVRPTEHGEGLQVMVYTRDAPDLFVTTCGYFDAKSLSVQDARVHTTRHGWALDSFIVLAPEGFADLRAQATLVEHELAERLRDPHAARHAHAPRRLPHSHARRSRVFPVMPQAELSPDERSQSWRLSVTATDRPGLLYALARVFAEHGVDLIMAKIMTLGERVEDVFIVSGSALERPRSQMQFERAILDALAGDEPRQQAA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Length
865 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
98.453 kDa
Sequence
MPHVDLNPLKQRMQAARAAAVAQFRQHPRPDMLLTELRRIVDQALRELVKLCPLPAGATLAAVGGYGRGELYPHSDVDLLILLPQPPSAADARAVEALVAALWDLGLEPGHSVRTLEDCEREARGDITVETALLESRWLAGSRTLMKRLDSAMQARLDAAVFFQAKRVEMQQRHARYQDTPYALEPNCKESPGGLRDLQVILWMARAAGFGHSWREVAQAGLLTSSEARDLRRAEQAFKRLRIELHLLTGRREDRVLFDLQPGLAAVYGIASTATRRASELLMQRYYWAARLVTQLNVILVQNIEERLFPRPDSDARLIDDDFRNLRERLDIVREDGFERNPTLLLRAFLVMQQHPELIGMSARTLRAIWHSRHRIDAQFRRNPVNRKLFLQILQQPRGIVHELRRMTMLNILPRYLPVFRRIVGQMQHDLFHVYTVDQHTLAVVRNLRRFTMPEHAQEYPLASQLIAGLDRHWLLYVAALFHDIAKGRGGDHSELGAREVRRFAQDHGLDPADAELVEFLVRHHLLMSAVAQKRDLSDPQVVRDFAAQVGDERRLAALYLLTVADIRGTSPRVWNAWKGKLLEDLFRLALAALGGAHADAHTVLTERKDEAARLTRLAGLRDDAREAFWNQLDIAYFLRHDASEIAWHTRHLYYQVAPDEPVVRVRPTEHGEGLQVMVYTRDAPDLFVTTCGYFDAKSLSVQDARVHTTRHGWALDSFIVLAPEGFADLRAQATLVEHELAERLRDPHAARHAHAPRRLPHSHARRSRVFPVMPQAELSPDERSQSWRLSVTATDRPGLLYALARVFAEHGVDLIMAKIMTLGERVEDVFIVSGSALERPRSQMQFERAILDALAGDEPRQQAA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Length
865 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
98.524 kDa
Sequence
MPHVDLNPLKQRMQAARAAAVAQFRQHPRPDMLLTELRRIVDQALRELVKLCPLPAGATLAAVGSYGRGELYPHSDVDLLILLPQPPSAADARAVEALVAALWDLGLEPGHSVRTLEDCEREARGDITVETALLESRWLAGSRTLMKRLDSAMQARLDAAVFFQAKRVEMQQRHAHYQDTPYALEPNCKESPGGLRDLQVILWMARAAGFGHSWREVAQAGLLTSSEARDLRRAEQAFKRLRIELHLLTGRREDRVLFDLQPGLAAVYGIASTATRRASELLMQRYYWAARLVTQLNVILVQNIEERLFPRPDSDARLIDDDFRNLRERLDIVREDGFERNPTLLLRAFLVMQQHPELIGMSARTLRAIWHSRHRIDAQFRRNPVNRKLFLQILQQPRGIVHELRRMTMLNILPRYLPVFRRIVGQMQHDLFHVYTVDQHTLAVVRNLRRFTMPEHAQEYPLASQLIAGLDRHWLLYVAALFHDIAKGRGGDHSELGAREVRRFAQDHGLDPTDAELVEFLVRHHLLMSAVAQKRDLSDPQVVRDFAAQVGDERRLAALYLLTVADIRGTSPRVWNAWKGKLLEDLFRLTLAALGGAHADAHTVLTERKDEAARLTRLAGLRDDAREAFWNQLDIAYFLRHDASEIAWHTRHLYYQVAPDEPVVRVRPTEHGEGLQVMVYTRDAPDLFVTTCGYFDAKSLSVQDARVHTTRHGWALDSFIVLAPEGFADLRAQATLVEHELAERLRDPHAARHAHAPRRLPHSHARRSRVFPVMPQAELSPDERSQSWRLSVTATDRPGLLYALARVFAEHGVDLIMAKIMTLGERVEDVFIVSGSALERPRSQMQFERAILDALAGDEPRQQAA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Pasteurella multocida (strain Pm70)
Length
864 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.736 kDa
Sequence
MLFPYFPLSELDVSAVRTQKENLKQFELTQFAHYEIYDLITNRTQFCDHLLRDLWLRFGLVKDNTLTLIAVGGYGREEMFPLSDLDFLILTSEQVEAQTEQKIRQFVQFLWDCGFDVGHAVRTLSECEQAGRDNITVATNLLEARYLEGNFSQFQQLDNVLQKADFWPREAFFQAKYQERVERYQRYHNTSYNLEPDIKHSPGGLRDLHLLYWIALRHTGAKNLTDILNSGFIYPQEYAQLLESQQFLFKVRFALHLILKRYDNRLLFERQIRVAELLEFVGPGNQGVEKMMKSFFQALQTISLLSDLLVKHYREHFLQTNEPVQVRLLDKEFQCVNNAICLRQANLFVEQPEQILSLFFHLTQDHQLDIHSSTLRQLHLALEQRSGYLSELPVARERFLRLFNQPGAIARALVPMHKYGVLKAYLPQWHHIEGLMQFDLFHCYTVDEHIVRTLLKLEYFLEAESVVPHPICSQIFSRLTDRTLLYIAALFHDIAKGRGGDHAELGAVDVAQFAQQHGFDQREIHTLTWLVEQHLLMSVTAQRRDIHDPEVVLHFAEAVQNNVRLDYLTCLTVADICATNETLWNSWKRTLIATLYQFTTQQFAQGMDCLLDHAEKIENHRQQALTLLTQNSLLSAVQIEEIWQHCPEEYFLRNTPKQIAWHTELLADNQTELLVKISNRFSEGGTEIFVYCQDQPNLFHKVVTTIGAKKFSIHDAQIITSHDGYVFDSFIITELDGKLVKFDRRRSLEKALMQALNTSKLPTFRATDNPKLQHFHVKTEVRFLKEQRTDQTEMELFALDQTGLLAKVSQVFSELKLNLLNAKITTIGEKAEDFFILTNSEDRALTAEQRQCLTQRLHEVLEPK

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Haemophilus influenzae (strain 86-028NP)
Length
863 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.122 kDa
Sequence
MLFSPTLSSPLTPSAVKIERENLKQFELENFSRYSIFELIENRCDFYDALLIQLWQEIELSEQLGIALIAVGGYGRREMFPLSDLDFLILVEQTPSPEIEEKITQFIQFLWDCGFEVGNSVRTLEQCESEGKQDITIATNLLEARFLAGNRPHFDALNELVKRADFWSKEDFFNAKVQEQIERYQRYHNTAYNLEPDIKYSPGGLRDLHLLYWVALRHSGALTLEAILQSGFIYPQEYQQLQESRAFLFKVRFALHLILKRYDNRLLFDRQIKVSELLGFRGEGNPAVEKMMKCFFQALHRISLISNLLIQHYRENVLPSNQDTVIDQLDDDFQLINQCLCLRNSFVFQEKPARILDLFFYLTQYEHANIHSDTLRQLQISLDQLSQKLCEIPAAREKFLRLFNQPNAIKRAFMPMHQYGVLTAYLPQWQAIEGLMQFDLFHIYTVDEHTLRVMLKLESFLSQESAQEHPIAHRIFSQLSDRTLLYIAALFHDIAKGRGGDHAELGAVDIADFAQLHGLDRREIDTLAWLVKSHLLMSITAQRRDIHDPEVVMNFAEAVQNQVRLDYLTCLTVADICATNGNLWNSWKRSLFASLYEFTGRQFSQGMKELLDYSEKSAENRKLAQQILMRDYSDITPISIEQLWARCPEDYFVRNTPKQIAWHTSLLVDFVEALLVKISNRFSLGGTEVFIYCQDQPHLFNKVVSTIGAKKFSIHDAQIITTQDGYVFDSFIITELNGELVEFDRRRELEQALTLALQSEKLPALSIVPNRQLQHFTVQTDVRFLQENKKEHTQMELVALDKAGLLAQVSQIFTELNLNLLNAKITTVGEKAEDFFILTNQFGQALDSQQREILRNVLYRNIG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Haemophilus influenzae (strain PittEE)
Length
863 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.197 kDa
Sequence
MLFPLSLSSPLTPSAVKIERENLKQFELENFSRYSIFELVENRSDFYDALLIQLWQEMGLSEQLGISLIAVGGYGRREMFPLSDLDFLILVEQTPIPEIEEKITQFIQFLWDCGFEVGHSVRTLQQCESEGKQDITIATNLLEARFLIGNRPHFDALNELVKRADFWSKEGFFNAKVQEQIERYQRYHNTAYNLEPDIKYSPGGLRDLHLLYWVALHHSGAQTLEDILQSGFIYPQEYQQLQESRAFLFKVRFALHLILTRYDNRLLFDRQIKVSELLGFRGEGNQAVEKMMKCFFQALHRISLISNLLIQHYRENVLSSNQATVIEQLDDDFQLINQCLCLRNSLVFQEKPARILDLFFYLTQYEQANIHSDTLRQLQISLEQLPQKLCEIPEAREKFLRLFNQPNSIKRAFMPMHQYGVLTAYLPQWQAIEGLMQFDLFHIYTVDEHTLRVMLKLESFLSQESAQEHPIAHRIFSQLSDRTLLYIAALFHDIAKGRGGDHAELGAKDVANFARLHGLDRREIDTLAWLVQSHLLMSITAQRRDIHDPEVVMNFAEAVQNQVRLDYLTCLTVADICATNGNLWNSWKRSLFASLYEFTEQQFAQGMKELLDYSEKSAENRKLAQQILTQDYSDIMPISIDQLWERCPEDYFVRNTPKQIAWHTSLLVDLVEALLVKISNRFSLGGTEVFIYCQDQPHLFNKVVSTIGAKKFSIHDAQIITTQDGYVFDSFIITELNGELVEFDRRRELEQALTLALQSEKLSALSITPNRQLQHFTVQTDVRFLHENKKEHTEMELVALDKAGLLAQVSQIFSELNLNLLNAKITTVGEKAEDFFILTNQFGQALDSQQREILRNVLYRNIG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Length
863 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.173 kDa
Sequence
MLFSPTLSSLLTPSAVKIERENLKQFELENFSCYSIFELIENRCDFYDALLIQLWQEIGLSEQQGISLIAVGGYGRREMFPLSDLDFLILVEQTPSHEIEEKITQFIQFLWDCGFEVGNSVRTLEQCELEGKQDITIATNLLEARFLTGNRPHFDVLNELVKRADFWSKEDFFNAKVQEQIERYQRYHNTAYNLEPDIKFSPGGLRDLHLLYWVALRHSGALTLEAILQSGFIYPQEYQQLQESRAFLFKVRFALHLILKRYDNRLLFDRQIKVSELLGFRGEGNPAVEKMMKCFFQALHRISLISNLLIQHYRENVLSSNQDTVIDQLDDDFQLINQSLCLRNSFVFQEKPARILDLFFYLTQYEHVNIHSDTLRQLQISLEQLSQKLCEIPAAREKFLRLFNQSNAIKRAFMPMHQYGVLTAYLPQWQAIEGLMQFDLFHIYTVDEHTLRVMLKLESFLPKGSAQEHPIAHRIFSQLSDRTLLYIAALFHDIAKGRGGDHAELGAEDVADFAQLHGLDRREIDTLAWLVQSHLLMSITAQRRDIHDPEVVMNFAEAMQNQVRLDYLTCLTVADICATNGNLWNSWKRSLFASLYEFTEQQFSQGMKELLDYSEKSAENRKLAQQILTQDYSDITSISIEKLWTRCPEDYFVRNTPKQIAWHTSLLVDFVEALLVKISNRFSLGGTEVFIYCQDQPHLFNKVVSTIGAKKFSIHDAQIITTQDGYVFDSFIITELNGELVEFDRRRELEQALTVALQSEKLPALSIVPNRQLQHFTVQTDVRFLQENKKEHTEMELVALDKAGLLAQVSQIFTELNLNLLNAKITTVGEKAEDFFILTNQFGQALAREERERLNSVIIQQIR

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Aromatoleum aromaticum (strain EbN1)
Length
862 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
98.195 kDa
Sequence
MSTAAIPTDAAVQAAIAEARARLADGSMRIRMAYEGHPATSTVLKGRAHLVDETIHRLWRACAMPADVALLAVGGYGRGELFPCSDVDLMVLLPDTADDAMQARLSVLLGALWDVGLEIGHSARTVAEAIDAAEQDITVQTNLLESRLLEGNRPLFEEFCRRYRALLDVRVFFKAKQLEQEKRYARYNDTPYALEPNCKESPGGLRDLQMLGWIARAAGLGRNWRDLARRRLITGAEARDLRSIERFLQHVRIRLHYLTGRSEDRLLFDYQERLASALGIEATAAKRASEVFMQRYYVNAKKVTQTNTILLQNYGVEIFPRRAGAAIVINERFQAVRELLDMREDDTFARHPSALLECFLILQQRSELKGMTARTLRALWLNRKRINAAFRADPHNRELFVAILQQKRGIVHEFRRMNQYGILSGYLPSWRRIVGQMQHDLFHVYTVDQHIMMVLRNMRRFTMGEHAHEYPLMAQLIMAFDRHWLLYVAALFHDIAKGRGGDHSKLGTIDAREFCEHHHLAREDADLVVWLVEHHLTMSHVAQKEDTSDPAVIGRFADTVGTERRLTALYLLTHADIRGTSPKVWNGWKGKLLEDLFFATRRLLRGATPQEALGLDDRQENARALLRYHGLRPGVEDALWAQLDAVYFMRHSAEEIAWHSRTLYYRPDALEPVVKARVSDADQGVQVMVFTRDQKDLFVRLTGFFGRLGFSILDAKVHTTRHGYALDSFMLQDPGNAEHYRDVITLIEHELTERLKKSAPPDRPSAGRLSRQVKHFPITPRVSILPDESGRHYILSLTAADRRGLLFAVAEVLAQNGIVLHTAKIATLGERVEDTFLLSGNGLSQDARVVKIERELLQRLHI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Shewanella oneidensis (strain MR-1)
Length
861 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
98.32 kDa
Sequence
MNTALLAKQSLIEQNQTLLARFKAKTPIEELVTQRCQFVDSLVKQAWQQHGLDQYPIALIAVGGYGRGELHPHSDVDLLFLFEGELSKAAETTLSEFIAFLWDANLEIGHSVRTLDDTLRLGRDDITIATNLLEARLLTGPETLFDQLYDAIRQSDFWTSSNFFIAKRDEQTARHAKASAFDLEPNIKSCPGGLRDIQTIAWVAMRHFGASRLEELVEYEFLEPAELEELLECQHFLWKLRFALHMAVGRDENRLLFDVQRQVAELMGYEDATQLAVEQMMKRYYRTVRRVMELNEMLLQLFKRATLGHTKALEIQAIDDNYQRRGAFIEALSDDLFDSGEEIVRLFVHIAKNSNIKGIYAPTLRSLRRARRAQLQPLQENPLCRQAFMEILKHPRGIAALSLMHKHGVLSAYLPAWRNIEGQMQFDLFHAYTVDEHTHRLLLNIERFSQPEQKEEFPLGSVLINQLPKKGLLVLGAIFHDIAKGRGGDHSKLGSSDALAFCKLHGLNDHDGRLVAWLVENHLVMSVTAQRRDISDPDVVADFASKVRDAVHLSYLYCLTVADICATNEKTWNNWKGSLLRDLYFSTQRVLARGKEKPVDIRARVREYQAKAKKELLRRGIKEKDLDTLWQRFKADYFLRHQPNQVAWHAEAILKHKQVDEPLVLVSKHTTRGGTELFVYCQDRPKLFATVMAVLDNKNINVHDANIMTSKDNYALDTFVILEQDGEPVSQLSRIQSIRKALEKALASDNPKLPRFRKLSRKMKPFNVPTQVSFLESNRHGTSMMELIALDTPGLLAKVGDIFYRCNTTLLSAKITTIGERAEDFFILQTNDGLQLNETQEHTLKEALISALSAINTESTN

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Ralstonia solanacearum (strain GMI1000)
Length
861 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.493 kDa
Sequence
MHTAAAATPATSPRDILKAERAHLFAQFEQHANVNLLVTKLARAVDQALILLWQDEGMPDTCALVAVGGYGRGELFPHSDVDILLLLPQTADKALETRLEAFIGHCWDMGLDIGSSVRTVDECISEATQDVTVCTSLLEARLLTGDEGLYRTFETHYQGHLDAADFYQSKMLEMRQRHAKYQDTPYSLEPNCKESPGGLRDLQVILWMTRAAGFGSSWNELLVNQLLTRREAKELAANERLLKTIRARLHLLAGRRQDVLVFDLQTQLGEAFGYRPNAAKRTSEQLMRRYYWAAKAVTQLNTVVLQNIEARLFPTELGITRTINGRFVERQGMLEIADPELYQREPAAILETFLVYEQTRGVKGLAANTLRALYNARTQMDARWRRDPANRATFLSILQQPQGITHALRLMNQTSVLGRYLVNFRRIVGQMQHDLFHVYTVDQHILMVVRNVRRFAIVEHAHEFPFCSQLMANFDKPWVLTVAALFHDIAKGRGGDHSVLGMADARRFCKQHGIASEDADLIVWLVEHHLTMSQVAQKQDLGDPEVIRHFADQVGSERYLSALYLLTVADIRGTSPKVWNAWKAKLLEDLYRITLRVLGGATTDPHAVLEGRKEEARVLLRLAAMDPHAHEALWAQLDVGVFLRHDARDIAWFTRHFYNRVDTTLPIVRARISPVGEGLQVAVYSPDRPDLFARICGYFERKGLTILDAKIHTTKHGYALDTFQVADPGSGLVEPGHYRDIITLVEHELAELIARETVLAEPPRGRISRQSRSFPIKPRVDLRPDERGQYYLLSLSATDRTGLLYAIARVLARHRVSVHTARINTLGERVEDVFLLDGRRLTQDNKLQLALESELLEALAI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Legionella pneumophila (strain Paris)
Length
861 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.698 kDa
Sequence
MKNDNRIIKNTIKQFKEKLCKDFSQKANITSITRKLAVFIDTILIQLFIKNKLHFGDNFCLLALGSYGRRELQLHSDIDLLILHTEKVSNIQLQRAQKFIQDCWDVGLEVSHQITTVSSCANLASQDLSVISTIMDMFLLCGHGALMEELIYQTHTLHMWPSHQYFFAKLQEQQNRYAKYGETAYNLEPNIKNGPGGLRDLQILLSISKRHFKIKKLAEGIGYGFITDKEYEELKYCQNFLWRVRFALHMLAGKPEERLSFDYQVKLAQFFGYQDQSHILAIEQFMKDYFKVIKRNRELNEMLLQWFNETIVYHQKQKIIRLDDEFQLSNRFIEVRNNRVFKQNPQSILKLFYWLVKRPDIEGVRASTIRLIRESLFLMGKRFRESKETANIFINIFRTGNDPYDALQRMNRYGVLAHYLDCFATVTGQMQYDLFHAYTVDQHTLFVIRNISRFKKNEYAKQFPLCAKIISALEKPEILYLGALFHDIAKGRGGDHSELGAIEAQQFTQRHYMEAEDSKLIVWLVRYHLLMSQTAQRKDIYDPKTIEQFCQLLPHARYLDYLYLLTVADICGTNPTLWNAWKDSLLKELYHAAKTRLHKQQELLDEAALISIRKQYAMDILISDGISSRVIQDLWSQFKGKYFLHESPEVIARHTKAILNSKQFPVVIIMPHHSQGGTEVFIYMPHKDERFTITTSVLSNHHVTIQEAAIITCDNQFDLDTYIILDENNQAFLNEQRARDIQKSLCDHLANTGRLPAVSRRRLSRALTHFNVKTQINFIDDNTNHQTQLFLVTNDRPGLLATISRVFLTLNIHLHNAKIATAGERVEDMFYISNQTGYSLNHEEKTILKEKLILEISKSKY

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Legionella pneumophila (strain Corby)
Length
861 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.711 kDa
Sequence
MKNDNRIIKNTIKQFKEKLCKDFSQKANITSITRKLAVFIDTILIQLFIKNKLHFGDNFCLLALGSYGRRELQLHSDIDLLILHTEKVSNIQLQRAQKFIQDCWDVGLEVSHQITTVSSCANLASQDLSVISTIMDMFLLCGHGALMEELIYQTHTLHMWPSHQYFFAKLQEQQNRYAKYGETAYNLEPNIKNGPGGLRDLQILLSISKRHFKIKKLAEGIGYGFITDKEYEELKYCQNFLWRVRFALHMLAGKPEERLSFDYQVKLAQFFGYQDQSHILAIEQFMKDYFKVIKRNRELNEMLLQWFNETIVYHQKQKIIRLDDEFQLSNRFIEVRNNRVFKQNPQSILKLFYWLVKRPDIEGVRASTIRLIRESLFLMGKRFRESKETANIFINIFRTGNDPYDALQRMNRYGVLAHYLDCFATATGQMQYDLFHAYTVDQHTLFVIRNISRFKKNEYAKQFPLCAKIITALEKPEILYLGALFHDIAKGRGGDHSELGAIEAQQFTQRHYMEAEDSKLIVWLVRYHLLMSQTAQRKDIYDPKTIEQFCQLLPHARYLDYLYLLTVADICGTNPTLWNAWKDSLLKELYHAAKTRLHKQQELLDEAALISIRKQYAMDILISDGISSRVIQDLWSQFKGKYFLHESPEVIARHTKAILNSKQFPVVIIMPHHSQGGTEVFIYMPHKDERFTITTSVLSNHHVTIQEAAIITCDNQFDLDTYIILDENNQAFLNEQRARDIQKNLCDHLANTGRLPAVSRRRLSRALTHFNVKTQINFIDDNTNHQTQLFLVTNDRPGLLATISRVFLTLNIHLHNAKIATAGERVEDMFYISNQTGYSLNHEEKTILKEKLILEISKSKY

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Length
861 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.771 kDa
Sequence
MKNDNRIIKNTIKQFKEKLCKDFSQKTNITSITRKLAVFIDTILIQLFIKNKLHFGDNFCLLALGSYGRRELQLHSDIDLLILHTEKVSNIQLQRAQKFIQDCWDVGLEVSHQITTVSSCANLASQDLSVISTIMDMFLLCGHGALMEELIYQTHTLHMWPSHQYFFAKLQEQQNRYAKYGETAYNLEPNIKNGPGGLRDLQILLSISKRHFKIKKLAEGIGYGFITDKEYEELKYCQNFLWRVRFALHMLAGKPEERLSFDYQVKLAQFFGYQDQSHILAIEQFMKDYFKVIKRNRELNEMLLQWFNETIVYHQKQKIIRLDDEFQLSNRFIEVRNNRVFKQNPQSILKLFYWLVKRPDIEGVRASTIRLIRESLFLMGKRFRQSKETANIFINIFRTGNDPYDALQRMNRYGVLAHYLDCFATVTGQMQYDLFHAYTVDQHTLFVIRNISRFKKNEYAKQFPLCAKIITALEKPEILYLGALFHDIAKGRGGDHSELGAIEAQQFTQRHYMEAEDSKLIVWLVRYHLLMSQTAQRKDIYDPKTIEQFCQLLPHARYLDYLYLLTVADICGTNPTLWNAWKDSLLKELYHAAKTRLHKQQELLDEAALISIRKQYAMDILISDGISFRVIQDLWGQFKGKYFLHESPEVIARHTKAILNSKQFPVVIIMPHHSQGGTEVFIYMPHKDERFTITTSVLSNHHVTIQEAAIITCDNQFDLDTYIILDENNQAFLNEQRARDIQKSLCDHLANTGRLPAVSRRRLSRALTHFNVKTQINFIDDNTNHQTQLFLVTNDRPGLLATISRVFLTLNIHLHNAKIATAGERVEDMFYISNQTGYSLNHEEKTILKEKLILEISKSKY

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Legionella pneumophila (strain Lens)
Length
861 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
100.671 kDa
Sequence
MKNDNRIIKNTIKQFKEKLCRDFSQKANITSITRKLAVFIDTILIQLFIKNKLHFGDNFCLLALGSYGRRELQLHSDIDLLILHTEKVSNIQLQRAQKFIQDCWDVGLEVSHQITTVSSCANLASQDLSVISTIMDMFLLCGHGALMEELIYQTHTLHMWPSHQYFFAKLQEQQSRYAKYGETAYNLEPNIKNGPGGLRDLQILLSISKRHFKIKKLAEGIGYGFITDKEYEELKYCQNFLWRVRFALHMLAGKPEERLSFDYQVKLAQFFGYQDQSHILAIEQFMKDYFKVIKRNRELNEMLLQWFNETIVYHQKQKIIRLDDEFQLSNRFIEVRNNRVFKQNPQSILKLFYWLVKRPDIEGVRASTIRLIRESLFLMGKRFRESKETANIFVNIFRTGNDPYDALQRMNRYGVLAHYLDCFATVTGQMQYDLFHAYTVDQHTLFVIRNISRFKKNEYAKQFPLCAKIITALEKPEILYLGALFHDIAKGRGGDHSELGAIEAQQFTQRHYMEAEDSKLIVWLVRYHLLMSQTAQRKDIYDPKTIEQFCQLLPHAKYLDYLYLLTVADICGTNPTLWNAWKDSLLKELYHAAKTRLHKQQELLDEAALISIRKQYAMDILISDGISSRVIQDLWSQFKGKYFLHESPEVIARHTKAILNSKQFPVVIIMPHHSQGGTEVFIYMPHKDERFTITTSVLSNHHVTIQEAAIITCDNQFDLDTYIILDENNQAFLNEQRARDIQKSLCDHLANTGRLPAVSRRRLSRALTHFNVKTQINFIDDNTNHQTQLFLVTNDRPGLLATISRVFLTLNIHLHNAKIATAGERVEDMFYISNQTGYSLNHEEKTILKEKLILEISKSKY

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Burkholderia vietnamiensis (strain G4 / LMG 22486)
Length
859 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.064 kDa
Sequence
MSAHAAPSPEALSRRAEFKAAKADLLERFRSATNVTSLMHALSKLTDSALKRVWDDCGLPATLALVAVGGYGRGELAPHSDVDILVLLPDAHDPALDARIERFIGMAWDLGLEIGSSVRTVAQCIEEASQDVTVQTSLLEARRIFGSTALFERFTVRYHEEALDARAFFTAKVLEMRQRHAKFQDTPYSLEPNVKESPGGLRDLQTILWIARAAGFGSSWRELDTRGLITEREARELRRNEGFLKALRARLHVIAGRRQDVLVFDLQTQAAESFGYRPTQAKRASEQLMRRYYWAAKAVTQLATILIQNIEAQLFPATSGITRVLSHDRFVEKQGMLEIVDDGVFERHPDAILEAFLLYETTRGVKGLSARTLRALYNSREIMNDTWRRDAQNRHTFMQILQQPEGITHAFRLMNQTSVLGRYLLNFRRIVGQMQHDLYHVYTVDQHILMVLRNIRRFAVAEHAHEYPFCSQLIGNFERPWVLYVAALFHDIAKGRGGDHSTLGMADARRFCREHGIGGDDAALIVWLVQHHLTMSQVAQKQDTSDPEVIKRFAAIVGNERYLTALYLLTVADIRGTSPKVWNTWKGKLLEDLYRITLAVLGGAKPDAHSELKSRQEQALALLRLETVPDDAHRALWDQLDVGFFLRHDAADIAWQTRVLYRHVNAETAIVRARPSPIGDALQVLVYVKDRPDLFAGICAYFDRNGLSVLDARVSTTRHGYALDNFIVTQTERDVRYRDIANLVEQQLATRLAETAPLPEPSKGRLSRLSRTFPITPRVDLRADERGQYYILSVSANDRPGLLYSIARVLAEHRVGVHAARINTLGERVEDIFLLDGAGLSDNRLQIQLETELLRAIAV

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Bordetella avium (strain 197N)
Length
858 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.978 kDa
Sequence
MNPTDLHPIKERMQAARAAAIADFRQHLRPDPLLSELRRIVDQALRDLLKLCPLPAGATLAAVGGYGRGELYPHSDVDLLILLPRAPDGPDESAIETLVASLWDLGLEPGHSVRTLAECETEASADITVETALLESRWLAGSRSLMKQFETAMTARLDARAFFRAKRVEMQQRHARYQDTPYALEPNSKESPGGLRDLQVILWMARAAGFGRNWRAVAQAGLLTAPEARDLRRAEQAFKRLRIELHLLTRRREDRLLFDLQPTLAEVYGIATTTTRRASELLMQRYYWAARLVTQLNVILIQNIEERLFPRPESDARAIDEEFRSLHGRLDIIREDCFERNPTLLLRAFLVMQQHPGLSGMSARTLRAIWHSRHRIDAQFRRNPVNRKLFLQILQQPRGIVHELRRMTMLNILPRYLPVFRRIVGQMQHDLFHVYTVDQHTLAVIRNLRRFTMPEHASEYPLASQVMAGLDRHWLLYVAALFHDIAKGRGGDHSELGARDARRFAQEHGLAPEDAELVEFLVRQHLLMSAVAQKRDLSDPEVINEFARQVKDERHLNALYLLTVADIRGTSPKVWNAWKGKLLEDLYRLTLAALGGAQDTRTVLAERKEEAARLLRLAGLRDDARDAFWQQLDVAYFLRHDASEIAWHTRHLYYQVQPDKPVVKVRPTEEGSGLQIMVYTRDTPDLFMNTCAYFDGKAFSIQDARIHTTRQGWALDSFIVLPAEPLADLRAQAALVEHELAERLRQAQGGARLADVRVFHRNRQSRVSRVFPVMPQAELHPDERSQSWRLSVTATDRPGLLHALARVMAENGVNLIMAKIMTLGDRVEDVFIISGAVLERPRTQMQFEHAVLDALAGE

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264)
Length
858 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
96.88 kDa
Sequence
MSASVAAPPPALSRKAEFKAAKAELLARFQTATNVTPLMHALSRATDDALRRLWHECGLPATLALVAVGGFGRGELSPHSDVDILVLLPDAHARELDERIERFIGMAWDLGLEIGSSVRTVDQCIEEASQDVTVQTSLLEARRIVGSTALFERFMLRYREALDARAFFQAKVLEMRQRHAKFQDTPYSLEPNVKESPGGLRDLQTILWIARAAGFGSSWRELDTRGLITDREARELRRNEGFLKTLRARLHVIAGRRQDILVFDLQTQAAESFGYRPTPAKRASEQLMRRYYWAAKAVTQLATILIQNIEAQLFPATSGVTRVLSPGRFVEKQGMLEIAADDVFERHPDAILEAFLLYEATRGVKGLSARTLRALYNSRDVMNNAWRRDPRNRHTFMQILQQPEGITHAFRLMNQTSVLGRYLLNFRRIVGQMQHDLYHVYTVDQHILMVLRNIRRFAVAEHAHEYPFCSQLIVNFERPWVLYVAALFHDIAKGRGGDHSALGMTDARRFCREHGIEGGDAALVVWLVQHHLTMSQVAQKQDTSDPEVIKRFADLVGNERRLTALYLLTVADIRGTSPKVWNTWKGKLLEDLYRATLAVLGGAQPDAHSELKTRQEEALALLRLETVPPDAHRALWDQLDVGYFLRHDAADIAWQTRVLYRHVAADTAIVRARPSPVGDALQVLVYVKDRSDLFAGICAYFDRNGLSVLDARVNTTRHGYALDNFIVTQTERDVQYRDIANLVEQQLAARLAESAPLPEPSKGRLSRLSRTFPITPRVDLRADERGQYYILSVSANDRPGLLYSIARVLAEHRVGVHAARINTLGERVEDVFMLDGTGLSDNRLQIQVETELLRAIAV

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
Length
857 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.774 kDa
Sequence
MDTTPELLLCQRIRDKLKADKQVLFAEFDANNQVNPLVTKLRRAVDVALTEAWTGLELPGDVALVAVGGYGRGELFPHSDVDVLLLLPGEPDAKMAAKLERFIGLCWDLGLEIGSSVRTVDDCIRESAADITIRTSLLEARLLIGNKALFKSLQTRYQADMDAADFFQAKLLEMRQRHAKYQDTPYALEPNCKESPGGLRDLQVILWMTEAARLGDSWKQLFERGLLTEREAQELTRNERLLRTIRARLHLLAGRRQDVLVFDLQTALAEAFGYRQTTNKRASEQLMRRYYWAAKAVTQLNSVLLLNIEAMLFPSESMVTREINDRFVERQGMLEITSDDLYERNPHAILETFLLYERTPGVKGLSPRTLRGLYNARTVMDASWRNDPVNRRLFLAIVQEPQGITHALRLMNQTSVLGRYLINFRRIVGQMQHDLFHVYTVDQHILMVVRNMRRFAIVEHTHEFPFCSQLMAGFDRPWVLWVAALFHDIAKGRGGDHSKLGTVDARRFCKQHGISREDTDLIAWLVEHHLTMSHVAQKQDLTDPDVVKAFAQVVGNGRYLTALYLLTVADIRGTSPKVWNAWKGKLLEDLYRITLRVLGGARLDTHSLWAQKRDDTIAQLRLKAFDPELAKPLWDKLDMSFFMRQDARDIAWLTRSLFNKVNSPNPVVKARISPAGEGLQVAVYVKDQPDLFARICGYFERKAFSIQDAKIETTRDGYALDTFQITDPGLAGDYRDILTLVEHELGERVRLECPLPDPTQGRLSRQSRSFPIKPRVDLRPDERGQYYLLSVSANDRTGLLYAIARVLAKHRVSVHSARINTLGERVEDVFLVDGSRLAADNRLQIQLEQDLLDALAI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Length
856 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.141 kDa
Sequence
MTLSAAPLQHWRQTLAEKRQQLADAYRADRDAPAFLRRYSQAVDQTLAALWREQGLDGQAALAAVGGYGRGQLFPCSDVDILILLPDPTPAEINDKVSHFIGLMWDIGLEIGHSVRTLDECLREAAGDITIETNLLENRLVAGPAEPWRELMRRLEAQRDPLAFFEGKTLEQQQRHTRHFGVSNNLEPNLKESPGGLRDLHTILWISKAAGLGDNWDSLVRRGILTLAEARLIKHSEEQLQKLRVDLHLLARRREDRLIFDLQQQVAQAWGLADTPAKRASEQLMQLYFRAAKTVNQLNGILLPNLRGRIYCQVPRVTQHISEYFHAVNGMLGIREVNVFDKHPHAILEAFLTLQRHPELSGFAPRMLRALWHGRSQINDRFRSDPRNRATFMQIFREPSGLTRTLRRMNLYGILGQYLPNFGQIVGQMQHDLFHVYTVDEHILMVVRNLRRFAISAYNHEYPFLSRLINDFERPEVLYLAGLFHDIAKGRGGDHSQLGIADADAFCRDHGLAEEDCQLVAWLVGQHLTMSSIAQKQDIYDPETVQRFAELVRTPRRLAALYLLTVADIRGTSPKVWNTWKAKLLEDLYHATLRVLSRGGEIDLASELEARKNQARAQLRLHAIPDAAEAGLWAQLDTVYFLRHEAKEIAWHARVLNRQLSPDTPQVRARLADDHEGLQVLIYSPDKPELFARACAFFGRTNYSIADAKVYTTRHGYALDTFHVFVPEHHDGDYRDMINFIEFELAAALATDQPLQLPPQGRISRHLKHFPITPQVSIRPDDKDSDFILSIVAGDRPGLLARIAKVLADYRLNVRSAKIMTLGGRAEDSFQVSGAALKDDKTALALEAALITALRI

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Length
852 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
96.964 kDa
Sequence
MPENLSSALETFKQQRNAAEAHYLKANRVSVFFREYTAAVETLLAALWAEHFQNSALCLMAVGGFGRGEPYPCSDVDLAVVSPAPLSDGIQEQIARFIQTLWDCKLMPSVKSGSVDELCESVRDDITGDTAFLEARFLFGNRQTADELAEKMNVQRNVAAFIEAKLVEMEHRHAKSQGSGAVLEPNIKSCPGGLRDIHTLLWIAKAQGLAANLPDLLKQRILTRAEAGMLSHGYRRLAHIRIRLHLNAKRAEDRLLFDLQPQVAESMGYQDENRRRQSEELMRVFYRAVKTVKQLGGILTPMLRSRVSSTPVRVTLRIDDDYIQVNNQIAARHTDIFFRRPEHIFKIVEIMQQRNDITALEPQTLRAWWGATRKINRSFYQNSENRRRFAGFFRSGNGLTQTLRFLNLYGVLGRYLPAWEKIVGLLQHDLFHIYPVDDHILAVVRNVRRLALDMHSHELPYASALMQSFEKQDILYLAAFFHDIAKGRGGDHAVQGIADARQFAADHFLTEEESDLLAWLVENHLLMSAVAQKEDIQDPGVLDAFCKRVQTHERLSALYLLTISDIRGTNPKLWNAWRASLLESLFHAAGRCLAGNDGNPHALFGRRRQEAADLLTRAAVPEKQQKKLWNALGSAYFARHQSREILWHAANLVHDFEPPIVRSRILPQSDSFQVMVFMPNGPRLFARLCRIFSRHGFDILAARAFITEHDYILDTFIVQIPSQHAPEDYPDIQSALEAELNSFIHGHTVAETQSCNRRISRRSRYMPIAPSITITPEEDYPDRYSVEITAVNRPFLLADMAEVFFAHNVSLRYAKISTLDERVEDSFTVFSPDLKNPKIQSSLKQALLEQLA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Neisseria gonorrhoeae (strain NCCP11945)
Length
852 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
96.996 kDa
Sequence
MPENLSSALETFKQQRNAAEAHYLKANRVSVFFREYTAAVETLLAALWAEHFQNSALCLMAVGGFGRGEPYPCSDVDLAVVSPAPLSDGIQEQIARFIQTLWDCKLMPSVKSGSVDELCESVRDDITGDTAFLEARFLFGNRQTADELAEKMNVQRNVAAFIEAKLVEMEHRHAKSQGSGAVLEPNIKSCPGGLRDIHTLLWIAKAQGLAANLPDLLKQRILTRAEAGMLSHGYRRLAHIRIRLHLNAKRAEDRLLFDLQPQVAESMGYQDENRRRQSEELMRVFYRAVKTVKQLGGILTPMLRSRVSSTPMRVTLRIDDDYIQVNNQIAARHTDIFFRRPEHIFKIVEIMQQRNDITALEPQTLRAWWGATRKINRSFYQNSENRRRFAGFFRSGNGLTQTLRFLNLYGVLGRYLPAWEKIVGLLQHDLFHIYPVDDHILAVVRNVRRLALDMHSHELPYASALMQSFEKQDILYLAAFFHDIAKGRGGDHAVQGIADARQFAADHFLTEEESDLLAWLVENHLLMSAVAQKEDIQDPGVLDAFCKRVQTHERLSALYLLTISDIRGTNPKLWNAWRASLLESLFHAAGRCLAGNDGNPHALFGRRRQEAADLLTRAAVPEKQQKKLWNALGSAYFARHQSREILWHAANLVHDFEPPIVRSRILPQSDSFQVMVFMPNGPRLFARLCRIFSRHGFDILAARAFITEHDYILDTFIVQIPSQHAPEDYPDIQSALEAELNSFIHGHTVAETQSCNRRISRRSRYMPIAPSITITPEEDYPDRYSVEITAVNRPFLLADMAEVFFAHNVSLRYAKISTLDERVEDSFTVFSPDLKNPKIQSSLKQALLEQLA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Neisseria meningitidis serogroup C (strain 053442)
Length
852 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
96.95 kDa
Sequence
MPANLSSALETFKRQRDAAEAHYLKANRVSVFFREYTAAVETLLAALWVEHFQNSALCLMAVGGFGRGELYPCSDVDLAVVSPAPLSDGIQEQIARFVQTLWDCKLMPSVKSGSVGELCESVRDDITGDTAFLEARFLFGNRQTADELAKKMNAQRNVAAFVEAKLVEMEHRHAKSQGSGAVLEPNIKSCPGGLRDIHTLLWIAKAQGLATDLPDLLKQRILTRAEAGMLSHGYRRLAHIRIHLHLNAKRAEDRLLFDLQPQVAESMGYEGLNLRRQSEELMRVFYRAIKTVKQLGGILTPMLQSRVSSTPLRVTLRIDDDYIQVNNQIAARHTDIFFRRPEHIFKIVEIMQQRNDITALEPQTLRAWWGATRKINRSFYQNSENRHRFAGFFRNGNGLTQTLRFLNLYGVLGRYLPAWEKIVGLLQHDLFHIYPVDDHILTVVRNVRRLALDMHSHELPYASALMQSFEKQDILYLAAFFHDIAKGRGGDHAIQGIADARQFAADHFLTEEESDLLAWLVENHLLMSTVAQKEDIQDPSVLDAFCKRVQTHERLSALYLLTISDIRGTNPKLWNAWRASLLESLFHAAGRYLTGNGGNPHTLFGRRRQEAADLLTRAAVPEKQQKKLWNALGSAYFARHQSREILWHAANLVHDFETPIVRSRILPQSDSFQVMVFMPNGPRLFARLCRIFSRHGFDILAARAFITEHDYILDTFIVQIPSQHAPEDYPDIQSALEAELNSFIHGHTVAEISSHSRRISRRSRYMPIAPSITITPEEDYPDWYSVEITAVNRPFLLADMAEVFFAHNVSLRYAKISTLDERAEDSFTVFSPDLNNPKIQSSLKQTLLEQLS

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Length
852 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.058 kDa
Sequence
MPANLSSALETFKQQRDAAEAHYLKANRVSVFFREYTAAVETLLAALWAEYFQNSALCLMAVGGFGRGELYPCSDVDLAVVSPAPLSDGIQEQIARFVQTLWDCKLMPSVKSGSVDELCESVRNDITGDTAFLEARFLFGNRQTADKLAEKMNAQRNVAAFVEAKLVEMEHRHAKSQGSGAVLEPNIKSCPGGLRDIHTLLWIAKAQGLATDLPDLLKQRILTRAEAGMLSHGYRRLAHIRIHLHLNAKRAEDRLLFDLQPQVAESMGYEGLNLRRQSEELMRVFYRAIKTVKQLSGILTPMLRSRVSSAPMRVTLRIDDDYIQVNNQIAARHTDIFFRRPEHIFKIVEIMQQRNDITALEPQTLRAWWGATRKINRSFYQNSENRHRFAGFFRNGNGLTQTLRFLNLYGVLGRYLPAWEKIVGLLQHDLFHIYPVDDHILTVVRNVRRLALDMHSHELPYASALMQSFEKQDILYLAAFFHDIAKGRGGDHAIQGIADARQFAADHFLTGEESDLLAWLVENHLLMSAVAQKEDIQDPDVLDAFCKRVQTHERLSALYLLTISDIRGTNPKLWNAWRASLLESLFHAAGRYLTGNGGNPHTLFGRRRQEAADLLTRAAVPEKQQKKLWNALGSAYFARHQSREILWHAANLVHDFETPIVRSRILFKSDSFQVMVFMPNGPRLFARLCRIFSRHGFDILAARAFITEHDYILDTFIVQIPSQHAPEDYPDIQSALEAELNSFIHGHTVAETQSHSRRISRRSRYMPIAPSITITPEEDYPDWYSVEITAVNRPFLLADMAEVFFAHNVSLRYAKISTLDERAEDSFTVFSLDLKNPKIQSSLKQTLLEQLS

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Neisseria meningitidis serogroup B (strain MC58)
Length
852 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.008 kDa
Sequence
MPANLSSALETFKQQRDAAEAHYLKANRVSVFFREYTAAVETLLAALWAEYFQNSALCLMAVGGFGRGELYPCSDVDLAVVSPAPLSDGIQEQIARFVQTLWDCKLMPSVKSGSVDELCESVRNDITGDTAFLEARFLFGNRQTVDKLAEKMNAQRNVAAFVEAKLVEMEHRHAKSQGSGAVLEPNIKSCPGGLRDIHTLLWIAKAQGLATDLPDLLKQRILTRAEAGMLSHGYRRLAHIRIHLHLNAKRAEDRLLFDLQPQVAESMGYEGLNLRRQSEELMRVFYRAIKTVKQLGGILTPMLQSRVSSTPLRVTLRIDDDYIQVNNQIAARHTDIFFRRPEHIFKIVEIMQQRNDITALEPQTLRAWWGATRKINRSFYQNPENRRRFAGFFRNGNGLTQTLRFLNLYGVLGRYLPAWEKIIGLLQHDLFHIYPVDDHILTVVRNVRRLALDMHSHELPYASALMQSFEKQDILYLAAFFHDIAKGRGGDHAIQGIADARQFAADHFLTGEESDLLAWLVENHLLMSAVAQKEDIQDPSVLDAFCKRVQTHERLSALYLLTISDIRGTNPKLWNAWRASLLESLFHAAGRYLTGNGGNPHTLFGRRRQEAADLLTRAAVPEKQQKKLWNALGSAYFARHQSREILWHAANLVHDFETPIVRSRILPKSDSFQVMVFMPNGPRLFARLCRIFSRHGFDILAARAFITEHDYILDTFIVQIPSQHAPEDYPDIQSALEAELNSFIHGHTVAETQSRSRRISRRSRYMPIAPSITITPEEDYPDWYSVEITAVNRPFLLADMAEVFFAHNVSLRYAKISTLDERAEDSFTVFSPDLKNPKIQSSLKQTLLEQLS

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
Length
852 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
96.831 kDa
Sequence
MPANLSSALETFKQQRDAAEAHYLKTNRVSVFFREYTAAVETLLAALWVEHFQNSALCLMAVGGFGRGELYPCSDVDLAVVSPAPLSDGIQEQIARFVQTLWDCKLMPSVKSGGIDELCESVRNDITGDTAFLEARFLFGNRQTADELAEKMNAQRNVAAFIEAKLVEMEHRHAKSQGSGAVLEPNIKSCPGGLRDIHTLLWIAKAQGLATNLPALVKQGILTRTEAGMLSHGYRRLAHIRIHLHLNAKRAEDRLLFDLQPQVAESMGYQGLNLRRQSEELMRVFYRAIKTVKQLSGILTPMLQSRVSSTPLRVTLRIDDDYIQVNNQIAARHTDIFFRRPEHIFKIVEIMQQRNDITALEPQTLRAWWGATRKINRSFYQNSENRHRFAGFFRNGNGLTQTLRFLNLYGVLGRYLPAWEKIVGLLQHDLFHIYPVDDHILTVVRNVRRLALDMHSHELPYASALMQSFERQDILYLAAFFHDIAKGRGGDHAIQGIADARQFAADHFLTEEESDLLAWLVENHLLMSTVAQKEDIQDPSVLDAFCKRVQTHERLSALYLLTISDIRGTNPKLWNAWRASLLESLFHAAGRYLAGNGGNPHALFGRRQQEAADLLTRAAVPEKQQKKLWNALGSAYFARHQSREILWHAANLVHDFETPIVRSRILPQSDSFQVMVFMPNGPRLFARLCRIFSRHGFDILAARAFITEHDYILDTFIVQIPSQHAPEDYPDIQSALEAELNSFIHGHTVAEISSHSRRISRRSRYMPIAPSITITPEEDYPDWYSVEITAVNRPFLLADMAEIFFAHNVSLRYAKISTLDERAEDSFTVFSPDLKNPKIQSSLKQALLEQLA

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Dechloromonas aromatica (strain RCB)
Length
852 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
97.701 kDa
Sequence
MSCDVAALRAEVKANQNQLRLNYEQSNDAVALLRDRCQHVDTVLEKLWLSLNFPASLALAAVGGYGRGELYPASDIDLLILLPQEASASLQEKLERLVGHFWDIGLEIGHSVRTVQECLDEAANDITVQTALLEARLLTGNTKLFATFQKRLRGNLDPLHFFEAKRLEQQERYLRFNETPYSLEPNCKESPGGLRDIQVIFWIAKAAGYGSTWAELHQNGIITQEEMIQMEGCEAYLNHLRIRLHFMLGRREDRLLFDYQSTLAANYGFVSNEAKRESEQLMQVYYRNAKTVTVLNTILLQNMGAALTPESEQTPQQLDESFQIVGNLLDIRDEQLYERNPLAILDSFLAMQESHELFGMTARTLRALWRAREQITPEFRANPENRAAFMKLLQGDRGIVHEFRRMNQLGILGRYLPNFGRIVGQMQHDLFHVYTVDQHILQVMRNIRRFTMSEFAHEYPLCSRIISELDRPWLLYVAALFHDIAKGRGGDHSELGTVDTREFCVNHGLSEEDTELVVWLVKNHLVMSQVAQKEDLSDPDVIANFIRLVGDTRHLQALYLLTHADIRGTSPKVWNNWKGKLLADLYYQAIHHINQGEAPAAHGVIAERQAEAMRLLRFFALSATVHERLWKQLDTVYFLRHSAEEIAWHTRSLHYRIYNNQPVVRARPNQEGDGLQVMVYTQDQPDLFARIVGFFARAGYSIVDAKIHTTAHGYALDSFVVLDIEERDNDREMVAYIEHELEQRLLHQMPRDVPSSGRLSRQVKHFPIKPEVSIRGDEKGTHFILSLVAADRPGLLYTVANTLTEHGAYLHTAKITTLGERAEDVFLISGGDLRDTHNRIRLETELMERLKV

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Thiobacillus denitrificans (strain ATCC 25259)
Length
850 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
95.305 kDa
Sequence
MSARPFADLRERLKSGRASLAAAYREKPRAAHYLARHAALVDALLAELSTRLGLARGICLVAVGGYGRGELFPGSDVDVMLLLPAEPLEAERQALESWVQACWDVGLEIGHSVRTVDACLAEADADITVETNLLEARRVWGATALFDDFGRRFRARFDAQRFFDGKLAEQHARHARFDDSAYKLEPNLKDSPGGLRDLHTIHWLAQACDIDAGWSGIARAGLLTEGEARRVAREERWLAKLRIHLHLLAGRREDRLAFDYQSELAACLGLAPTAHRRAGERLMQGYFRAAKLVQRANDILIQSLRVRLFPVVAPPLPIDDDFQLRAGLLEARDPDVFLRKPDALLRAFLVYARHPQLAGFEPTTLRAVWRASARVDRAFRATPAHRALFIALLREPLGVTRALRAMHRYGLLGRYIPAFGRIVGQMQHDLFHVYTVDEHILTVLRNLRRFTVAQLAHEFPLASRLIAAFDKPELLYLAALFHDIAKGRGGDHSALGALDARGFCRQHGLDKTDTDLVAWLVDMHLVMSRTSQKEDISDPKVIAAFAARVGDTRRLDALYLLTVADIRGTSPTVWNAWKGKLLEDLYHAAFARLQGADLAIAGIAARREEARVNLALYGLPRDAADALWRHLDKAYFARFDARDMAWHARMLWRRDATAGAVVRARLSPAGEGIQVMVYAPDRPDIFVRICAFFARIQYTVLEAKIHTTRNGYALDSFQVMDLAHRNIHYRDFLAFVEYELARDLDPARPLQAVQPGRLSRHQRHHPYPAAVHLEADRGGDGQVLSITCADRGGLLFAIAEELMRHEISVYAAKIDTLGERVEDTFLIRGERLNAPPERAALENELRGVLG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Thiobacillus denitrificans (strain ATCC 25259)
Length
850 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
95.305 kDa
Sequence
MSARPFADLRERLKSGRASLAAAYREKPRAAHYLARHAALVDALLAELSTRLGLARGICLVAVGGYGRGELFPGSDVDVMLLLPAEPLEAERQALESWVQACWDVGLEIGHSVRTVDACLAEADADITVETNLLEARRVWGATALFDDFGRRFRARFDAQRFFDGKLAEQHARHARFDDSAYKLEPNLKDSPGGLRDLHTIHWLAQACDIDAGWSGIARAGLLTEGEARRVAREERWLAKLRIHLHLLAGRREDRLAFDYQSELAACLGLAPTAHRRAGERLMQGYFRAAKLVQRANDILIQSLRVRLFPVVAPPLPIDDDFQLRAGLLEARDPDVFLRKPDALLRAFLVYARHPQLAGFEPTTLRAVWRASARVDRAFRATPAHRALFIALLREPLGVTRALRAMHRYGLLGRYIPAFGRIVGQMQHDLFHVYTVDEHILTVLRNLRRFTVAQLAHEFPLASRLIAAFDKPELLYLAALFHDIAKGRGGDHSALGALDARGFCRQHGLDKTDTDLVAWLVDMHLVMSRTSQKEDISDPKVIAAFAARVGDTRRLDALYLLTVADIRGTSPTVWNAWKGKLLEDLYHAAFARLQGADLAIAGIAARREEARVNLALYGLPRDAADALWRHLDKAYFARFDARDMAWHARMLWRRDATAGAVVRARLSPAGEGIQVMVYAPDRPDIFVRICAFFARIQYTVLEAKIHTTRNGYALDSFQVMDLAHRNIHYRDFLAFVEYELARDLDPARPLQAVQPGRLSRHQRHHPYPAAVHLEADRGGDGQVLSITCADRGGLLFAIAEELMRHEISVYAAKIDTLGERVEDTFLIRGERLNAPPERAALENELRGVLG

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Length
835 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
89.047 kDa
Sequence
MTDEAEDSGPGGYAAARLRLLTEGARSGPPRRRALAELTDGWLAGLFGAATEEHTGISLVAVGGYGRGELSPRSDLDLLLLHDGRDDKAVAALADRLWYPVWDLGIDLDHSVRTPQQARKTAGQDLKVHLGLLDARHLAGDLGLTASLRTAVLADWRNQAPKRLPELRDLCAERAERQGELQFLLEPDLKEARGGLRDATALRAVAASWLADAPREGLAEARRRLLDVRDALHLATGRATDRLALQEQDQVAAELGLLDADALLRQVYEAARVISYAGDVTWREVGRVLRSRSVRPRLRAMMNGRNGGKPVAERSPLAEGVVEQDGEAVLARTARPERDPALPLRAAAAAAQAGLPLSRHAVRRLAATARPLPTPWPAEAREQLVTLLGSGRPTVQVWEALEAEGLVTRLLPDWERVRCRPQRNAVHLWTVDRHLIETAVRAAGFTRRVHRPDLLLIAALLHDIGKGWPGDHSVAGETIARDVAARIGFDGADTAVLATLVRHHLLLVETATRRDLDDPATVRAVAQAVGTEHTLELLHALTEADALATGPAAWSSWRGSLVADLVKRVSGVLAGEPQPEAESAAPTAEQERLAVEAFRTGGPVLALRAQTEPPADSAPAPSSPSSPSFPSPLSSPSSPSSADGPEPLGVELLIAVPDQAGVLPAVAGVLAMHRLTVRTAELRSVPLPDGVEGSVLLLDWRVAAQYGSLPQAARLRADLVRALDGTLDIAARLAERDAAHPRRRGVEPPPPRVTVAPAASRLATVIEVRAQDAPGLLFRLGRALEAAGVRVRSAHVSTLGANAVDAFYVTRGEGTPLPGDEAASVARGLEESLRT

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Length
835 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
89.047 kDa
Sequence
MTDEAEDSGPGGYAAARLRLLTEGARSGPPRRRALAELTDGWLAGLFGAATEEHTGISLVAVGGYGRGELSPRSDLDLLLLHDGRDDKAVAALADRLWYPVWDLGIDLDHSVRTPQQARKTAGQDLKVHLGLLDARHLAGDLGLTASLRTAVLADWRNQAPKRLPELRDLCAERAERQGELQFLLEPDLKEARGGLRDATALRAVAASWLADAPREGLAEARRRLLDVRDALHLATGRATDRLALQEQDQVAAELGLLDADALLRQVYEAARVISYAGDVTWREVGRVLRSRSVRPRLRAMMNGRNGGKPVAERSPLAEGVVEQDGEAVLARTARPERDPALPLRAAAAAAQAGLPLSRHAVRRLAATARPLPTPWPAEAREQLVTLLGSGRPTVQVWEALEAEGLVTRLLPDWERVRCRPQRNAVHLWTVDRHLIETAVRAAGFTRRVHRPDLLLIAALLHDIGKGWPGDHSVAGETIARDVAARIGFDGADTAVLATLVRHHLLLVETATRRDLDDPATVRAVAQAVGTEHTLELLHALTEADALATGPAAWSSWRGSLVADLVKRVSGVLAGEPQPEAESAAPTAEQERLAVEAFRTGGPVLALRAQTEPPADSAPAPSSPSSPSFPSPLSSPSSPSSADGPEPLGVELLIAVPDQAGVLPAVAGVLAMHRLTVRTAELRSVPLPDGVEGSVLLLDWRVAAQYGSLPQAARLRADLVRALDGTLDIAARLAERDAAHPRRRGVEPPPPRVTVAPAASRLATVIEVRAQDAPGLLFRLGRALEAAGVRVRSAHVSTLGANAVDAFYVTRGEGTPLPGDEAASVARGLEESLRT

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Length
808 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Similarity
Belongs to the GlnD family.
Mass
86.438 kDa
Sequence
MEAESPCAASDLAVARRELLSGNHRELDPVGLRQTWLDLHESWLIDKADEIGIADASGFAIVGVGGLGRRELLPYSDLDVLLLHDGKPADILRPVADRLWYPLWDANIRLDHSVRTVSEALTIANSDLMAALGMLEARHIAGDQQLSFALIDGVRRQWRNGIRSRMGELVEMTYARWRRCGRIAQRAEPDLKLGRGGLRDVQLLDALALAQLIDRHGIGHTDLPAGSLDGAYRTLLDVRTELHRVSGRGRDHLLAQFADEISAALGFGDRFDLARTLSSAGRTIGYHAEAGLRTAANALPRRGISALVRRPKRRPLDEGVVEYAGEIVLARDAEPEHDPGLVLRVAAASADTGLPIGAATLSRLAASVPDLPTPWPQEALDDLLVVLSAGPTTVATIEALDRTGLWGRLLPEWEPIRDLPPRDVAHKWTVDRHVVETAVHAAPLATRVARPDLLALGALLHDIGKGRGTDHSVLGAELVIPVCTRLGLSPPDVRTLSKLVRHHLLLPITATRRDLNDPKTIEAVSEALGGDPQLLEVLHALSEADSKATGPGVWSDWKASLVDDLVRRCRMVMAGESLPQAEPTAPHYLSLAADHGVHVEISPRDGERIDAVIVAPDERGLVSKAAAVLALNSLRVHSASVNVHQGVAITEFVVSPLFGSPPAAELVRQQFVGALNGDVDVLGMLQKRDSDAASLVSARAGDVQAGVPVTRTAAPPRILWLDTAAPAKLILEVRAMDRAGLLALLAGALEGAGAGIVWAKVNTFGSTAADVFCVTVPAELDARAAVEQHLLEVLGASVDVVVDEPVGD

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Length
808 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory protein (GlnB), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII protein and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII protein, and plays an important role in the regulation of nitrogen assimilation and metabolism (By similarity).
Similarity
Belongs to the GlnD family.
Mass
86.438 kDa
Sequence
MEAESPCAASDLAVARRELLSGNHRELDPVGLRQTWLDLHESWLIDKADEIGIADASGFAIVGVGGLGRRELLPYSDLDVLLLHDGKPADILRPVADRLWYPLWDANIRLDHSVRTVSEALTIANSDLMAALGMLEARHIAGDQQLSFALIDGVRRQWRNGIRSRMGELVEMTYARWRRCGRIAQRAEPDLKLGRGGLRDVQLLDALALAQLIDRHGIGHTDLPAGSLDGAYRTLLDVRTELHRVSGRGRDHLLAQFADEISAALGFGDRFDLARTLSSAGRTIGYHAEAGLRTAANALPRRGISALVRRPKRRPLDEGVVEYAGEIVLARDAEPEHDPGLVLRVAAASADTGLPIGAATLSRLAASVPDLPTPWPQEALDDLLVVLSAGPTTVATIEALDRTGLWGRLLPEWEPIRDLPPRDVAHKWTVDRHVVETAVHAAPLATRVARPDLLALGALLHDIGKGRGTDHSVLGAELVIPVCTRLGLSPPDVRTLSKLVRHHLLLPITATRRDLNDPKTIEAVSEALGGDPQLLEVLHALSEADSKATGPGVWSDWKASLVDDLVRRCRMVMAGESLPQAEPTAPHYLSLAADHGVHVEISPRDGERIDAVIVAPDERGLVSKAAAVLALNSLRVHSASVNVHQGVAITEFVVSPLFGSPPAAELVRQQFVGALNGDVDVLGMLQKRDSDAASLVSARAGDVQAGVPVTRTAAPPRILWLDTAAPAKLILEVRAMDRAGLLALLAGALEGAGAGIVWAKVNTFGSTAADVFCVTVPAELDARAAVEQHLLEVLGASVDVVVDEPVGD

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Length
808 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory protein (GlnB), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII protein and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII protein, and plays an important role in the regulation of nitrogen assimilation and metabolism (Probable).
Similarity
Belongs to the GlnD family.
Mass
86.438 kDa
Sequence
MEAESPCAASDLAVARRELLSGNHRELDPVGLRQTWLDLHESWLIDKADEIGIADASGFAIVGVGGLGRRELLPYSDLDVLLLHDGKPADILRPVADRLWYPLWDANIRLDHSVRTVSEALTIANSDLMAALGMLEARHIAGDQQLSFALIDGVRRQWRNGIRSRMGELVEMTYARWRRCGRIAQRAEPDLKLGRGGLRDVQLLDALALAQLIDRHGIGHTDLPAGSLDGAYRTLLDVRTELHRVSGRGRDHLLAQFADEISAALGFGDRFDLARTLSSAGRTIGYHAEAGLRTAANALPRRGISALVRRPKRRPLDEGVVEYAGEIVLARDAEPEHDPGLVLRVAAASADTGLPIGAATLSRLAASVPDLPTPWPQEALDDLLVVLSAGPTTVATIEALDRTGLWGRLLPEWEPIRDLPPRDVAHKWTVDRHVVETAVHAAPLATRVARPDLLALGALLHDIGKGRGTDHSVLGAELVIPVCTRLGLSPPDVRTLSKLVRHHLLLPITATRRDLNDPKTIEAVSEALGGDPQLLEVLHALSEADSKATGPGVWSDWKASLVDDLVRRCRMVMAGESLPQAEPTAPHYLSLAADHGVHVEISPRDGERIDAVIVAPDERGLVSKAAAVLALNSLRVHSASVNVHQGVAITEFVVSPLFGSPPAAELVRQQFVGALNGDVDVLGMLQKRDSDAASLVSARAGDVQAGVPVTRTAAPPRILWLDTAAPAKLILEVRAMDRAGLLALLAGALEGAGAGIVWAKVNTFGSTAADVFCVTVPAELDARAAVEQHLLEVLGASVDVVVDEPVGD

Gene
glnD
Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Length
692 amino acids
Function
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism (By similarity).
Similarity
Belongs to the GlnD family.
Mass
75.97 kDa
Sequence
MNNPAQLRQDTEKEVLALLGSLVLPAGTALAATGSLARSELTPYSDLDLILIHPPGATPDGVEDLWYPIWDAKKRLDYSVRTPDECVAMISADSTAALAMLDLRFVAGDEDLCAKTRRRIVEKWRQELNKNFDAVVDTAIARWRRSGPVVAMTRPDLKHGRGGLRDFELIKALALGHLCNLPQLDAQHQLLLDARTLLHVHARRSRDVLDPEFAVDVAMDLGFVDRYHLGREIADAARAIDDGLTTALATARGILPRRTGFAFRNASRRPLDLDVVDANGTIELSKKPDLNDPALPLRVAAAAATTGLPVAESTWVRLNECPPLPEPWPANAAGDFFRILSSPKNSRRVVKNMDRHGLWSRFVPEWDRIKGLMPREPSHISTIDEHSLNTVAGCALETVTVARPDLLVLGALYHDIGKGFPRPHEQVGAEMVARAASRMGLNLRDRASVQTLVAEHTAVAKIAARLDPSSEGAVDKLLDAVRYDLVTLNLLEVLTEADAKATGPGVWTARLEHALRIVCKRARDRLTDIRPVAPMIAPRSEIGLVERDGVFTVQWHGEDLHRILGVIYAKGWTITAARMLANGQWSAEFDVRANGPQDFDPQHFLQAYQSGVFSEVPIPALGITATFWHGNTLEVRTELRTGAIFALLRTLPDALWINAVTRGATLIIQAALKPGFDRATVERSVVRSLAGS