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pfp

Gene
pfp
Protein
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
Organism
Treponema pallidum (strain Nichols)
Length
573 amino acids
Function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Similarity
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade Long sub-subfamily.
Mass
62.427 kDa
Sequence
MSISLLQQERHRYLPKVPDLLRGDFRRVCARRGLSTTAVADYDALRSLFARTYGQPLVNFVNASEKNEDSPMETAPEPRGLRVAIVLSGGQAPGGHNVIAGLFDGLKRWHADSVLIGFLGGPAGVLSGDHIEICADRVDAYRNTGGFDLIGSGRTKIESESQFAAAAQTVTRMALDALVVVGGDDSNTNAALLAEHFVNSGISTKVIGVPKTIDGDLKNEAIETSFGFDTATKTYSELIGNIARDACSARKYWHFIKLMGRSASHIALECALKTQPNVCLISEEVAAQSLTLAQIVQSLCDTIATRAQHGEHFGIVLVPEGLIEFIPEMKALITELNEVMARRAQEFEALDTPDAQRVWIEQALSASARAVFNALPAEISTQLLADRDPHGNVQVSRIDTERLLILQVTERLAQMKQEGTYTGVFSSIAHFFGYEGRCAFPSNFDADYCYTLGLTACLLAVHRFTGYVASVRNLTSSVAEWAVGGVPLTMLMNMERRHGSQKPVIKKALVDLEGMPFRVFSRRRASWALKTSYVYPGAVQYYGPPAVCDEPSVTIRLERPAPAANSSFGHRSS

Gene
pfp
Protein
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Length
555 amino acids
Function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Similarity
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade Long sub-subfamily.
Mass
62.443 kDa
Sequence
MNTSLFKQERQKYIPKLPNILKKDFNNISLVYGENTEAIQDRQALKEFFKNTYGLPIISFTEGESSLSFSKALNIGIILSGGPAPGGHNVISGVFDAIKKFNPNSKLFGFKGGPLGLLENDKIELTESLINSYRNTGGFDIVSSGRTKIETEEHYNKALFVAKENNLNAIIIIGGDDSNTNAAILAEYFKKNGENIQVIGVPKTIDADLRNDHIEISFGFDSATKIYSELIGNLCRDAMSTKKYWHFVKLMGRSASHVALECALKTHPNICIVSEEVLAKKKTLSEIIDEMVSVILKRSLNGDNFGVVIVPEGLIEFIPEVKSLMLELCDIFDKNEGEFKGLNIEKMKEIFVAKLSDYMKGVYLSLPLFIQFELIKSILERDPHGNFNVSRVPTEKLFIEMIQSRLNDMKKRGEYKGSFTPVDHFFGYEGRSAFPSNFDSDYCYSLGYNAVVLILNGLTGYMSCIKNLNLKPTDWIAGGVPLTMLMNMEERYGEKKPVIKKALVDLEGRPFKEFVKNRDKWALNNLYLYPGPVQYFGSSEIVDEITETLKLELLK

Gene
pfp
Protein
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
Organism
Spirochaeta thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1)
Length
554 amino acids
Function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Similarity
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade Long sub-subfamily.
Mass
61.08 kDa
Sequence
MTRISPLQKARYGYVPKLPPVLQDEIARIQAELGQPTEAVADREDLKRLFANTYGKPIATLTRGSNPEAGRRRTVGVILSGGPAPGGHNVICGLFDALKKANRESTLIGFKGGPSGILDDEWIEFTDSLINQYRNTGGFDIIGSGRTKIETPEQFAKALENAKKHGLDALVIIGGDDSNTNAALLAEYFVQQGAPIQVIGIPKTIDGDLKNEYIEASFGFDTATKVYAELIGNIARDAISSRKYWHFIRLMGRSASHIALECALQTHPNVCIVSEEVREKNMTLSQIVDQIVDAVVKRAAKGENFGVVLVPEGLIEFIPEVGALIDELNTLLAKEAEVFNRIDDPRERISWVKGKLSGNNQHVFSSLPETIQAQLLMDRDPHGNVQVSRIETEKLLIEMVSSRLKALKEEGAYKGKFSALNHFFGYEARCAFPSNFDADYCYALGFTAFVLIANGLTGYIAAIKNLARPAVEWKPMGIPLTMMMNMEKRHGKMKPVIRKALVDLEGAPFKRFATQRDAWATESAYVFPGAIQYYGPDDVCNQPTMTLKLEQGLE

Gene
pfp
Protein
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
Organism
Porphyromonas gingivalis
Length
549 amino acids
Function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Similarity
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade Long sub-subfamily.
Mass
61.084 kDa
Sequence
MAKSALHLARMSYQPKMPASLQGAVKIIEGKATEAVSDKEEIAAIFPRTYGLPLISFAPGGERTEYPPTNVGVILSGGQAPGGHNVIAGLFDEMKLLNPDSRLFGFLMGPDGLIEHKYRELTAEVIDEYRNTGGFDMIGSGRTKLDKPEQFEAGLEILRELDIKALVIIGGDDSNTNACILAEYYASIDAGIQVIGCPKTIDGDLKNKQIETSFGFDTAAKVYSELIGNIQRDCNSARKYWHFIKLMGRSASHITLECALQTHPNICIVSEEVEANNYYLDDVVTYIAETVVRRSEAGMNFGTVLIPEGLIEFLPAMKRLIKELNEFLSQNDAEFKLIKRSAQRQYIKNKLSPENSRLYDSLPVDVARQLIADRDPHGNVQVSLIATEKLLADMTAQKLAEWAEEGRFQGRFSTLTHFFGYEGRCAMPSNFDANYCYCLGRAASILIAAGKTGYMAAIKNTADPVSEWEAGGVPMTMMMNMERRSGKMKPVIRKALVDMDGEPYRALREMRREWALSTEYVYPGPIQFFGPEHVCDSPTMTLRLEKNDR

Gene
pfp
Protein
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Length
420 amino acids
Function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Similarity
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade B2 sub-subfamily.
Mass
45.308 kDa
Sequence
MAARNAFYAQSGGVTAVINASACGVLETARQYPDRIGTVYAGRNGIVGALTEDLIDTGQESAEAIAALRHTPSGAFGSCRYKLKGLEENRAQYERLIEVFRAHDIGYFFYNGGGDSADTCLKVSQLSEKLGYPLQAVHIPKTVDNDLPITDCCPGFGSVAKYIAVSVREASFDVRSMAATSTCIFVLEVMGRHAGWIAAAGGLASDERHELALVILFPEQVFDPERFLRAVDEKVRSHGYCSVVVSEGIRGADGRFVAESGSRDVFGHARLGGVAPVIADLIKERLGYKYHWAVADYLQRAARHIASRTDVEQAYAVGKAGVEMALKGLSAVMPAIVRTSDSPYRWEITAASLAEVANVEKKMPLEFISADGFGITEACRRYLRPLIEGEDYPPYAGGLPDYVTLCNVAVPKKLAASFSV

Gene
pfp
Protein
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
Organism
Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9)
Length
419 amino acids
Function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Similarity
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade B2 sub-subfamily.
Mass
45.705 kDa
Sequence
MAQHNAFYAQSGGVTAVINASACGVIEACRRHDDRIGKVYAGHNGIIGALTEDLIDVSQESDEAIAALRHTPAGAFGSCRYKLKDIETHRTQYERLIEVFRAHDIRYFFYNGGGDSADTCLKVSQLSEKMGYPLTAIHVPKTVDNDLPITDNSPGFGSVAKYIATSTLEASLDIASMCATSTKVFVLEVMGRHAGWIAAAGALAGQGEGDPPHLVIFPEIDFDRAAVMARVEESVKKCGYCVIVVSEGARYEDGTFLADSGNTDAFGHRQLGGVAPTLAGMIKQDLGYKYHWAVADYLQRAARHLASKTDVDQAYAVGEKAVELALDGQNAKMPAIKRISDEPYAWTVEAAPLADVANREKFMPRDFIREDGFGITEQCRRYLAPLIQGEDFPPFENGLPKVAKLAKHRVERKLPEFKL

Gene
pfp
Protein
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Length
419 amino acids
Function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Similarity
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade Short sub-subfamily.
Mass
46.465 kDa
Sequence
MAERLGILVGGGPAPGINSVISSVTIEAINNGLEVIGIYDGFKHLVEGKTNMVKKLSIEDVSRIHIEGGSILRTSRVNPAKSEETLEKTVQTLKKLGIKYLVTIGGDDTAFSASKVCERSKGEIKVVHVPKTIDNDLPLPENMPTFGFETARHVATELVYNLMQDSRTTNRWYFVAMMGREAGHLALGVGKAASATITIIPEEFKEGVTLEEVCDVLDGAILKRKLMGRDDGVAVIGEGIAEKMDPEELANIPGVIVEKDPHGHLRLAEIPLATILKRAIERRYAERGERIHIVDVTIGYELRSARPIPFDIVYTRTLGYGAVRFLLGDYSDLPGGMVCVVGGRIKILPFDAFMDPKTGRTKVRVVDVRSEDYRVARKYMIRLEKKDLEDPETLEKLAKLAKMEPEEFKKKYWHTTELP

Gene
pfp
Protein
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
Organism
Xanthomonas campestris pv. campestris (strain B100)
Length
418 amino acids
Function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Similarity
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade B2 sub-subfamily.
Mass
44.647 kDa
Sequence
MTNGNLLYAQSGGVTAVINATAAGVIGEARARKIKVLAARNGILGALREELIDTSKESAAAIAALAQTPGGAFGSCRYKLKSLEQDRAKYERLLEVLRAHDVRWFLYNGGNDSADTALKVSQLAKAFGYPLHCIGVPKTIDNDLAVTDTCPGFGSAAKYTAVSVREAALDVAAMADTSTKVFIYEAMGRHAGWLAAAAGLAGQGPDDAPQIILLPERAFDQAAFLAKVRQMVERVGWCVVVASEGIQDAQGKFVADAGGATDSFGHAQLGGVASFLAAQVKQELGYKVHWTLPDYLQRSARHLASKTDWEQAQAVGKAAVQYALKGMNAVIPVIERVSDAPYRWKIVPAPLHKVANHEKKMPPSFLRKDGFGITERARRYFAPLIKGEAPLAYGSDGLPKYVSLKNVAVAKKLPAWEG

Gene
pfp
Protein
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
Organism
Methylomicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z)
Length
409 amino acids
Function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Similarity
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade P sub-subfamily.
Mass
44.437 kDa
Sequence
MNKPKKVAILTAGGLAPCLSSAIGSLIERYTEIDPSIEIICYRSGYKGLLLGDSYAVTPKIRENAALLHKFGGSPIGNSRVKLTNVKDCIKRGLVQEGQDPQKVAADQLVKDGVDVLHTIGGDDTNTAAADLAAFLAKNDYGLTVIGLPKTIDNDVFPIKQSLGAWTAAEQGAQYFQNVVAEYNANPRMLIVHEVMGRNCGWLTAATAMEYRKLLDRSEWLPEIGLDRAAYEVHGVFVPEMEIDLAAEAKRLREVMDKVDCVNIFVSEGAGVDAIVAEMQAKGQEVPRDAFGHIKLDAVNPGKWFGEQFAEMIGAEKTLIQKSGYFARASASNVDDIRLIKSCADLAVECAFRRESGVIGHDEDNGNVLRAIEFPRIKGGKPFDIDTPWFVQMLAGIGQSKGARVEVSH

Gene
pfp
Protein
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
Organism
Methylomonas methanica
Length
409 amino acids
Function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Similarity
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade P sub-subfamily.
Mass
44.542 kDa
Sequence
MNKPKKVAILTAGGLAPCLNSAIGSLIERYTEIDPSIEIICYRGGYKGLLLGDSYPVTAEVRKKAGVLQRFGGSVIGNSRVKLTNVKDCVKRGLVKEGEDPQKVAADQLVKDGVDILHTIGGDDTNTAAADLAAFLARNNYGLTVIGLPKTVDNDVFPIKQSLGAWTAAEQGARYFMNVVAENNANPRMLIVHEVMGRNCGWLTAATAQEYRKLLDRAEWLPELGLTRESYEVHAVFVPEMAIDLEAEAKRLREVMDKVDCVNIFVSEGAGVEAIVAEMQAKGQEVPRDAFGHIKLDAVNPGKWFGEQFAQMIGAEKTLVQKSGYFARASASNVDDMRLIKSCADLAVECAFRRESGVIGHDEDNGNVLRAIEFPRIKGGKPFNIDTDWFNSMLSEIGQPKGGKVEVSH

Gene
pfp
Protein
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
Organism
Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1)
Length
404 amino acids
Function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Similarity
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade P sub-subfamily.
Mass
43.246 kDa
Sequence
MVKKVALLTAGGFAPCLSSAIAELIKRYTEVSPETTLIGYRYGYEGLLKGDSLEFSPAVRAHYDRLFSFGGSPIGNSRVKLTNVKDLVARGLVASGDDPLKVAADQLIADGVDVLHTIGGDDTNTTAADLAAYLAQHDYPLTVVGLPKTIDNDIVPIRQSLGAWTAADEGARFAANVIAEHNAAPRELIIHEIMGRNCGYLAAETSRRYVAWLDAQQWLPEAGLDRRGWDIHALYVPEATIDLDAEAERLRTVMDEVGSVNIFISEGAGVPDIVAQMQATGQEVPTDAFGHVQLDKINPGAWFAKQFAERIGAGKTMVQKSGYFSRSAKSNAQDLELIAATATMAVDAALAGTPGVVGQDEEAGDKLSVIDFKRIAGHKPFDITLDWYTQLLARIGQPAPIAAA

Gene
pfp
Protein
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
Organism
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Length
404 amino acids
Function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Similarity
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade B2 sub-subfamily.
Mass
44.156 kDa
Sequence
MFKGKVVVAQGGGPTAVINQSMVGAVLESRKFRNVELVYGAVHGVRGIVDEHFLDLTQETTHNLEMVAETPSSALGSTREKPDLKYCQEIFKVLKAHEIGYFFYIGGNDSSDTVRIVSEEAAKADYGLRCIHIPKTIDNDLVVNDHTPGFPSAARFVAQAFSGVNLDNQALPGVYIGVVMGRHAGFLTAASALGKKFQDDGPHLIYLPERTFDVDTFVSDVKEVYDRTGRCIVAVSEGIHDASGEPIITKLAEEVERDAHGNVQLSGTGALADLLVSVVKKKSGIKRVRGDTLGYLQRSFVGCVSDVDQREAREVGEKAVQYAMWGQTNGSVTIHRTGFYSVDYQLTPLLDVAGKTRTMPDSFIAANGHDVTTDFLMYLRPLLGRGMPDAYRLRDNRVAKVLNR

Gene
pfp
Protein
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
Organism
Dictyoglomus thermophilum
Length
346 amino acids
Function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Similarity
Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily.
Mass
37.448 kDa
Sequence
MSKMRIGVLTGGGDCPGLNPAIRGIVMRALDYGDEVIGLKYGWAGLLKADTMPLSLEMVEDILEIGGTILGSSRTNPFKKEEDVQKCVENFKKLNLDALIAIGGEDTLGVASKFSKLGLPMIGVPKTIDKDLEETDYTLGFDTAVEVVVDAIKRLRDTARSHARVIVVEIMGRHAGWLALYGGLAGGADYILIPEVEPNLEDLYNHIRKLYARGRNHAVVAIAEGVQLPGFTYQKGQEGMVDAFGHIRLGGVGNVLAEEIQKNLGIETRAVILSHLQRGGSPSIRDRIMGLLLGKKAVDLVHEGKSGLFVAVKGNELVPVDITLIEGKTKNVDPAFYESVKTFFNK

Gene
pfp
Protein
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
Organism
Amycolatopsis methanolica
Length
341 amino acids
Function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Similarity
Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily.
Mass
36.229 kDa
Sequence
MRVGVLTGGGDCPGLNAVIRAVVRKGIEAHGWEIVGFRSGWRGPLTGDSRPLGLDDVEEILIRGGTILGSSRTNPYKEEGGVEKIRAVLADQGVDALIAIGGEDTLGVAKKLTDDGIGVVGVPKTIDNDLAATDYTFGFDTAVHIATEAIDRLRTTAESHYRAMVVEVMGRHAGWIALHAGLAGGANVILVPERPFSVEQVVEWVERRFEKMYAPIIVVAEGAVPEGGAEVLRTGEKDAFGHVQLGGVGTWLADEIAERTGKESRAVVLGHTQRGGTPTAYDRVLATRFGLHAVDAVADGDFGTMVALRGTDIVRVKLAEATAELKTVPPERYEEAEVFFG

Gene
pfp
Protein
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
Organism
Amycolatopsis mediterranei (strain S699)
Length
341 amino acids
Function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Similarity
Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily.
Mass
36.272 kDa
Sequence
MRVGVLTGGGDCPGLNAVIRAVVRKGIEVHGWDFVGFRNGWNGPLTGDSRPLGLNDVEDILTRGGTILRSSRTNPYKVEGGVDKIKQVLADQGVDALIAIGGEDTLGVAKRLTDDGIGVVGVPKTIDNDLGATDYTFGFDTAVSIATEAIDRLHTTAESHHRALVVEVMGRHAGWIALHSGLAGGASVILVPERHFNVDQVVSWVERRFEKEFAPIIVVAEGALPEGGEEKLLTGEKDAFGHVRLGGIGTWLADEIAHRTGKESRAVVLGHVQRGGTPTAYDRVLATRFGLNAVDAVADGDFGVMVALKGTDIVRVKLSEATAELKTVPVERYQEAEVFFG

Gene
pfp
Protein
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
Organism
Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)
Length
337 amino acids
Function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Similarity
Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily.
Mass
36.834 kDa
Sequence
MKIGVLTGGGDAPGLNIAVYTFVKLAERKHEVYAIYHGWRGLLNKEVKRVSSRDLLDFAFSGGTYIRTSRTNPFKDEERARLLESNVKELGLDVVVAIGGDDTLGAAGEAQRRGILDAVGIPKTIDNDVYGTDYTIGFDSAVNAAIEATESFKTTLISHERIGVVEVMGREAGWIALFTGLSTMADAVLIPERPASWDSVAKRVKEAYNERRWALVVVSEGIKEYGGPKDEYGHSRLGGVGNELAEYIERSTGIEARAVVLGHTIRGVPPTAFDRILAVRYATAAYEAVENGRYGVMVAYSNGDIAYVPIVDVVGKNRLVSGYWMRLYETYWPDLAG