PHS1

Alpha-glucan phosphorylase 1

962 amino acids

Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (By similarity). May be not required for the degradation of starch, but the phosphorolysis of starch may play an important role in water stress tolerance.

Belongs to the glycogen phosphorylase family.

108.585 kDa

MDTMRISGVSTGAEVLIQCNSLSSLVSRRCDDGKWRTRMFPARNRDLRPSPTRRSFLSVKSISSEPKAKVTDAVLDSEQEVFISSMNPFAPDAASVASSIKYHAEFTPLFSPEKFELPKAFFATAQSVRDALIMNWNATYEYYNRVNVKQAYYLSMEFLQGRALSNAVGNLGLNSAYGDALKRLGFDLESVASQEPDPALGNGGLGRLASCFLDSMATLNYPAWGYGLRYKYGLFKQRITKDGQEEAAEDWLELSNPWEIVRNDVSYPIKFYGKVVFGSDGKKRWIGGEDIVAVAYDVPIPGYKTKTTINLRLWSTKAPSEDFDLSSYNSGKHTEAAEALFNAEKICFVLYPGDESTEGKALRLKQQYTLCSASLQDIVARFETRSGGNVNWEEFPEKVAVQMNDTHPTLCIPELMRILMDLKGLSWEDAWKITQRTVAYTNHTVLPEALEKWSLELMEKLLPRHVEIIEKIDEELVRTIVSEYGTADPDLLEEKLKAMRILENVELPSAFADVIVKPVNKPVTAKDAQNGVKTEQEEEKTAGEEEEDEVIPEPTVEPPKMVRMANLAVVGGHAVNGVAEIHSEIVKQDVFNDFVQLWPEKFQNKTNGVTPRRWIRFCNPYLSDIITNWIGTEDWVLNTEKVAELRKFADNEDLQSEWRAAKKKNKLKVVSLIKERTGYTVSPDAMFDIQIKRIHEYKRQLLNILGIVYRYKKMKEMSASEREKAFVPRVCIFGGKAFATYVQAKRIVKFITDVASTINHDPEIGDLLKVIFVPDYNVSVAELLIPASELSQHISTAGMEASGTSNMKFSMNGCVLIGTLDGANVEIREEVGEENFFLFGAKADQIVNLRKERAEGKFVPDPTFEEVKKFVGSGVFGSNSYDELIGSLEGNEGFGRADYFLVGKDFPSYIECQEKVDEAYRDQKRWTRMSIMNTAGSFKFSSDRTIHEYAKDIWNIKQVELP

PHS1

Dual specificity protein phosphatase PHS1

929 amino acids

Probable dual specificity phosphatase that binds and dephosphorylates MPK18, modulating the organization and dynamics of cortical microtubules. Acts as negative regulator of abscisic acid (ABA) signaling during seed germination and light-induced stomata aperture.

104.235 kDa

MAEPEKKRDQPFSQEKDEEKDLYLVHDEHESPLPLTVTSRVLYMLGDIASGPAYRFTQWLDLVRKRSATYGSSGFPHRLHRIDDMVTSAGERNTDPKSPPSRQSSEISLWERLGKASTVDIDSSCFSWNMLSSLHHTEHSSSTDHSEEDQSKPLEVTVNSGGVVFFALFNSSSSEDASRKEEAAVIKFASSRMATQSERLGYEFSKWLGVQIPQARVIHSCNPEWTLIKEATEKAQAKATSEGDEVGEMTCSELLEALELSRCLLLMSYVHGCPMLESMSSFETEEKAERAAAALGRILVLDLVIRNEDRLPCRQLRWRGNPANLLLTDRIVSSAKHHECSFDEAFDSAIKRYHPKDYRSIQRERRASSVDSRSRLSISDQMLVSQASDFSDITESPRSYDTGLMSPMSDRSVAADFHLVAIDSGVPRRPPAGKRASDQEIYPRLVELLLNSSQYSSNLLHEITEGSLGYPQAEDGEETSNVRSVVTPVVREFRNGFRAGLRDLQEFHIFLVTLHQKLDVLLRAFFSMMDKTMCADFDREDFAVPESPSHTHGHEVNHYPSPSKDRVPSDNSSDHSESDMQKSVPRTPNSENKEDGSSPKSRESWHGRSGKGGESLSSQRLAAKLRDFHKFAKVDAESNKELDQWNETLRNEVMKLCQENGFNTGFFEGSDNNSCTDAYELKVRLEHILERISLISKAANTEKPSMIQENLFIGGGLAARSIYTLQHLGITHVLCLCANEIGQSDTQYPDLFEYQNFSITDDEDSNIESIFQEALDFIKHGEETGGKILVHCFEGRSRSATVVLAYLMLQKKLTLLEAWSKLRKVHRRAQPNDGFARILINLDKKCHGKVSMEWRQRKPTMKVCPVCGKNAGLSSSSLKLHLQKSHRKLSSGSVDSAMNMEIQKALEALKLSTGRGSSASSNSFQSHPG

PHS1

Beta-phellandrene synthase (neryl-diphosphate-cyclizing), chloroplastic

778 amino acids

Monoterpene synthase catalyzing the production of beta-phellandrene from neryl diphosphate. Produces also lower amounts of delta-2-carene, alpha-phellandrene and limonene. When incubated in vitro with geranyl diphosphate, catalyzes the formation of acyclic myrcene and ocimene as major products in addition to beta-phellandrene.

Belongs to the terpene synthase family. Tpse subfamily.

90.819 kDa

MIVGYRSTIITLSHPKLGNGKTISSNAIFQRSCRVRCSHSTTSSMNGFEDARDRIRESFGKLELSPSSYDTAWVAMVPSRHSLNEPCFPQCLDWIIENQREDGSWGLNPTHPLLLKDSLSSTLACLLALTKWRVGDEQIKRGLGFIETYGWAVDNKDQISPLGFEVIFSSMIKSAEKLDLNLPLNLHLVNLVKCKRDSTIKRNVEYMGEGVGELCDWKEMIKLHQRQNGSLFDSPATTAAALIYHQHDQKCYQYLNSIFQQHKNWVPTMYPTKVHSLLCLVDTLQNLGVHRHFKSEIKKALDEIYRLWQQKNEQIFSNVTHCAMAFRLLRMSYYDVSSDELAEFVDEEHFFATNGKYKSHVEILELHKASQLAIDHEKDDILDKINNWTRAFMEQKLLNNGFIDRMSKKEVELALRKFYTTSHLAENRRYIKSYEENNFKILKAAYRSPNINNKDLLAFSIHDFELCQAQHREELQQLKRWFEDYRLDQLGLAERYIHASYLFGVTVIPEPELSDARLMYAKYVMLLTIVDDHFESFASKDECFNIIELVERWDDYASVGYKSEKVKVFFSVFYKSIEELATIAEIKQGRSVKNHLINLWLELMKLMLMERVEWCSGKTIPSIEEYLYVTSITFCAKLIPLSTQYFLGIKISKDLLESDEICGLWNCSGRVMRILNDLQDSKREQKEVSINLVTLLMKSMSEEEAIMKIKEILEMNRRELLKMVLVQKKGSQLPQLCKDIFWRTSKWAHFTYSQTDGYRIAEEMKNHIDEVFYKPLNH

PHS1

Protein POOR HOMOLOGOUS SYNAPSIS 1

349 amino acids

Required for accurate chromosome segregation in meiosis. Required for pairing to occur between homologous chromosomes. Acts in early recombination steps and ensures pairing fidelity and proper repair of meiotic DNA double-strand-breaks. Regulates recombination and pairing of homologous chromosomes during meiotic prophase by controlling transport of RAD50 from cytoplasm to the nucleus. May affect pairing of the gene-rich fraction of the genome rather than preventing pairing between repetitive DNA elements.

39.499 kDa

MAGSLTASNRRRNAEDSSEIYRWTIGFARFVHYPSSPSPHPVLKPLGKREQYHSPHGTWLSASSSTVSLHIVDELNRSDVILSVKLGQKVLEEHYISKLNFTWPQMSCVSGFPSRGSRAIFVTYMDSANQIQKFALRFSTCDAALEFVEALKEKIKGLKEASTQNQKNKTRCDVSFQSDYNPSDAIIPRATQKEPNMVRPLNSYVPEMLPRIVYEAQYQKSETRSEVSFQSDYNPSIEIFPRATEEEPNMVRFFDSSVPEVLPRPEYEAGQALYPSQSTLNQIPSLPPSFTTLLSGCFPDSTLDAGQTTVKQNPDLKSQILKYMEDSSFQDMLQKVERIIDEIGGNWIT

PHS1

Protein POOR HOMOLOGOUS SYNAPSIS 1

347 amino acids

Required for accurate chromosome segregation in meiosis. Required for pairing to occur between homologous chromosomes. Acts in early recombination steps and ensures pairing fidelity and proper repair of meiotic DNA double-strand-breaks (PubMed:14704428, PubMed:19918061). Regulates recombination and pairing of homologous chromosomes during meiotic prophase by controlling transport of RAD50 from cytoplasm to the nucleus. May affect pairing of the gene-rich fraction of the genome rather than preventing pairing between repetitive DNA elements (PubMed:19918061).

38.258 kDa

MADAADSSMALVHSSLADSVLTSPRTLRQGQKWEVEYARYFGTPRRDPTAAPPSGLRYIMRGVHRHQGTWIPASCPASLCVCHPSLPSAVPVLTISIGDVVFEEHFVSILNFSWPQVTCVTQCPIRGSRVVFVSFCDKFKQIQKFAVRFPQPCDAESFLSCVECSCGSSGTMDIIPFGSDYVCEDSSASEYIVSNGLHHRLDDASNLEEQCFDHTIDEPPMNYHEETDQHVLEPLSASNTSNNSAFPPSFNQMLKSCSIDYDQEEPCPLAASNHVLQEVYVLDTSHDVANEERTAGKGMDAAEGVDASILTYDLMARIKTYMADESFNDMLLKLDKAIDELGGDMSL

PHS1

Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PHS1

217 amino acids

Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.

Belongs to the very long-chain fatty acids dehydratase HACD family.

24.511 kDa

MSKKLASPLSFLPLYNLLSAVGWSYLLYLVISLYPKVGQPAFFYQTKNVATLVQCGAIIEIINSFLGVVRSPLLTTVAQVSSRLLVVLGIFQLLPNTSGVQSVVYISLLLAWSITEIVRYLYYFFMLVFKNGAPKILILLRYNLFWILYPTGVASELRIIYCALNAAESQYSLLYKRILIAAMLAYIPGFPMLFLHMVAQRKKVMKSLRSSFGKKLI

PHS1

Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PHS1

217 amino acids

Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.

Belongs to the very long-chain fatty acids dehydratase HACD family.

24.511 kDa

MSKKLASPLSFLPLYNLLSAVGWSYLLYLVISLYPKVGQPAFFYQTKNVATLVQCGAIIEIINSFLGVVRSPLLTTVAQVSSRLLVVLGIFQLLPNTSGVQSVVYISLLLAWSITEIVRYLYYFFMLVFKNGAPKILILLRYNLFWILYPTGVASELRIIYCALNAAESQYSLLYKRILIAAMLAYIPGFPMLFLHMVAQRKKVMKSLRSSFGKKLI