ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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Q6CIB4 | MKVAGFILGALIQFSLTEGHVEQNENANLTEMWGEDWPFSGIQTFAHLPHHKCLIDMEKKFDIGVIGVPFDTAVSFRGGARFGPQAIRKASQRQTSMRGFNFRADINPYQDWASVVDCGDVPVTPMDNCLALKMMTAAYENLLSHESQTSDNNLPPRFVTLGGDHSIILPALRALRKTYGRLAVIHFDSHLDTWAPSKYPSFWHSDTSEFTHGSMLWIAHNEGLLTENNNIHAGLRTRLSGSSFEDYDDDDKVGFHRIEADEIMDGGIKSIVEKIKSKIPSDVPVYISVDIDVLDPSAAPGTGTMEVGGWMTRELIRIIRELEDLNLVGADIVEVSPPFDPTEITSLAGAQIAYELITNMVKKGPIDPELIKHNLELSDKLTQGQQLLGFSSPTDELNDKIQKEQFVLQA | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the hydrolysis of 4-guanidinobutanoate to gamma-aminobutyrate (GABA) and urea. Involved in an alternative, arginase-independent arginine degradation pathway via GABA.
Catalytic Activity: 4-guanidinobutanoate + H2O = 4-aminobutanoate + urea
Sequence Mass (Da): 45550
Sequence Length: 410
Pathway: Amino-acid degradation; L-arginine degradation.
EC: 3.5.3.7
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Q9RR46 | MSKIKVEELTKIFGKKASKASSLLSQGKSKTDILKETGATIGVNKASFSVEEGEIFVIMGLSGSGKSTLVRLLNRLIEPTSGKIWLDGKELSSLNKKELLEVRRKSMSMVFQNFGLFPNRTINRNVEYGLEIQGMDKEEREKNAAESLALVGLAGYGDQYPSQLSGGMQQRVGLARALANNPDILLMDEAFSALDPLNRKDMQDQLLDLQDKMKKTIIFITHDLDEALRIGDHIMIMRDGSVVQTGSPEEILAHPANEYVEKFIEDVDRSKVYTASNVMIRPEIVNFEKDGPRVALKRMREAGTSSVFVVKRNRELVGIVHAAEVSKLVKENITSLETALHRDVPTTGLDTPLAEIMDTISTTTIPIAVTEDGKLKGIIIRGSVLAALSGNEVNVNA | Function: Part of the ABC transporter complex GbuABC involved in glycine betaine uptake. Responsible for energy coupling to the transport system. Involved, with BetL and OpuC, in osmoprotection and cryoprotection of Listeria. Can also uptake carnitine when carnitine is abundant in the growth medium.
Catalytic Activity: a quaternary ammonium(out) + ATP + H2O = a quaternary ammonium(in) + ADP + H(+) + phosphate
Sequence Mass (Da): 43626
Sequence Length: 397
EC: 7.6.2.9
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Q9I3S3 | MDKNLHQPLGGNEMPRFGGIATMMRLPHVQSPAELDALDAAFVGVPLDIGTSLRSGTRFGPREIRAESVMIRPYNMATGAAPFDSLNVADIGDVAINTFNLLEAVRIIEQEYDRILGHGILPLTLGGDHTITLPILRAIKKKHGKVGLVHVDAHADVNDHMFGEKIAHGTTFRRAVEEDLLDCDRVVQIGLRAQGYTAEDFNWSRKQGFRVVQAEECWHKSLEPLMAEVREKVGGGPVYLSFDIDGIDPAWAPGTGTPEIGGLTTIQAMEIIRGCQGLDLIGCDLVEVSPPYDTTGNTSLLGANLLYEMLCVLPGVVRR | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes specifically the hydrolysis of 4-guanidinobutanoate to 4-aminobutanoate and urea. Has no activity against arginine, agmatine, 3-guanidinopropionate and guanidinoacetate.
Catalytic Activity: 4-guanidinobutanoate + H2O = 4-aminobutanoate + urea
Sequence Mass (Da): 34728
Sequence Length: 319
EC: 3.5.3.7
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Q9RR45 | MPNIPTIPLASWIDKLVDGLTQFEGFFNVITNIIGGIVDAFQWVFDLVPPWLFIILLVFGTFWVNRKGKKWGLIIFEVVGLLLIWNLDFWRDMTQTLTLVLTSSLIALVIGVPLGIWMAKSNIVESIFKPVLDFMQTMPAFVYLIPAVAFFGIGMVPGVVASVIFAMPPTVRMTNLGIRQVSTELVEAADSFGSTPWQKLWKVQLPMAKSTMMAGINQSIMLALSMVVIASMIGAMGLGTRVYFAVGRNDAGGGFVAGIAIVIVAIILDRLTQAFNKKAKSE | Function: Part of the ABC transporter complex GbuABC involved in glycine betaine uptake. Responsible for the translocation of the substrate across the membrane. Involved, with BetL and OpuC, in osmoprotection and cryoprotection of Listeria. Can also uptake carnitine when carnitine is abundant in the growth medium.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30919
Sequence Length: 282
Subcellular Location: Cell membrane
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Q9RR44 | MLKKLITTAVLAMLIFTLAACGTTLAPYDAKKDLGEQINYTITGIDAGAGIMLATQNAIKDYHLDDDNWQLQTSSTAAMTSTLQKAMKDKRPIVVTGWTPHWMFTKFDLKFLDDPKNVYGNAENIHTIVRKGLKEDKPSAYQVLDNFFWTAEDMSEVMLEVNDGVDPEEAAKKWIKNNPDKVAKWTDGVEKVDGDEIKLTYVAWDSEIASTNVVAEALKQVGYKPTIQAMEIQPMWASVATDAADGMVAAWLPNTSGIYYKDYKGKFEDLGPNLKGAKIGLAVPKYMTNINSIEDLKTSK | Function: Part of the ABC transporter complex GbuABC involved in glycine betaine uptake. Involved, with BetL and OpuC, in osmoprotection and cryoprotection of Listeria. Can also uptake carnitine when carnitine is abundant in the growth medium.
Location Topology: Lipid-anchor
Sequence Mass (Da): 33276
Sequence Length: 300
Subcellular Location: Cell membrane
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O36362 | MAHTGSTVCAFLIFAVLKNVFCQTPTSSSEVEDVIPEANTVSDNIIRQQRNNTAKGIHSDPSAFPFRVCSASNIGDIFRFQTSHSCPNTKDKEHNEGILLIFKENIVPYVFKVRKYRKIVTTSTIYNGIYADAVTNQHVFSKSVPIYETRRMDTIYQCYNSLDVTVGGNLLVYTDNDGSNMTVDLQPVDGLSNSVRRYHSQPEIHAEPGWLLGGYRRRTTVNCEVTETDARAVPPFRYFITNIGDTIEMSPFWSKAWNETEFSGEPDRTLTVAKDYRVVDYKFRGTQPQGHTRIFVDKEEYTLSWAQQFRNISYCRWAHWKSFDNAIKTEHGKSLHFVANDITASFYTPNTQTREVLGKHVCLNNTIESELKSRLAKVNDTHSPNGTAQYYLTNGGLLLVWQPLVQQKLLDAKGLLDAVKKQQNTTTTTTTTRSRRQRRSVSSGIDDVYTAESTILLTQIQFAYDTLRAQINNVLEELSRAWCREQHRASLMWNELSKINPTSVMSSIYGRPVSAKRIGDVISVSHCVVVDQDSVSLHRSMRVPGRDKTHECYSRPPVTFKFINDSHLYKGQLGVNNEILLTTTAVEICHENTEHYFQGGNNMYFYKNYRHVKTMPVGDVATLDTFMVLNLTLVENIDFQVIELYSREEKRMSTAFDIETMFREYNYYTQRVTGLRRDLTDLATNRNQFVDAFGSLMDDLGVVGKTVLNAVSSVATLFSSIVSGIINFIKNPFGGMLLFGLIAAVVITVILLNRKAKRFAQNPVQMIYPDIKTITSQREELQVDPISKHELDRIMLAMHDYHASKQPESKQDEEQGSTTSGPADWLNKAKNVLRRRAGYKPLKRTDSFESTGVP | Function: Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress.
PTM: A proteolytic cleavage by host furin generates two subunits that remain linked by disulfide bonds.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 97060
Sequence Length: 854
Subcellular Location: Virion membrane
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P17471 | MAARGGAERAAGAGDGRRGQRRHLRPGRVLAALRGPAAPGAGGARAALAAALLWATWALLLAAPAAGRPATTPPAPPPEEAASPAPPASPSPPGPDGDDAASPDNSTDVRAALRLAQAAGENSRFFVCPPPSGATVVRLAPARPCPEYGLGRNYTEGIGVIYKENIAPYTFKAIIYYKNVIVTTTWAGSTYAAITNQYTDRVPVGMGEITDLVDKKWRCLSKAEYLRSGRKVVAFDRDDDPWEAPLKPARLSAPGVRGWHTTDDVYTALGSAGLYRTGTSVNCIVEEVEARSVYPYDSFALSTGDIIYMSPFYGLREGAHREHTSYSPERFQQIEGYYKRDMATGRRLKEPVSRNFLRTQHVTVAWDWVPKRKNVCSLAKWREADEMLRDESRGNFRFTARSLSATFVSDSHTFALQNVPLSDCVIEEAEAAVERVYRERYNGTHVLSGSLETYLARGGFVVAFRPMLSNELAKLYLQELARSNGTLEGLFAAAAPKPGPRRARRPRRLRPAPGRGQRARRRRHAGGRVTTVSLAEFAALQFTHDHTRTSEHHVHRLASPWCLLQNKERALWAEAAKLNPSAAASAALDRRAAARMLGDAMAVTYCHELGEGRCSSRTRMRAPGGVCYSRRGSFFGNESEPVEGQLGEDNELLPGRELVEPCTANHKRYFRFGADYVYYENYAYVRRVPLAELEVISTFVDLNLTVLEDREFLPLEVYTRAELADTGLLDYSEIQRRNQLHELRFYDIDRVVKTDGNMAIMRGLANFFQGLGAVGQAVGTVVLGAAGAALSTVSGIASFIANPFGALATGLLVLAGLVAAFLAYRYISRLRSNPMKALYPITTRALKDDPGRNRPGEEEEEFDAAKLEQAREMIKYMSLVSAVERQEHKAKKSNKAARLLATRLTQLALRRRAPPEYQQLPMADVGGA | Function: Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress.
PTM: A proteolytic cleavage by host furin generates two subunits that remain linked by disulfide bonds.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 101950
Sequence Length: 928
Subcellular Location: Virion membrane
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P03188 | MTRRRVLSVVVLLAALACRLGAQTPEQPAPPATTVQPTATRQQTSFPFRVCELSSHGDLFRFSSDIQCPSFGTRENHTEGLLMVFKDNIIPYSFKVRSYTKIVTNILIYNGWYADSVTNRHEEKFSVDSYETDQMDTIYQCYNAVKMTKDGLTRVYVDRDGVNITVNLKPTGGLANGVRRYASQTELYDAPGWLIWTYRTRTTVNCLITDMMAKSNSPFDFFVTTTGQTVEMSPFYDGKNKETFHERADSFHVRTNYKIVDYDNRGTNPQGERRAFLDKGTYTLSWKLENRTAYCPLQHWQTFDSTIATETGKSIHFVTDEGTSSFVTNTTVGIELPDAFKCIEEQVNKTMHEKYEAVQDRYTKGQEAITYFITSGGLLLAWLPLTPRSLATVKNLTELTTPTSSPPSSPSPPAPSAARGSTPAAVLRRRRRDAGNATTPVPPTAPGKSLGTLNNPATVQIQFAYDSLRRQINRMLGDLARAWCLEQKRQNMVLRELTKINPTTVMSSIYGKAVAAKRLGDVISVSQCVPVNQATVTLRKSMRVPGSETMCYSRPLVSFSFINDTKTYEGQLGTDNEIFLTKKMTEVCQATSQYYFQSGNEIHVYNDYHHFKTIELDGIATLQTFISLNTSLIENIDFASLELYSRDEQRASNVFDLEGIFREYNFQAQNIAGLRKDLDNAVSNGRNQFVDGLGELMDSLGSVGQSITNLVSTVGGLFSSLVSGFISFFKNPFGGMLILVLVAGVVILVISLTRRTRQMSQQPVQMLYPGIDELAQQHASGEGPGINPISKTELQAIMLALHEQNQEQKRAAQRAAGPSVASRALQAARDRFPGLRRRRYHDPETAAALLGEAETEF | Function: Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress.
PTM: A proteolytic cleavage by host furin generates two subunits that remain linked by disulfide bonds.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 95639
Sequence Length: 857
Subcellular Location: Virion membrane
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B2IBC4 | MDDVVKSLLQRTTSSLTKPAPARPSREEAEAAVEVLLRWTGDDPSREGLRDTPKRVVKAFEEFFSGYNADASDVLSRVFEEVHGYDNMVLVRDIPFSSHCEHHMVPFFGVAHIGYYPSEAGVIGLSKLARLVDIFAKRLQTQEALTAQIIGAIDEHLQPRGCAIMLEAEHMCMSMRGVQKHGTSTLTTQFTGVFKNDPAEQVRFFGMVRNPKS | Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 23769
Sequence Length: 213
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
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Q8G3S1 | MNEYIESCHREKHTYDEEGVREAVRLFLKSIGEDPEREGLVETPDRIARACRELFTGLQASPADALEKHFDVDTDELVLVKDIELYSVCEHHLLPFHGVAHVGYIPAKDGVMGLSKLARLVEVYARRPQVQERLTQQIADALVEYAGARGVIVVTECEHLCMSMRGIKKSSARTVTSAVRGMLRNPATRAEAMSLILDK | Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 22302
Sequence Length: 199
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
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Q492J7 | MSILTQEALLVRDALSVRGLENPLIELNINHKIRKRRIENHMRAIVHLLNLDLEHDSLLNTPKRIAKMYIEEIFSGLDYSNFPKIAIIQNTMQINEMITVRGINITSTCEHHFIVFNGKVTISYIPEKNVIGLSKINRIVQFFSKRPQLQERLTKQIFLALQTLLNTDNVAIFIDAVHYCVKARGIHDVSSTTTTTALGGLFESNTNTREEFLHAIMYCNH | Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 25354
Sequence Length: 221
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
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Q89IW2 | MDATIKSIRPSKPSDRQPESRPAELDPAEFLAAAVRADQPRPARAQAEAAVKTLLAYIGENTEREGLLDTPRRVVEAFDELYQGYHQCPAEVLDRTFGETAGYDDFVLVRDIEFTSQCEHHMMPFYGKAHIAYTPVERVVGLSKLARLTDIFARRLQTQEHLTAQIAAAIDEVLKPRGVAVLIEAEHTCMSVRGVAKHGASTFTSRFTGMFRDNPAEQARFLSLVRGTR | Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 25543
Sequence Length: 229
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
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A5VQL0 | MDARIFQDNDDTSLPVNQASVTRIHKKPGKAEAEAAVRTLLLWVGEDPDREGLLETPKRVAKAYQELFGGYSGSPEEVLGTTFEEVAGYDDMVLVKDISFFSHCEHHMVPIIGKAHVAYLPEGRVVGLSKIARVVDIFARRLQTQESITAQIADSIQRILKPRGVAVMIEAEHMCMAMRSIRKQGSSTITTTFTGDFKEKADQQVRFMTLIRT | Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 23766
Sequence Length: 213
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
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Q19980 | MSRIENESGFLSSDAASVGSEDDKVEMKKRNGTIPKEDHLKSMCNAYQSIIQHVGEDINRQGLLKTPERAAKAMMAFTKGYDDQLDELLNEAVFDEDHDEMVIVKDIEMFSLCEHHLVPFMGKVHIGYIPNKKVLGLSKLARIVEMFSRRLQVQERLTKQIATAMVQAVQPSGVAVVIEASHMCMVMRGVQKINASTTTSCMLGVFRDDPKTREEFLNLINKR | Function: Involved in serotonin and dopamine biosynthesis that affects movement, mating behavior, foraging behavior, and cell migration.
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 25132
Sequence Length: 223
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
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Q8ZWW5 | MITDRKAKAKPERGVEELLEYLGEDLTKPGVLNTPKRFVKAMEELTRGLREPPPEVVFFPLEYDVELGPVVIENIGAVSLCEHHLLPILLRISVAYVPGDGVPGLSKVIRLVKWAAARPIMQERFTEWLADLLMEKLRAKGVQVKVCGVHMCSFIRGVKDEHHNMITEARRGEIDVKLSCKRPLGCR | Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 21088
Sequence Length: 187
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
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Q7UJJ7 | MFRESDNTIAPSNQDLNKPVVDKEQPAERTPFFVDKNAPHNEVDFARIESAVREILEAVGEDPDRDGLLETPERVARMYAEMFAGLKSDPGRHLAKVFAEDYDEIVLVRDISFCSMCEHHLLPFTGKAHIAYLPSGKVVGLSKLARVVEEVARRPQVQERLTHTVANLIEDRLSARGVAVVVESTHSCMTMRGIRKPGSLCLTSAMRGAFKTDPKSRAEVLGLINRAAS | Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 25410
Sequence Length: 229
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
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Q2SLC0 | MQIVRALPDIAKTRTEFETYTLQWVGMEDIAVPLTLNIGGGKQQSLPAKANVYVSLDDAAEKGIHMSRLHAILNQLASQVCDKEGLDLLLRNMVASQGKISRSAKVELVFDLLLPKPSLLSNETGFQTYRIEIGGQCLSEKYDYSLKITVPYSSTCPCSAALSRQLFSDAIDNEFSTSRIDKQELLSWALTSTVATPHSQRSYAYLNLLLGNHGWPSLSSFIMQIEEAIGTPVQTMVKRTDEQEFARLNADNLMFCEDAARNVKTLLEQSSWIEDYWFKVEHQESLHAHNAVVIDQKYSKGAML | Function: Converts GTP to 7,8-dihydroneopterin triphosphate.
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 34042
Sequence Length: 304
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
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Q9KE60 | MKTKQWPSKTERHKRFGSVPPVAGKKPIHKEEMADLQNMPNDFLFALDSVGIHNVKHPCIIQSNLKPYEQTTVGTFSLTTGLEQMSKGINMSRLTELLQEYHQTGFILSLKNMQAFTKDLAERMEQSSAHVHVTFPWFFERESPSLNKIGLAHAEARLNVHFDETLGFTHEVGLTAAVTTLCPCSKEISEYSAHNQRGYVTIKATFYEPTEGSDDWKVTLLEAAESNASSILYPVLKRPDEKAVTEKAYENPRFVEDMVRLTAADLYENETIKAFTVECRNEESIHQHDAIATLSYSKK | Function: Converts GTP to 7,8-dihydroneopterin triphosphate.
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 33899
Sequence Length: 299
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
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Q5R041 | MPTVMPDVANQTQAQTEGALDWVGMSNIEVPLMVAAAGVPERPVAAKVEAFVNLKNPKTKGIHMSRLYLLLDKMSTEGELSHDTLKQLLNDFIESHKDISDQAFIKFDFDYHLRRKSLISKKQGWKAYPVSLTGRYDAGQLKLELSVDVPYSSTCPCSAALARQLIQDAFSEKFAGQEQVDASIMHEWLGSTEGIVATPHSQRSVAEVKVALSDSVNDFPIVELIDAIEGALKTPVQAAVKREDEQEFARLNGQNLMFCEDASRRLQHQLNQMSNFRDFWLRVNHYESLHAHDAVSVTTKGVPGGYSA | Function: Converts GTP to 7,8-dihydroneopterin triphosphate.
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 34233
Sequence Length: 308
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
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Q6U5S4 | MLPDIQSTKGDGEGESLSWVGMEQIDLPIDIAGRPVSAKVNAGINLLSSPEAEKGIHMSRLYLLLDELTQGEITPALLQHVLKAFLVSHQGRSDEASIEISGDLLLSRKSLNSNHSGWKAYPLTLSAELRQSFTVTLKVGIPYSSTCPASAALSRHVAGLQFSKDFGNRIDRLPAAEIADWLVEKGMPATPHSQRSWAWVDIRLNPEAKSLPVLELIDYAEVALGTAVQTVVKRSDEQAFAVANGQNLMFCEDAARRLNNVFRCASFCEAFDIRVEHQESLHPHNAVARIHWKGSKNVT | Function: Converts GTP to 7,8-dihydroneopterin triphosphate.
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 32801
Sequence Length: 299
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
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C5CEC0 | MRDVQSEKDHRNIPINMVGIKGLKYPIIVMDRTNKRQHTIGTFNLFVDLPKDFRGTHMSRFVEVLDRHNMKVTPKNMESILDDMREALKATVAHVTVDFPYFIRKNAPISGIGSYSSYNCGFISTKNKEFDFILKVEVPVLTVCPCSKEISDRGAHNQRAMVNVQVRMNSLVWIEEIIEMVEDAASAPIFTLLKREDEKFITEVSYDNPRFVEDVSREVVLRFMNDPRISWYRVEVSSQESIHNHEAYACIEKGKSL | Function: Converts GTP to 7,8-dihydroneopterin triphosphate.
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 29720
Sequence Length: 257
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
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Q1MPD2 | MKDIQSTPAQIAFPIDRVGVKGLKFPIQIQTRDIGMQHTVAIVDMGVDLSVSSRGTHMSRFVEVLQDWNEPLCCESLERLVKQTQKKLQSQHAYIAFFFPYFLHKRAPSTNMLSLFSYDCKLSAKSINYNIEFILELTVPVMTVCPCSKAISHEGAHSQRSEIYIQLRLEQFRFIEDFIVLAESSASSPLYSLLKRADEKYVTEDAFAHPKFVEDVVRNISSKLITVTDVLGFRVEVESFESIHAHNAFAYIEHEFIC | Function: Converts GTP to 7,8-dihydroneopterin triphosphate.
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 29492
Sequence Length: 258
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
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A2SJ45 | MTHASALGLTQHIPDTQSERDERHLAIQRVGVKEVRYPLTVRIGEQLSPTVASWSLDVALPAEQKGTHMSRFVAWLDALSASGKPLDATALRDELAVMLDKLHAVEGRIEARFPFFIRKHAPVSGVSSLLDYQGAWIAEHRAGSGTTVWCEVVVPVKSLCPCSKEISDYGAHNQRSHVTIRAELMEPPGDRRRPPPPGGGESTRERPVVDSAVELGFEALVRFAEASASSEIWGLLKRPDEKWITERAYENPKFVEDLVRDVALRLNADARIGRYRVEVENFESIHNHSAFAVIERE | Function: Converts GTP to 7,8-dihydroneopterin triphosphate.
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 33097
Sequence Length: 297
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
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Q5F9K6 | MNAIADVQSSRDLRNLPINQVGIKDLRFPITLKTAEGTQSTVARLTMTVYLPAEQKGTHMSRFVALMEQHTEVLDFAQLHRLTAEMVALLDSRAGKISVSFPFFRKKTAPVSGIRSLLDYDVSLTGEMKDGAYGHSMKVMIPVTSLCPCSKEISQYGAHNQRSHVTVSLTSDAEVGIEEVIDYVETQASCQLYGLLKRPDEKYVTEKAYENPKFVEDMVRDVATSLIADKRIKSFVVESENFESIHNHSAYAYIAYP | Function: Converts GTP to 7,8-dihydroneopterin triphosphate.
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Mass (Da): 28747
Sequence Length: 257
Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
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P0AEP8 | MAKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATAGNIGVCLGTSGPAGTDMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDVQVAEIEFDPDMYEPLPVYKPAASRMQIEKAVEMLIQAERPVIVAGGGVINADAAALLQQFAELTSVPVIPTLMGWGCIPDDHELMAGMVGLQTAHRYGNATLLASDMVFGIGNRFANRHTGSVEKYTEGRKIVHIDIEPTQIGRVLCPDLGIVSDAKAALTLLVEVAQEMQKAGRLPCRKEWVADCQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPKRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQRAFDMDYCVQLAFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKALMAQYRVPVVVEVILERVTNISMGSELDNVMEFEDIADNAADAPTETCFMHYE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the condensation of two molecules of glyoxylate to give 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde).
Catalytic Activity: 2 glyoxylate + H(+) = 2-hydroxy-3-oxopropanoate + CO2
Sequence Mass (Da): 64732
Sequence Length: 593
Pathway: Organic acid metabolism; glycolate degradation; 3-phospho-D-glycerate from glycolate: step 2/4.
EC: 4.1.1.47
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Q9NP62 | MEPDDFDSEDKEILSWDINDVKLPQNVKKTDWFQEWPDSYAKHIYSSEDKNAQRHLSSWAMRNTNNHNSRILKKSCLGVVVCGRDCLAEEGRKIYLRPAICDKARQKQQRKRCPNCDGPLKLIPCRGHGGFPVTNFWRHDGRFIFFQSKGEHDHPKPETKLEAEARRAMKKVNTAPSSVSLSLKGSTETRSLPGETQSQGSLPLTWSFQEGVQLPGSYSGHLIANTPQQNSLNDCFSFSKSYGLGGITDLTDQTSTVDPMKLYEKRKLSSSRTYSSGDLLPPSASGVYSDHGDLQAWSKNAALGRNHLADNCYSNYPFPLTSWPCSFSPSQNSSEPFYQQLPLEPPAAKTGCPPLWPNPAGNLYEEKVHVDFNSYVQSPAYHSPQEDPFLFTYASHPHQQYSLPSKSSKWDFEEEMTYLGLDHCNNDMLLNLCPLR | Function: Transcription factor involved in the control of expression of placental growth factor (PGF) and other placenta-specific genes . Binds to the trophoblast-specific element 2 (TSE2) of the aromatase gene enhancer . Binds to the SYDE1 promoter . Has a central role in mediating the differentiation of trophoblast cells along both the villous and extravillous pathways in placental development .
PTM: Polyubiquitinated in the presence of UBE2D2 and FBXW2 (in vitro).
Sequence Mass (Da): 49268
Sequence Length: 436
Subcellular Location: Nucleus
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P70348 | MELDDFDPEDKEILSWDINDVKLPQNVKTTDWFQEWPDSYVKHIYSSDDRNAQRHLSSWAMRNTNNHNSRILKKSCLGVVVCSRDCSTEEGRKIYLRPAICDKARQKQQRKSCPNCNGPLKLIPCRGHGGFPVTNFWRHDGRFIFFQSKGEHDHPRPETKLEAEARRAMKKVHMASASNSLRMKGRPAAKALPAEIPSQGSLPLTWSFQEGVQLPGTYSTPLIANAPQQNSLNDCLSFPKSYDLGGSTELEDPTSTLDSMKFYERCKFSSSRIYGSEEQFQPPVPGTYGDYEDLQTWNKNVALGRNPSDDIYYPAYPLPVASWPYDYFPSQNSLEHLPQQVPSEPPAAQPGCHPLWSNPGGEPYEEKVSVDLSSYVPSLTYHPPQQDPFLLTYGSPTQQQHALPGKSNRWDFDEEMACMGLDHFNNEMLLNFCSLR | Function: Transcription factor that is necessary for placental development . Involved in the control of expression of placental growth factor (PGF) and other placenta-specific genes. Binds to the trophoblast-specific element 2 (TSE2) of the aromatase gene enhancer. Binds to the SYDE1 promoter. Has a central role in mediating the differentiation of trophoblast cells along both the villous and extravillous pathways in placental development (By similarity).
PTM: Polyubiquitinated in the presence of UBE2D2 and FBXW2 (in vitro).
Sequence Mass (Da): 49589
Sequence Length: 436
Subcellular Location: Nucleus
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O75603 | MPAAAVQEAVGVCSYGMQLSWDINDPQMPQELALFDQFREWPDGYVRFIYSSDEKKAQRHLSGWAMRNTNNHNGHILKKSCLGVVVCTQACTLPDGSRLQLRPAICDKARLKQQKKACPNCHSALELIPCRGHSGYPVTNFWRLDGNAIFFQAKGVHDHPRPESKSETEARRSAIKRQMASFYQPQKKRIRESEAEENQDSSGHFSNIPPLENPEDFDIVTETSFPIPGQPCPSFPKSDVYKATCDLATFQGDKMPPFQKYSSPRIYLPRPPCSYELANPGYTNSSPYPTLYKDSTSIPNDTDWVHLNTLQCNVNSYSSYERSFDFTNKQHGWKPALGKPSLVERTNHGQFQAMATRPYYNPELPCRYLTTPPPGAPALQTVITTTTKVSYQAYQPPAMKYSDSVREVKSLSSCNYAPEDTGMSVYPEPWGPPVTVTRAASPSGPPPMKIAGDCRAIRPTVAIPHEPVSSRTDEAETWDVCLSGLGSAVSYSDRVGPFFTYNNEDF | Function: Transcription factor that binds specific sequences on gene promoters and activate their transcription. Through the regulation of gene transcription, may play a role in parathyroid gland development.
Sequence Mass (Da): 56610
Sequence Length: 506
Domain: The C-terminal conserved inhibitory domain (CCID) negatively regulates the transcriptional activity of the protein.
Subcellular Location: Nucleus
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O09102 | MPADSTQDEDAVLSYGMKLTWDINDPQMPQEPTHFDHFREWPDGYVRFIYSSQEKKAQRHLSGWAMRNTNNHNGHILKKSCLGVVVCARACALKDGSHLQLRPAICDKARLKQQKKACPNCHSPLELVPCRGHSGYPVTNFWRLDGNAIFFQAKGVHDHPRPESKSETEGRRSALKRQMASFYQPQKRRSEEPEARSTQDIRGHLNSTAALEPTELFDMTADTSFPIPGQPSPSFPNSDVHRVTCDLPTFQGDIILPFQKYPNPSIYFPGPPWGYELASSGVTGSSPYSTLYKDSSVVPDDPDWIPLNSLQYNVSSYGSYERTLDFTARYHSWKPTHGKPSLEEKVDCEQCQAVPTSPYYNLELPCRYLPVPAAGTQALQTVITTTVAYQAYQHPALKHSDSMQEVSSLASCTYASENLPMPIYPPALDPQEGVIQAASPSGRAPLKVPGDCQAPRPTLDFPQEADPSGTDGADVWDVCLSGVGSVMGYLDRTGQPFSFDNEDF | Function: Transcription factor that binds specific sequences on gene promoters and activate their transcription. Through the regulation of gene transcription, may play a role in parathyroid gland development.
Sequence Mass (Da): 56039
Sequence Length: 504
Domain: The C-terminal conserved inhibitory domain (CCID) negatively regulates the transcriptional activity of the protein.
Subcellular Location: Nucleus
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P03069 | MSEYQPSLFALNPMGFSPLDGSKSTNENVSASTSTAKPMVGQLIFDKFIKTEEDPIIKQDTPSNLDFDFALPQTATAPDAKTVLPIPELDDAVVESFFSSSTDSTPMFEYENLEDNSKEWTSLFDNDIPVTTDDVSLADKAIESTEEVSLVPSNLEVSTTSFLPTPVLEDAKLTQTRKVKKPNSVVKKSHHVGKDDESRLDHLGVVAYNRKQRSIPLSPIVPESSDPAALKRARNTEAARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVGER | Function: Master transcriptional regulator that mediates the response to amino acid starvation . Binds variations of the DNA sequence 5'-ATGA[CG]TCAT-3' in canonical nucleosome-depleted 5'-positioned promoters, and also within coding sequences and 3' non-coding regions . During nutrient starvation (low or poor amino acid, carbon or purine sources), it activates genes required for amino acid biosynthesis and transport, autophagy, cofactor biosynthesis and transport, mitochondrial transport, and additional downstream transcription factors . Activates transcription by recruiting multiple coactivators, including the mediator complex, the SAGA complex, and the SWI/SNF complex, to enable assembly of the pre-initiation complex at core promoters .
PTM: Phosphorylated by the cyclin-CDK PCL5-PHO85. Phosphorylation of Thr-165 induces degradation of GCN4 by the E3 ubiquitin ligase complex SCF(Cdc4).
Sequence Mass (Da): 31310
Sequence Length: 281
Domain: Residues 89 to 100 and 106 to 125 define the N-terminal activation domain (NTAD) and the central acidic activation domain (CAAD) respectively, which can function independently to promote high-level transcription of the target genes.
Subcellular Location: Nucleus
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Q9AR19 | MDSHSSHLNAANRSRSSQTPSPSHSASASVTSSLHKRKLAATTAANAAASEDHAPPSSSFPPSSFSADTRDGALTSNDELESISARGADTDSDPDESEDIVVDDDEDEFAPEQDQDSSIRTFTAARLDSSSGVNGSSRNTKLKTESSTVKLESSDGGKDGGSSVVGTGVSGTVGGSSISGLVPKDESVKVLAENFQTSGAYIAREEALKREEQAGRLKFVCYSNDSIDEHMMCLIGLKNIFARQLPNMPKEYIVRLLMDRKHKSVMVLRGNLVVGGITYRPYHSQKFGEIAFCAITADEQVKGYGTRLMNHLKQHARDVDGLTHFLTYADNNAVGYFVKQGFTKEIYLEKDVWHGFIKDYDGGLLMECKIDPKLPYTDLSSMIRQQRKAIDERIRELSNCQNVYPKIEFLKNEAGIPRKIIKVEEIRGLREAGWTPDQWGHTRFKLFNGSADMVTNQKQLNALMRALLKTMQDHADAWPFKEPVDSRDVPDYYDIIKDPIDLKVIAKRVESEQYYVTLDMFVADARRMFNNCRTYNSPDTIYYKCATRLETHFHSKVQAGLQSGAKSQ | Function: Acetylates histone H3 and ADA2 proteins in vitro. Acetylates 'Lys-14' of histone H3. Acetylation of histones gives a specific tag for epigenetic transcription activation. Operates in concert with certain DNA-binding transcriptional activators. Acts via the formation of large multiprotein complexes that modify the chromatin (By similarity).
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Mass (Da): 63124
Sequence Length: 568
Domain: The N-terminal part (1-150) is not required for interactions with the ADA2 proteins.
Subcellular Location: Nucleus
EC: 2.3.1.48
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P93255 | MALRMWASSAANALGVSCAPKSHLLPALSLSRCFSTVLDGLKYASSHEWVKHGGSVATIGITDHAQGHLGDVVFAELPEGGAVSAGKPFASVESVKATSDVNSPISGEIVEVNTKLSDSPGLLNSSPYEEGWMVKVKPSNPAELESLMGSKEYTKFCEEEDAH | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Sequence Mass (Da): 17131
Sequence Length: 163
Subcellular Location: Mitochondrion
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Q9HII1 | MDELLSMLNFLGMKDPEELFSDIPKSVRKKSIGIGGGLDEYRVIDRAMEIGRKNKTDMINFLGNGIYDRVIPEAVNYILSKPEFLDSYTPYQPEISQGMLQSMFEYQSLISDLMGMDVTNASMYDGYSALGEAARMAYRINGHSKILVPESSYDSKISVLRNYIWGLNMKIMKYRIGEDGMIDLDDLSSKIDSDTSAIVVENPNGYGILDKNIFGVKDIKKDAVLISYVDPISLGVVKPPGEYGSDIAVAEGQQLGIPMNFGGPLLGLMSFKMEHIRRSPGRIIGESIDSNGKRAYVMTLQTREQHIRRAKATSNICSNQALLTLAASAYLSIMGSTGLRKVALLTIKHSRMIKEKLSSIGVKPYFSTESFSDVMFRLERDVMEALASKNILGGLKLRQLISDTPMKDATFFTVTEKTDAAAIEKLAAALEVI | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 47937
Sequence Length: 433
EC: 1.4.4.2
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Q5JGX5 | MGKHYIPNSAHKDEMLKEIGFSSIEDLFSDVPKGMVKEFNLPEGKSEYEVFTELNETLSKNKTVLEMPSFLGAGTYFHYVPAHVKYLIERSEFLTAYTPYQPEISQGMLQALFEYQSLIAELVGLPIVNSSMYDWGTAMAEAALMSARVTKRNKFVVPKHLSPEKKLVLKTYTAGPGLETVEVPWDERGQMDIEKLKEAVEGAAGVYIEMPNFFGLLEENIREIGEIAHDAGALFVVGVDPTILGIVEAPGELGADIVVGEAAYFGNPMNFGGPRAGIFAVRNDRKLIRQMPGRIIGMTKDADGKRAFVMTLQTREQHIRRAKATSNICSNEALVAVAAAIHLATLGPKGVRELGEVILKNTAYLKKRLAEVGEIVFDGVNFKDVPVRFEVPYSVIHERLLERNIHGGYYIGKHFQELGETALFAATETTRKEWVDGLVDALREIIGEAEL | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 50014
Sequence Length: 451
EC: 1.4.4.2
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Q9WY56 | MNYPYIPHTDEDVRAMLDFIGVSSIEELFSSIPVSARSSLNIPESRDEFSVFKQLKEISEMNNSLEDYAVFLGAGVYKRYVPTVVYDLAMKPDFLTAYTPYQAEVSQGTLQALFEYQTMVCELTGMEVANASMYDGATALAEAALMSFRLTGKEKVVVARSVHPEYRAVLRTYLEKRGFTVVEAGYDETGRVLLEEVDEETAAIAVQYPNFFGIIEDLDYVRSRSGNALLIVVVEPVSLALLEPPGSYGADIVVGEGQSLGLPMWFGGYSLGIFATREEYVRQMPGRLIGQTVDQAGNTAYTMILQTREQHIRRARATSNICSNHAHAALIAAVYMSVMGPDGLKEVARRSYNAAHYLQERLEEIGFKLCFSGEFFNEFVFNVPEDYPDRWRKMMEKKILGPLPLEEFYPELGDTALACATEVISKEDIEKLLEAMK | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 48942
Sequence Length: 437
EC: 1.4.4.2
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Q3SMB8 | MPFIPHTEEDVSAMLGAIGAASIEDLFDEIPPALKTGKLKDVPDGLPEMAVARLMQERASQDGFWSNFIGAGVYEHHIPAAIWQITTRGEFYSAYTPYQAEASQGTLQLIYEYQTMMTRLTGLDVSNASLYDGASALAEAVLMAVRSHKSSRRVLVPKTVHPVYRSVVVTTVRNQGIDLVELEYDPATGKTVLPSEPGAFAGLVIPQPNFFGVLEDVHTMTDWTHANGGLAIALVNPTTLAVLEAPGKWGTKGADIAVGEGQPLGAPMASGGPYFGFMCCRQDFVRQMPGRIVGRTVDLDGKPGFALTLQAREQHIRRSKATSNICTNQGLVVTAATQYMALLGPQGLAKVAAASHANTVALAEKLGAIPGVARAFASPCFHEVVLKLDDGTLKGTSAKDVLRALRAQGILGGLDISGWYPELGQAILVCVTETKTGADLDHYAQHLERILSKRREAPPCAYKN | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 49680
Sequence Length: 464
EC: 1.4.4.2
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Q9YA18 | MWRQSRWNEPLITEMSRRGRRGALPPRPDEKVVKEVGPLKLPQSLARGSPPSLPEVSEVEVVRHYTRLSQMAYGVDNGPVPLGSCTMKYNPRVAARLAFDPRLETLHPLQDDETVQGVLEAIYMVQEWLRHITGMDACTVHPAAGSQGELAGVLMIKRFHEMRGDLDKRRVIIVPDSAHGTNPASAAMGGFQVVEVPTGDDGNVDMEALKAAVGGDTAGLMITNPSTLGLFEENILEISRLVHEAGGLLYYDGANLNGIIGRARPGDMEFDIAHVNLHKTFSVPHGGGGPGSGPVCVKRVEVVDGVTLEDLLPGPRVVYSREEGLYRVRPPGRWSVGRLRAWIANTLAVLWAYAYILAMGPQGLRLAGEVSVVNTNYFIRLMEGHWGYSLPYAPSRPRKHEVVLSAKPLKRETGATAEDVAKGLLDAGLYAPTIYFPLIVEEALMIEFTESETKENIEAYAARLKEIAEEARRDPSTPRKWPRNTTSARVDNVRANHPRTVTPTWRVEVLRRQGKLGPLR | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 57349
Sequence Length: 520
EC: 1.4.4.2
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Q0AVH9 | MSKVIFARSVAGGGGFFLPPCDVAEIEPAAEINPEFLRAEAPLLPELSEVEVVRHYVELSQRAYGVDNGFYPLGSCTMKYNPKINEWAARLPGFANLHPYQPEESVQGALELLYRAEKLCCEIGGMDRFTLQPAAGAHGELTGLMIIKAYHQHRQDLARTKILVPDSAHGTNPATAHVLGFEVVEVKSNEEGLVDLQDLKACMSSEVAGLMLTNPNTLGLFEKEIEEIATVVHADGGLLYYDGANLNGIVGVARPGDMGFDVLHFNLHKTFGTPHGGGGPGSGPVGVKDFLSGFLPHPLVEKKEEGYYLDYDRPLSIGKVRSFYGNFGVIVKAYAYMMALGGPGLREACELAVLNSNYLRHHLQEDYHIPFNRLCKHEFVASGQKQLAENGVSTLDIAKRLMDYGFHPPTVYFPLIVKEALMIEPVETESRERLDEFIAAMREIAREARENPDILHQAPHSTVIKRVDEVRAARQPILRWPGLGAE | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 53556
Sequence Length: 486
EC: 1.4.4.2
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Q4FMV1 | MLKNAQKDFIQRHIGPSVDEQNVMLKELGYQNLDDLIKDTVPEKILLKDDLDIGDPNSEYKALRKLKDISKKNKIYSSFIGMGYYGTYTPYVILRNILENPGWYTSYTPYQPEVAQGRLEMLLNFQQMIIDFTGMDIANASLLDEGTAAAEAMGLSYRISKSESKKVFVSKNCHPQTIDVIKTRAEPLGLEIIVGDEDKDIKEDIICGIIQYPGTLGDIKDPSEAISKIHKFNGKAVLACDLLALAKLKTPAELGADIAVGSSQRFGIPMGYGGPHAAFFATKDEYKRSMPGRIVGVSVDRHGKKAYRLALQTREQHIRRDKATSNICTAQALLAIVSAAYAVYHGPQGIKKIAESVSQLTKNFADKLKQSGYELYSNEFFDTVTIKTLDKTEKIYKNALDQGVNIRKVNSEMLAVSFDERKNLYRANQLLKIFNCSETIKETMNESLSNIPKNLLRTSTYLDHPVFNSYHSETEMLRYLKKLEDSDIALNKSMIALGSCTMKLNAVAEMIPVTWKEFSQPHPFSPVEQMDGYRELFTDLKNWLRSITGFSGVSLQPNAGAQGEFAGLMVIRKFHEKNGETNRNVCLIPSSAHGTNPASAQMVGMKVVVVKCDQYGNVDYEDLKNKAEEHSENLAALMVTYPSTHGVFEEKITDICELIHNHGGQVYMDGANLNALVGIAKPGNFGPDVCHINLHKTFCIPHGGGGPGMGPIACKKHLEIFLPKHSVIKDCGPVTGMGAVSAAPWGSSSILSISWMYIKMMGSEGLRKASQVAILNANYIAHKLKDSFPILYKGKSGNVAHECIIDIRTIKSETGITEEDIAKRLIDFGYHAPTMSWPVAGTMMIEPTESESLSEIDKFCSTLIKIKQEIDKIQSGEYDKTDNPLKNAPHTHVELTSNKWDHKYEREEAAYPSEFLRTNKYWPPVGRVDNVYGDKNLFCTCPSMEEYEDTAA | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 106007
Sequence Length: 952
EC: 1.4.4.2
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Q7V9K4 | MRNTKASKFSDRHLGLIEEAQVEILNALGHADINDFISSVVPEEILDAQPPDELLPKALNEIEALEELRSIAKKNQIKRSLIGLGYYGTYTPAVIQRHVFENPAWYTSYTPYQAEIAQGRLEALFNFQTLITELTGLPIANASLLDEGTAAAEAMSLSFAVNKQTKARKFIVDDQVLPQTLAVLKTRAEPLELDIEVVNLTDLVINETVFGLLIQLPGKSGQLWDPSSLIAQAHEFNALVTVAIDPLAQVLIAPMGQLGVDIAIGSSQRFGVPIGFGGPHAAFFAIKEEYKRLVPGRLVGQSIDSKGHSALRLALQTREQHIRRDKATSNICTAQALLATIASFYAVYHGPHGLEEIAKNIIYLRSQLELYLKEFGYTFAPDCRFDTLEIHCLEAPEIHRLSILSGFNLRILPLGASIEKSKGFAVSFDELSTTKELYKLCKIFADVKDKNFEPRENTNFNFKESLTSLPLRTTPWLKQQVFNNYRTETELMRYIQKLASRDFSLVNGMIPLGSCTMKLNATAELLPITWKEFSSIHPFVPSDQAKGYGYLSEQLEGWLCALTGFDGVSLQPNAGSQGEFAGLLVIRAWHKAINQADRNICLIPKSAHGTNPASAVMAGFKVVAVECDEYGNIDFEDLVLKVETYSSELGALMITYPSTHGVFEPNIRQICDQVHLHGGQVYLDGANLNAQVGLCRPGAFGADVCHLNLHKTFCIPHGGGGPGIGPIAVAKHLVAFLPSKNFHASDNNAAIGAISASPLGSASILPISWMYIRMMGADGLRQASSLAILSANYIANKLDPYFQVLFKAPNGKVAHECILDLRSIKRITGIEVDDVAKRLMDYGFHAPTISWPVAGTLMIEPTESESFEEINRFCEAMISIRSEIDAIESGITDLSNNPLRLAPHTMETVTAEIWDRPYTRQQAAFPLKDQFMNKFWPAVSRIDNAFGDRNLVCSCSTLEELSET | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 106218
Sequence Length: 964
EC: 1.4.4.2
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Q46IC1 | MSKAELKDFTFKSRHIGPTNEDEALMLQHLGYENAEEFISSVIPNEIFDSENNGVSIPDGCDQNKALTEINIISKKNVEHRSLIGLGYHSTVIPPVIQRNVLENPNWYTAYTPYQAEISQGRLEALFNFQTLISELTGLPISNASLLDEATAAAEAISLSLTVRKNKNANKFLVDQEILPQTLDVLKTRCEPLGISLEMFDNNNFEIDKNVFGILIQLPGKNGRIWDPTKIINDAHKCNAIVTIAIDPLAQVLIKPMGEFGADIVVGSAQRFGVPIAFGGPHAAFFATKEIYKRQIPGRIVGQSVDVEGNQALRLALQTREQHIRRDKATSNICTAQVLLAVLSSFYAVHHGPKGLKQIAENVVKYRSNFESILMNLEYPIEKYSAFDSVDVYCSEASEVIQLASEEGYNLRVLPIGSDFENAKGFGVTFDELTCDEEIYKLHQILAQVKGKKTHDLSNFIFENASLIDIPLREKSWLEQSVFNQYQSETDLMRYIHCLVSKDFSLVQGMIPLGSCTMKLNAAAELLPIEWREFSSIHPFAPHTQLTGFHEIINDLENWLSALTGFQGVSLQPNAGSQGEFAGLLVIRSWHQSLGEGHRNICLIPTSAHGTNPASAVMSGFKVVSVKCDEYGNVDLEDLKNKSKIHSKNLAALMVTYPSTHGVFEPNIREMCQVIHQEGGQVYLDGANLNAQVGICRPGSYGIDVCHLNLHKTFSIPHGGGGPGVGPIAVADHLVPYLPGHSIIKCGGQKAISAVSAAPFGSAGILPISWMYIRMMGSDGLRKASSIAILSANYLAKRLDPYYPVLFKDPNGLVAHECILDLRPLKSQLGIEVEDVAKRLMDYGFHAPTISWPVAGTLMVEPTESESLPELDRFCDAMIGIREEIEQIKLGKIDPINNPLKQSPHTLKTVTSDDWDRPYSRKEAAYPLPDQEKYKFWPSVSRINNAYGDRNLICSCPSVQDLEDINSV | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Mass (Da): 107029
Sequence Length: 968
EC: 1.4.4.2
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Q7NFJ5 | MSDLKRTPLCAQHLQLGARLVPFGGWEMPLQYSTLTREHRAVRTAVGLFDISHMGKYTLSGPDVLAQIQRLVPSDLARLQPGQAQYTVLLNEQAGIIDDLIFYCRSPEHWVVIVNGATNDKDRRWLAEHLQGVHFDDLTGTHTLLALQGPAAVETLQPLVDIDLARLGRFEHAQVSLAGKPAFLARTGYTGEDGFEIMSLEPEGIALWQSLTAAGVPPCGLGARDTLRLEAAMHLYGQDMDESTTPLEASLGWVIDWDKPDYFGREILLAQKAQGTERRLVGLTVEGRQIARHGYGLFDGEQQVGVVTSGTLTPTVDRPIALAYVGKPFAPIGSRLEVDIRGRRAMATVVKRPFYRRAL | Function: The glycine cleavage system catalyzes the degradation of glycine.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Mass (Da): 39569
Sequence Length: 359
EC: 2.1.2.10
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Q9K934 | MTELKKTPLFDLYEQYGGKVIDFGGWALPVQFSSIKEEHEAVRTKAGLFDVSHMGEVEVTGAQALNYLQRLVTNDVSKIKDGQAQYTAMCYENGGTVDDLLIYRRSEDQYLLVINAANIDKDIAWMEKHAIDGVSITNVSNQTAQLALQGPVAENVLQTLTEEPLADIKFFRFVDGVNIAGVNVLLSRTGYTGEDGFELYCLAEDAPVLWKKLIEAGKEHGVVPCGLGARDTLRFEAKLPLYGQELTKDISPIEAGIGFAVKVDKEDFIGKEILKKQKEQGAPRKLVGLEMVDKGIPRTGYEVYVDNQKIGFVTTGTQSPTLKKNVGLALLQAEHSELGTEVIVHVRKRQLIAKVVATPFYKRGN | Function: The glycine cleavage system catalyzes the degradation of glycine.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Mass (Da): 40309
Sequence Length: 365
EC: 2.1.2.10
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A1WWA3 | MPQRTPLYDQHVGAGARVVDFAGWEMPLHYGSQLAEHQAVRSDVGLFDVSHMAVTDLSGPGARALLREQLANDVAKLDGRPGQALYSCLLNGRGGVVDDLIVYLREDASYRVVSNAATREKVRPRLLEQAHAAGVTAEARDDLAMIAVQGPRAASVLEQLFGDQAAAALACKPFQAAAIGEIFAGRTGYTGEDGFELILPADQAPALWDRLTEAGAQPCGLGARDSLRLEAGLNLNGHEMDEETTPLEAALGWTVAWDPEDRDFIGRAALEEQRRHGAAWRLIGLLVEGRAPAREGYVVRTDAGDGVITSGAHSPTLGGPIALARVPAGAEGDWRVVIRKREAAARRVKPPFVRHGKVCV | Function: The glycine cleavage system catalyzes the degradation of glycine.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Mass (Da): 38494
Sequence Length: 360
EC: 2.1.2.10
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Q5V230 | MTLRAPPLSAIHERADASFTDFGGWEMPVEFESIRIEHEAVRSEAGKFDVSHMGQITVAGPDAATLTQRLTTNDVTVLDPGEAQYGAITDEDGIMLDDTVVYRLPEGAADEFLFIPNAGHDGEMTERWLSERDERGLDATVTNRTEEYAMIAVQGPDAPDLLSAETDVSLTALSRFEVAAGAVAGVDSLIARTGYTGEPGFEILCPPDDAGVVWDALECQPCGLGARDTLRLEMGFLLSGQEFHPVDEPRTPYEAGIGWTVKLDTEFVARDALEGVAADGPEEKLIGIELVDRGVPRHGYDVTTPDGEPIGHITSGTMSPTLGAPIALAYVPSAYAEPDKSVRVVVRGEPKKARTRSTPFLDR | Function: The glycine cleavage system catalyzes the degradation of glycine.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Mass (Da): 39071
Sequence Length: 363
EC: 2.1.2.10
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B8D1D7 | MKKTPLFEIHKELGARLIEFHGWSMPVQYTSIIEEHKAVRNQCGLFDVSHMGEILVEGPGALESLQKIVTNNVARLKKGQVLYTPMCKDDGGIIDDLLVYCLGQDKYLMVVNASNIEKDFNWVRDNSNQRTEVVNESDNYALLALQGPNSKKILEKVSSVNLDSLKFYNFTTGTLKGAEVLISRTGYTGELGYELYLSPDKAVEVWQALMEAGSDLGLIPAGLGARDTLRLEKGYCLYGNDIDENTHPLEAGLGWTVKFDKASFIGKRALLKYKEEGLSRKLVGFKLKGRGIPRHGYPIKDNGDQIGVVTSGSMSPTLSEGIGMGYVRYDKATPGESITIVVRNRAITGEVVKLPFI | Function: The glycine cleavage system catalyzes the degradation of glycine.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Mass (Da): 39457
Sequence Length: 357
EC: 2.1.2.10
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P48728 | MQRAVSVVARLGFRLQAFPPALCRPLSCAQEVLRRTPLYDFHLAHGGKMVAFAGWSLPVQYRDSHTDSHLHTRQHCSLFDVSHMLQTKILGSDRVKLMESLVVGDIAELRPNQGTLSLFTNEAGGILDDLIVTNTSEGHLYVVSNAGCWEKDLALMQDKVRELQNQGRDVGLEVLDNALLALQGPTAAQVLQAGVADDLRKLPFMTSAVMEVFGVSGCRVTRCGYTGEDGVEISVPVAGAVHLATAILKNPEVKLAGLAARDSLRLEAGLCLYGNDIDEHTTPVEGSLSWTLGKRRRAAMDFPGAKVIVPQLKGRVQRRRVGLMCEGAPMRAHSPILNMEGTKIGTVTSGCPSPSLKKNVAMGYVPCEYSRPGTMLLVEVRRKQQMAVVSKMPFVPTNYYTLK | Function: The glycine cleavage system catalyzes the degradation of glycine.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Mass (Da): 43946
Sequence Length: 403
Subcellular Location: Mitochondrion
EC: 2.1.2.10
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Q5QVA8 | MGSRTPLYEAHVKAGAKMVDFHGWDMPLNYGSQIEEHHAVRRDCGVFDVSHMTIVDVEGSQAQAFLRYLLANDVAKLKTEGKAQYTSMLNENGGVIDDLIVYFFSENAYRMVVNSATRDRDLAWIEKVAADFDVTTKERDDMGMLALQGPKAADKIQGVLTAEQYAEIDGMKPFVGKDVGDYFIATTGYTGEKGYEIVVPAEQLEALWNDLLKADVAPCGLGARDTLRLEAGMNLYGQDMDENITPLEANMGWSVAFEPADRDFIGRKALEQKKAEGHDKLVGLVMEEKGVLRHGQKVTVEGGEGIITSGTFSPTLGFSVAMARVPSSVGDTAEVEMRKKQMPVKVVKPGFVRNGQSVL | Function: The glycine cleavage system catalyzes the degradation of glycine.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Mass (Da): 39369
Sequence Length: 359
EC: 2.1.2.10
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O86567 | MSSTELRRTALDATHRALGATMTDFAGWDMPLRYGSEREEHVAVRTRAGLFDLSHMGEITVTGPQAAELLNFALVGNIGTVKPGRARYTMICREDGGILDDLIVYRLEEAEYMVVANASNAQVVLDALTERAAGFDAEVRDDRDAYALLAVQGPESPGILASLTDADLDGLKYYAGLPGTVAGVPALIARTGYTGEDGFELFVKPEHAVGLWQALTGAGEAAGLIPCGLSCRDTLRLEAGMPLYGNELSTALTPFDAGLGRVVKFEKEGDFVGRAALTEAAERAASRPPRVLVGLVAEGRRVPRSGYRVVAGGEVIGEVTSGAPSPTLGRPIAMAYVDPAHAAPGTEGVGVDIRGSHEPYEVVALPFYKRQK | Function: The glycine cleavage system catalyzes the degradation of glycine.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Mass (Da): 39401
Sequence Length: 372
EC: 2.1.2.10
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B2FR21 | MTQKTLLNDTHRALGAKMVDFGGWDMPIHYGSQLDEHHLVRRESGVFDVSHMTVVDLRGDQVRPFLRRLLANSVDKLKVPGKALYSCMLNPRGGVIDDLIVYYLGDDFFRMVVNASTREKDLAWLREQAAPFGVSVEQRPDLAILAVQGPQARAIVIGLARESEREALTKLGRFAALQVQSDDGVELFVARTGYTGEDGFEILLPQDAVVAFWNRLLAAGVKPAGLGARDTLRLEAGMNLYGQDMDEEISPYEAALAWTVSLDEGRDFIGRDALEAQKAAGTARQMIGLVMDEKGVLRHGQAVTTAGGQGEILSGTFSPTLAKGIAFARVPAGELGEVTVDIRGRQVPVRVVKFPFVREGQAQPGVLADA | Function: The glycine cleavage system catalyzes the degradation of glycine.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Mass (Da): 40269
Sequence Length: 370
EC: 2.1.2.10
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Q67N36 | MNESLKRTPLYELHLKLGARMVPFGGWEMPVQYSSVIEEHRAVREAAGLFDVSHMGEFEVRGPQALDLIQLVSTNDAAKLAVGRVQYALMCYENGTVVDDILIYRLDEHRYWLVVNAGNTQKDWEWINTARERAGLHNLELIDRSAEIALLALQGPKAEEILQPLATGVVLSQLEPFSLAKNVTVSGVPTLVLSRTGYTGEDGFEIYVKAEDVAALWEALLEAGDEQGLLPCGLGARDTLRFEAKLPLYGHEISDQHNPLEAGLGFAVKLKKGVDFIGRDALARIKEQGPTRKLVGIEMIDRGVPRQGYPVAVGGEVVGEVTTGSFSPTLEKNIALAYVPVAHSAVGTEVEVIIRGRALKARVVETPFYRSPHRR | Function: The glycine cleavage system catalyzes the degradation of glycine.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Mass (Da): 41243
Sequence Length: 375
EC: 2.1.2.10
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A6LP67 | MKYTPLYEEHVKLGAKMVDFAGFNMPIQYTSIKDEVLAVRKNVGMFDVSHMGEVIVEGKDSTKFVDFLITNDFKNLKPGEIVYTAMCNENGGFVDDLLAYKISEEKAMLVINASNIEKDFSWMKKISESFDVTLENKSDEYVLIAVQGPNAQKTLQKITNVDLEQIGYYTFTEGNVLDIKAIISRTGYTGEDGFEIYTTDKDGIIKIWKKLLNLNVIPAGLGARDCLRLEASLLLYGNDMDETITPLEVGIKWAVKFEKDFMGKEALKRQLEEGTSRRLKGFKIIDKGIARHGYKVFKDGKEIGYVTSGTFSPTLNQAIGMALIEKGYKSGEIIEIEIRNKLVKAEIVKMPFYRGSVKSKKKG | Function: The glycine cleavage system catalyzes the degradation of glycine.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Mass (Da): 40855
Sequence Length: 363
EC: 2.1.2.10
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Q9WY54 | MKRTPLFEKHVELGAKMVDFAGWEMPLYYTSIFEEVMAVRKSVGMFDVSHMGEFLVKGPEAVSFIDFLITNDFSSLPDGKAIYSVMCNENGGIIDDLVVYKVSPDEALMVVNAANIEKDFNWIKSHSKNFDVEVSNISDTTALIAFQGPKAQETLQELVEDGLEEIAYYSFRKSIVAGVETLVSRTGYTGEDGFELMLEAKNAPKVWDALMNLLRKIDGRPAGLGARDVCRLEATYLLYGQDMDENTNPFEVGLSWVVKLNKDFVGKEALLKAKEKVERKLVALELSGKRIARKGYEVLKNGERVGEITSGNFSPTLGKSIALALVSKSVKIGDQLGVVFPGGKLVEALVVKKPFYRGSVRREV | Function: The glycine cleavage system catalyzes the degradation of glycine.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Mass (Da): 40333
Sequence Length: 364
EC: 2.1.2.10
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Q9BSE5 | MLRLLASGCARGPGPGVGARPAAGLFHPGRRQSRQASDAPRNQPPSPEFVARPVGVCSMMRLPVQTSPEGLDAAFIGVPLDTGTSNRPGARFGPRRIREESVMLGTVNPSTGALPFQSLMVADLGDVNVNLYNLQDSCRRIQEAYEKIVAAGCIPLTLGGDHTITYPILQAMAKKHGPVGLLHVDAHTDTTDKALGEKLYHGAPFRRCVDEGLLDCKRVVQIGIRGSSTTLDPYRYNRSQGFRVVLAEDCWMKSLVPLMGEVRQQMGGKPIYISFDIDALDPAYAPGTGTPEIAGLTPSQALEIIRGCQGLNVMGCDLVEVSPPYDLSGNTALLAANLLFEMLCALPKVTTV | Function: Hydrolyzes linear guanidino acids to form urea and the corresponding amines. Displays specificity for substrates having a negatively charged head group and short chains including taurocyamine, guanidino propanoic and butanoic acids. May protect cells by detoxifying potentially harmful amounts of guanidino acids. Metabolizes L-arginine with low efficiency.
Catalytic Activity: 3-guanidinopropanoate + H2O = beta-alanine + urea
Sequence Mass (Da): 37660
Sequence Length: 352
Pathway: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
Subcellular Location: Mitochondrion
EC: 3.5.3.-
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A2AS89 | MLRLLRSSWARGLGSGVATWRPSAGLFRPGCPGIRQASGASDTPHHQSPSSESPVQPVGVGVCSMMRLPLQSSPEGLDAAFIGVPLDTGTSNRPGARFGPCRIREESLMLGAVNPSTGALPFQSLRVADLGNVNVNLYNLQDSCLLIREAYQNVLAAGCIPLTLGGDQTITYPILQAVAKEHGPVGLVHVGAHTNTTDKPREEKVYHRTPFRRSVDEGLLDSKRVVQIGIRGSSRTLDPYRYSRSQGFRVVLAEDCWMKSLVPLMAEVRQQMGGKPLYISFAIDALDPAYAPGTGTPEIAGLTPSQALEIIRGCQGLNVVGCDLVEVSPPYDLSGNTALLAANLLFEMLCALPKVTTV | Function: Hydrolyzes linear guanidino acids to form urea and the corresponding amines. Displays specificity for substrates having a negatively charged head group and short chains including taurocyamine, guanidino propanoic and butanoic acids. May protect cells by detoxifying potentially harmful amounts of guanidino acids. Metabolizes L-arginine with low efficiency.
Catalytic Activity: 3-guanidinopropanoate + H2O = beta-alanine + urea
Sequence Mass (Da): 38255
Sequence Length: 358
Pathway: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
Subcellular Location: Mitochondrion
EC: 3.5.3.-
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Q8TB36 | MAERQEEQRGSPPLRAEGKADAEVKLILYHWTHSFSSQKVRLVIAEKALKCEEHDVSLPLSEHNEPWFMRLNSTGEVPVLIHGENIICEATQIIDYLEQTFLDERTPRLMPDKESMYYPRVQHYRELLDSLPMDAYTHGCILHPELTVDSMIPAYATTRIRSQIGNTESELKKLAEENPDLQEAYIAKQKRLKSKLLDHDNVKYLKKILDELEKVLDQVETELQRRNEETPEEGQQPWLCGESFTLADVSLAVTLHRLKFLGFARRNWGNGKRPNLETYYERVLKRKTFNKVLGHVNNILISAVLPTAFRVAKKRAPKVLGTTLVVGLLAGVGYFAFMLFRKRLGSMILAFRPRPNYF | Function: Regulates the mitochondrial network by promoting mitochondrial fission.
PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41346
Sequence Length: 358
Subcellular Location: Mitochondrion outer membrane
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O88741 | MARRQDEARAGVPLRVEGPPDKEVHLILYHWTHSFSSQKVRLVIAEKALKCEEHDVSLPLSEHNEPWFMRLNSAGEVPVLVHGENIICEATQIIDYLEQTFLDERTPRLMPDEGSMYYPRVQHYRELLDSLPMDAYTHGCILHPELTVDSMIPAYATTRIRSQIGNTESELKKLAEENPDLQEAYIAKQKRLKSKLLDHDNVKYLKKILDELEKVLDQVETELQRRNEETPEEGNQPWLCGESFTLADVSLAVTLHRLKFLGFARRNWGHGKRPNLETYYERVLKRKTFNKVLGHVNNILISAVLPTAFRVAKKRAPKVLGSTLVVGLLVGMGYFAFMLFRRRLGSMILALRPRPNYF | Function: Regulates the mitochondrial network by promoting mitochondrial fission.
PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41311
Sequence Length: 358
Subcellular Location: Mitochondrion outer membrane
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Q9LIN2 | METNLLLVKCVLLASCLIHPRACSPSCNFPAIFNFGDSNSDTGGLSASFGQAPYPNGQTFFHSPSGRFSDGRLIIDFIAEELGLPYLNAFLDSIGSNFSHGANFATAGSTVRPPNATIAQSGVSPISLDVQLVQFSDFITRSQLIRNRGGVFKKLLPKKEYFSQALYTFDIGQNDLTAGLKLNMTSDQIKAYIPDVHDQLSNVIRKVYSKGGRRFWIHNTAPLGCLPYVLDRFPVPASQIDNHGCAIPRNEIARYYNSELKRRVIELRKELSEAAFTYVDIYSIKLTLITQAKKLGFRYPLVACCGHGGKYNFNKLIKCGAKVMIKGKEIVLAKSCNDVSFRVSWDGIHFTETTNSWIFQQINDGAFSDPPLPVKSACTR | Function: Lipase that can hydrolyze p-nitrophenyl butyrate and p-nitrophenyl palmitate in vitro . Possesses low activity against p-nitrophenyl acetate . Substrate preference is p-nitrophenyl palmitate > p-nitrophenyl butyrate >> p-nitrophenyl acetate . Lacks cholinesterase activity .
Catalytic Activity: H2O + hexadecanoate ester = an aliphatic alcohol + H(+) + hexadecanoate
Sequence Mass (Da): 42062
Sequence Length: 380
Subcellular Location: Secreted
EC: 3.1.1.-
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Q55EC7 | MAEADPGLPTQAIWDIPFESLEFNEKIGKGSFGSVFRGCYLGLDVAIKKIEKADDPEYLKYIDREVSMLQSLRHPFIVNFSGICVHSSGLYIVTEFVSGGDVRQLLKKTPPIGWDKRVSIAVDLAKAMVFLHAKKIIHRDLKSKNILLDEFQRIRLCDFGFARMSEQTKKSRHMTMCGTEGWVAPEILLGMSYDTSCDVFSYGVVLAELITGRKPGVDLWVRSPETCFDINPEELKQKSIPGCPSELISVCVECCLYEPLTRPKFDEILSQLKVCQNNLKVATAAAAAAAAAAAAAAAVVSTPTIQTPIIQTPNISFSPNNSNNNNNNNNNISNISPDITTGIQQINLSSSGGSNNSSPSTPPQGSQLVSLAQSRRNTMSLHRKSMELNLVDGQLSTTPPPTSPIQSRPHKPSDSIWKIAAKPKHVGYQTLKRKQGPCYAALTSHITKMIERATSDYYYDTSYIQDFLLAYRCFAPPQQIFELLLSRYIANSPDNFTNDINGWKKVQRVIQLRVIIFFKRWIDYYPQDFLEEAMEDNLNEFDKISAQQNSSTALLLGTTISNNELLIDPKLMTELQKKRSELELLIQINSPSDFINNNNNNNNNPVNNINNINNNNSVNSSSSNNNNNNNNNNSNNNNNNNNNNNNNNNNNNGLNIINIAAANQSKMMLQNGNNRYSVLVTSNGIGNGEEPYPVSIIPPPTTSEYLDVKDIHSTELARQITIINSFYFNRIKAREFIEYIWEKCGEESTTTPYVGTSFVEVVPAENIHKFVRKCNNLARFVSTEILKQTKLQKRVATIERFIEAAEKCLANNDYAAVFSIVEPLVDQSIERLSDTWRNVSQRNLATFEHLKSIVSKENDHKKYRELLPDAKPPCIPNIHLLLDELSFIETSSPRLLPGGIVNFFHYRQLSRKILQSQQLQSHCFRPIPSIQKVLTKPPSELFDDELIKNNSLKCEPPVSL | Function: Promotes the exchange of Ras-bound GDP by GTP.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 107769
Sequence Length: 960
EC: 2.7.11.1
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Q94361 | MLPNNQWQIPINNGLTHQENMAAHAAVMKLRVHDLQSIISQLSLRKPRPQKSEHQKVVVESLRDPHHARQIYQMASNFPNGNYEMQKRPATTSQVRSHPYVLPSRSGASNHLVNHHYQQQQQQQPQPHNLLHQQMMASHHSHLQQQHHPSTVRWLTPELLEEQLRGSMRYGAPAAAAATNAPLHSSFPNHGRSSQQSLQKSEKSNRPKKMYADNFEPLPLPFYDVISVLLKPVELHSSDSPTLKQTKQLQFPFLLTAEHISKISYRADVTPLPRYELQLRFFNLTEPVQGPQKDDFPLNCYARVDDSVVQLPNVIPTNKTNAEPKRPSRPVNITSNMNRYKKEHTVAVEWLADKRVWAAGVYFVHRVNSDILFKRLNQNVSRHRSLEVTKQEVIKKLSGGEDDIAMDRLNISLLDPLCKTRMTTPSRCQDCTHLQCFDLLSYLMMNEKKPTWQCPVCSSNCPYDRLIVDDYFLDMLAKVDKNTTEVELKEDGSYDVIKEEAFCISDDDDDDVVPATVNGTASCSSTNGNGLANEAAKKKPADDDIITLSDDDDEELNRGIMNSLNDSFSPGRHTASAELAAQKTPPQQKKKTKDDDIEIITLDDTPPRPVAASANLPMRQMSQQNQMPVGSSPSGMASTQMGMNEGASKTIRDALNKIGEQSANSSTQSSPLVQLHHTTHPLNFAQSSYMNPSSGSQTPTSQYGYSPMINQAPHFQMQNGLIGRNNQMVHMQQHHLQQQQQQQQSPQIMSPSFYAQQQMSNGGAFAYYPPQYPQQQYRQN | Function: Functions as an E3-type smo-1 ligase . Mediates smo-1 conjugation to air-2 in vitro and is required for proper chromosome alignment . In the early embryo, specifically suppresses checkpoint activation in response to DNA damage, maybe by promoting mus-101 sumoylation . In embryos, plays a role in determining telomere localization in the nucleus .
Sequence Mass (Da): 88139
Sequence Length: 780
Pathway: Protein modification; protein sumoylation.
EC: 2.3.2.-
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Q9ZPQ3 | MVTLIVATTADPASINPAAALLAMPGWTAGPILPPDIKSFSNKQTRVIQHDRSIVKEDDLDLRWEEATGEVVDEVIFLSRHTAVSNRPALTVHPIGVLHLKDGESPPQGGKPGWAALPSTRIGPWFRLLKKMAEAHGLVPEFEITLEATHHGPITNKPTMFLEIGSTEEYWKRQDAAQVMALLMWEGLGLGGSEEVGKWKSETGKRKVLLGIGGGHYAPRHMDIALKDDIWVGHLLSGYSLPMEDPTQTKTTPGENYIGGNWRQSIKAAFEATKASFPGGEILAHLDHKSFKGWQKKAITEFLAEESINVGKPNDFT | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Hydrolyzes D-aminoacyl-tRNA into D-amino acid and free tRNA. Broad specificity toward the amino acid, but strict specificity toward the D-isomer. Seems to be required for ethanol tolerance.
Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
Sequence Mass (Da): 34732
Sequence Length: 317
Subcellular Location: Nucleus
EC: 3.1.1.96
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B0XT72 | MKASAVTAALAVGASTVLAAPSIKARDDVTPITVKGNAFFKGDERFYIRGVDYQPGGSSDLADPIADADGCKRDIAKFKELGLNTIRVYSVDNSKNHDECMNALADAGIYLVLDVNTPKYSINRAKPKESYNDVYLQYIFATVDAFAGYKNTLAFFSGNEVINDGPSSSAAPYVKAVTRDLRQYIRSRKYREIPVGYSAADIDTNRLQMAQYMNCGSDDERSDFFAFNDYSWCDPSSFKTSGWDQKVKNFTGYGLPLFLSEYGCNTNKRQFQEVSSLYSTDMTGVYSGGLVYEYSQEASNYGLVEISGNNVKELPDFDALKTAFEKTSNPSGDGNYNKTGGANPCPAKDAPNWDVDNDALPAIPEPAKKYMTEGAGKGPGFAGPGSQDRGTQSTATAEPGSGSATGSSSSGTSTSSKGAAAGLTVPSLTMAPVVVGAVTLLSTVFGAGLVLL | Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall morphogenesis.
PTM: The GPI-like anchor contains a phosphoceramide lipid group. The anchor position has not been determined.
Location Topology: Lipid-anchor
Sequence Mass (Da): 48121
Sequence Length: 452
Subcellular Location: Cell membrane
EC: 2.4.1.-
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B0Y8H9 | MLPTYVRLFTAVCALATTASAVVPIEVKGKDFVNSKTGDRFQILGVDYQPGGSSGFTKDKDPLSDPDACLRDAALMQRLGVNTIRIYNLSPSLNHDECASIFNAAGIYMILDVNSPLYGGYLDRTDPESTYNDVYFKQVFGVIEAFKNFPNTLAFFAGNEVINEQSVKNVPTYVRAIQRDMKDYIAKNLDRSIPVGYSAADIRPILMDTLNYFMCADDANSQSDFFGLNSYSWCGNSSYTKSGYDVLTKDFADASIPVFFSEYGCNEVQPRYFSEVQALYGQEMTQSFSGGLVYEYTQEENDYGLVQINDNGTVTLLVDYDNLMAQYSKLDMSRIQASNTTQTSAKPPKCESSLITNSTFTDSFDLPKRPSKVQTMIDKGLSDANTGKLVEVKNTDIKQKIYNANGEEITGIKLSILASGESNTPGAHSSGSTSGSSSSGGSSSSSSDKESAAGTISVPFVGLLSAASFMAFFML | Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall morphogenesis (By similarity).
PTM: The GPI-like anchor contains a phosphoceramide lipid group.
Location Topology: Lipid-anchor
Sequence Mass (Da): 51718
Sequence Length: 475
Subcellular Location: Cell membrane
EC: 2.4.1.-
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B0XT09 | MRYSLVVGVVLLSGCAIATGSKFFYANNGSEFYIRGVAYQEDYSGGGAGGTGQSEANYVDPLADGSKCERDIPYLLQLRTNVIRTYAVNPSLNHDACMQKLSDAGIYVITDLASPDESITSNSPVWTVDQYARYTSVIDAFQKYDNVIGFFAGNEVVNQANQSAGAAFVKAAARDMKAYIKTKGYRQSLAIGYATTDNPEIRLPLSDYLNCGDQADAVDFFGYNIYEWCGDKTFQTSGYQNRTEEYKDYSIPIFFSEYGCNTEKPRKFTDVPVLFGPQMDNVWSGGIVYMYFETTNDYGLVSVSGSAVTPEPDFTYLSSEIQSATPTGVNSASYSPTNSPRACPTVDDTWLAKSSPLPPIPNAELCSCMVSSLSCVVKDSVDAEKYGELFGQVCGYGGGICDGIARNATAGSYGAYSVCTSKDQLSYVFDRYYKSQKKAASACDFAGAASVQSPKGESADCKSLVSQAGSAGTGTVTSQPTGGSGSTGGGGGGGGGGGGGGGAAASTSTSKGAAAGAASPAAVRVGGWPLVTYGLVAAMAGILMISL | Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall morphogenesis (By similarity).
PTM: The GPI-like anchor contains a phosphoceramide lipid group.
Location Topology: Lipid-anchor
Sequence Mass (Da): 57218
Sequence Length: 547
Subcellular Location: Cell membrane
EC: 2.4.1.-
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O85467 | MIWNWLRKKKKSNTSKLNETDNQEQHSNNQEDDNKEQTRSMKHNKGKNNEQKDSSQDKQQSAKQGDSSQDKQQNPKQEDSSQDKQQNPKQGDSSQDKQQSAKQKDPSQDKQQNPKQEDSSQDKQQSAKQGDSSQDKQQSAKQGDSSQDKQQNAKQDEPSQSKQQSSGGNSIYDFTKPEKDRIHSLQNLIEKLKKSSDFVNYHTSDDETMPYWISYYRPSLDGEKLQKYLMPTLLERPNASLEELKEHIPMSGITITNDLQKIEDMVLKGHAIIQLNQQDQKCMLANIAIDNYRAPTPPLNESTVIGPQEGFVEDIDTNINLVRKRLPVLDLQTKEMIIGEFSKTKVVMMYLDNLAEKDNVDFLEESLRALEYDQINDSAYLQELMGEKSIFPLYINTERTDRVTKALIDGKIAIFVDGSPSVLLTPVSYFDFFISPEDYNVSWMYATFSRILRLIAVLFSICATPLYVAVLNYHYELIPSDLLETLILSRAQVPFPPLIEALFLELAIDLLREAGARLPMKVGQTLGIVGGIVIGQASVQAGLTSNILLIIVALSALASFITPIYKMGNAVRLLRFPFLAFAEIGGLFGISLGFIFLFTHLFRLTSLRKPYALFYPTRQQSVKDSWIRFPLTMIDTRDVQARPQHVKKAAKGISTKHRSDFDD | Function: Required for inosine germination.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75311
Sequence Length: 663
Subcellular Location: Cell membrane
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P49939 | MPLFSKRKNNTDSKDKQNTDERNQEQQQEKERPVLISPSLAKNIAETKKEVGSSSDVIIREIKIGEQDHVHLAVIYISGLVDNNTIHESLIDPLVQDESIQNTHAIQQILEKTLPLGGVKAEKSWDKLFSELMLGNALIFADGHDEALICSTQGGEQRSIQEPSTQVSFRGPRQGFTESLQTNISMIRRYIKNPNLWVEKMKKGSVTNTDIALMYIQGICDEKVLKEVKQRLEKIDIDSILESGYIEQLIEDETFTTFPTMYHTERPDVVAGNLLEGRFAIIVDGTPFVLIAPALFVQFFQSVEDYYSRFDIATSIRILRVLVFFISLVAPAVYVAATTFHQEMIPTQLLVVIAAQREIVPFPAVVEALTMEVAFEILREAGVRLPRVVGSAVSIVGALVIGQAAVQAGIVSPAMVIIVALTAIASFATPAFAMAISARLIRFIFIIASAVMGFYGLILGIIMMFVHLCSLRSFGVPYMSPLAPFSSQGVKDALFRVPWWADEKRPESVSKEDKVRQGKDQRPEPAASRGMVNKDLEEGDQNGT | Function: Involved in the germination response to the combination of glucose, fructose, L-asparagine, and KCl.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60386
Sequence Length: 544
Subcellular Location: Cell membrane
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P49940 | MEKARISIRQLFVMIIIFELGSSLLITPGSMAGRDAWIAVLLGCAIGLFLFYLYQGIYQCYPNSSPKEYMDDMLGTKLSWLFSFLYILYFAYIAARVLRDFGEMLLTFAYHDTPIIIVNALLMVVSIYAVRKGIEVLARAAELLFGAMYLLGAIGLVLIIVSGTIDPHNLKPVLANGISPVLHSVFTQTMYVPFGEVVLFVMIFPNLNDRKDVKKMGMIAMAISGLIVALTVAINISVLDVDLTLRSQFPLLSTIQTIKVEEFLDRLDVFFMLALIIGGFFKVSLYLYATVVGTSTLFKEKNPSQLAYPMGLGILILSITIATNFSEHLNEGLNVVPLYIHLPFQLLFPLFLFIVAVWKKKRREKSKGEEAKK | Function: Involved in the germination response to the combination of glucose, fructose, L-asparagine, and KCl.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41770
Sequence Length: 373
Subcellular Location: Cell membrane
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P49941 | MVRKCLLAVLMLLSVIVLPGCWDKRELTDLAIISAIGIDRTNDSNYVLHLQIINPGNVAGGLQGGGAGDRPPVSVYSIEGNNITEALRKASMKVSRRLYFAHTNLVVINEKLAKEEGLDFVLDNLDRDTEFRTTATFVVAHKTKAENIVKILTPIDKIPSNKVNKTLDFTEAQYGRVVKINIQDVLKTLAANTMAPVIPGYMMIGDDKKGVSMENTQATDPKAILQADGLAVFDKAGYLKYWLEDDESVGAVWLMNKIQHTFINADWGKTKDAVSLQVTHQDTKLVPKMRNGRPYIHVKVSVEGIIDAVKYPFQLSDPKVLAAIEKALNKELEKEISHTVKKIKKNKIDFIGFGDTIYRKYPEQWEKMKDTWDKEYLPELPIDVKAETYIRRTGLRNNPIKHQFKDD | Function: Involved in the germination response to the combination of glucose, fructose, L-asparagine, and KCl.
Location Topology: Lipid-anchor
Sequence Mass (Da): 45836
Sequence Length: 407
Subcellular Location: Cell membrane
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Q331Q7 | MTADRWAGRTVLVTGALGFIGSHFVRQLDARGAEVLALYRTERPEIQAELAALNRVRLVRTELRDESDVRGAFKYLAPSIDTVVHCAAMDGNAQFKLERSAEILDSNQRTISNLLNCVRDFGVGEVVVMSSSELYSASPTVAAREEDDFRRSMRYTDNGYVLSKTYGEILARLHREQFGTNVFLVRPGNVYGPGDGFDCSRGRVIPSMLAKADAGEEIEIWGDGSQTRSFVHVADLVRASLRLLETGKYPEMNVAGAEQVSILELAGMVMAVLGRPERIRLDPSRPVGAPSRLLDLSRMSEVIDFDPQPLRAGLEETARWYRLHKR | Function: Catalyzes the stereospecific reduction of the C-4 keto group of dTDP-4-dehydro-6-deoxy-D-allose, leading to dTDP-6-deoxy-D-allose, an intermediate in the biosynthesis of the mycinose moiety of dihydrochalcomycin (GERI-155) antibiotic. Cannot directly reduce dTDP-4-dehydro-6-deoxyglucose, and thus acts after the epimerization step catalyzed by GerF.
Catalytic Activity: dTDP-6-deoxy-alpha-D-allose + NAD(+) = dTDP-4-dehydro-6-deoxy-alpha-D-allose + H(+) + NADH
Sequence Mass (Da): 36261
Sequence Length: 326
EC: 1.1.1.364
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Q93N70 | MGKLLELEGNLFEVMKEIRDELGSPNDLTIREVALAGSFTRCAVVFLCGLTDKDNVYKYVVRTLQYEEVQNEAAVVQTLLDRFISIAEVGKKTTFPDIINAILAGDTVILIDNIQTAIIINSRAWEKRSLEPPVTEDLIRGPRVGLNEDINVNKMLIRRSLRDPKLRFQSYIMGKRSQKEVTLVYIEDIINPHIVKELDRRLQSIVTDVVLETGTIEQLIQDNNLSPFPQFLNTERPDNIIASLAKGKAAILVDGSPFALIAPLVFVDIFQSVEDHYERWVIGTLLRFLRMGSGIIAVLLPAMYVALVSYHQGLIPSKLAYSIAGAREGVPFPAYIETLMMALTMELIREAGIRLPKPMGQTIGIVGGLVIGEAAVNAGIVNPFLVIIIAVTAIATFSLPVYSITITFRILLFVFVLAATAFGLYGIILALIALAIHITNLTSVGIPYTTPIAPAFYKDWKEEFIRMPKSMLKDRPEYLQTKDSTIRPKERK | Function: Contributes to the L-alanine germination response.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54800
Sequence Length: 492
Subcellular Location: Membrane
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Q93N69 | MKPFEYGDEEIGSREIGFAVSSTIIGIGALSMPRDIANQTLFSDGWIILLLGGLICAVLGWFVTRVAILFPKQNFVQYTSAHLTKPVAYTISSILVLTFAALTAYESRMISVISQTYLFSDTPIQLLSFFFLLVVIYGIAGSRAALLRLNVLFLPIVLIAIVLLSLLNINLMEINNLLPAFQTKVSQYAVGVKNSIFTFIGFEVALFYAVLLNNKTAKKAPMAVAKAVMVNVLSYILIYVTCISVFTYMTTRGLTYPTIELGKEIEIGGGFLERFDAIFFTTWIITIYNTTAMYYDVASLLFCAMFPKVKKQIFIFISAPIIFMVNMIPSSLNTLSSYGTYLAWIDMGCVVLAPLLVLIVYKIKRRNGGNETPS | Function: Contributes to the L-alanine germination response.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41486
Sequence Length: 374
Subcellular Location: Membrane
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Q93N68 | MEMKHLLKIIMVMALTGFMSGCSELEEIEERGFVVGAAYDIVKEKKANPIMKGTYQMVLPSKLSQQGGQGGGDSENYINVSAKADSVFEQIRIIAKKISRTLFFPHIQVIIFSEELLSHPYILQNTLDVYIRDHEMRRNIRLFVSNKNAEAILKQSAKPENLPAQYIDMLAEHPPKNAQMIEAARIGEVQEKMISNRSFVLPILELTKQGVQMNGAALFRGKDNKCVGNLSGEETVGMNYIIGKKIGGFFTIRKKNQLITYEIHKLRRKIKVSTTNATKPKFDIHLSLEGTLAELHFSDHKKVLNEKRLEKDISEEMEKRIQKSIKLVQKKYKVDVLELGEVYKRHNYKEWKKVSKNWDQGENYFSNAEITVHVHPTIEHSGSALPKRVK | Function: Contributes to the L-alanine germination response.
Location Topology: Lipid-anchor
Sequence Mass (Da): 44597
Sequence Length: 390
Subcellular Location: Membrane
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Q9KI10 | MEFEFFFQIALILLSTKLAGDLSVRLGQPSVLGKLIVGIVIGPAVLGWIENSELLTQLSNVGVILLMFMAGLETDLEELNANRNSSLAVALGGIILPFVGGYVSGLVMGMEQGNAVFLGLLLCATSVSISVQTLRDLGKMKTRESTTMLGAAVFDDILVVILLAFAMSFLGTDDVNLTMVILKKVVFFASIILIGWKGVPAIMRWLSPLRVSESIVSAALIICFSFAYFGELLGIAGIIGAFAAGIAISQTNYKHEVEKKVEPIAYAMFVPVFFVSIGMNITFDGIGNQIWFILALTVIAVLTKLIGCGFGARMTGFDAKSSAIIGAGMVSRGEVALIIAGTGLSSGLLAQDYFTAIVIVVILTTMITPPMLKYTFGAKDKAMKASK | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. Can also use potassium as a coupling ion, without completely replacing H(+). This Na(+)/H(+)-K(+) antiport is much more rapid than Na(+)/H(+) antiport. Can also extrude lithium. Important for the inosine-dependent germination of spores.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41093
Sequence Length: 387
Subcellular Location: Membrane
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Q6FKZ9 | MDLTVEPNLKSLITSSTHKWIFVGGKGGVGKTTSSCSIAIQMALAQPHKKFLLISTDPAHNLSDAFGEKFDKDARKVTGMDNLSCMEIDPSAALKDMNDMAVSSAGENGNDDLGGLLQGGALADLTGSIPGIDEALSFMEVMKHIKKQEQGDGESFDTVIFDTAPTGHTLRFLQLPTTLSKLLDKFSEITGRLGPMLNSMMGSGNVDIAGKLNELKANVETIKEQFTDPDLTTFVCVCISEFLSLYETERLIQELISYDMDVNSIIVNQLLFAEFDQEHNCKRCQSRWKMQKKYLDQIDELYEDFHVVKMPLCAGEIRGLNNLKKFSQFLFKEYDPVADNTVIYELEEKN | Function: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1 and GET2, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the GET1-GET2 receptor, and returning it to the cytosol to initiate a new round of targeting. Cooperates with the HDEL receptor ERD2 to mediate the ATP-dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER. Involved in low-level resistance to the oxyanions arsenite and arsenate, and in heat tolerance.
Sequence Mass (Da): 38895
Sequence Length: 350
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q2GXW1 | MSATLINVDDGDAMEPTLQSILDQRSLRWIFVGGKGGVGKTTTSCSLAIQLAKVRRSVLLISTDPAHNLSDAFSQKFGKEARLIDGFENLSAMEIDPNGSIQDLLAGQGEGDAGADMGGMGGMMQDLAFAIPGIDEAMSFAEVLKQVKSLSYETIIFDTAPTGHTLRFLQFPSVLEKALAKVSQLSNQYGPLLNGFLGSNGTLPNGQNLNEMMEKLETLRATISEVNTQFKDERLTTFVCVCIPEFLSLYETERMIQELASYGIDTHSIVVNQLLFPKPGSDCEQCTARRRMQKKYLEQIEELYDEFNVVKMPLLVEEVRGKERLERFSEMLVTPFVPPS | Function: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.
Sequence Mass (Da): 37554
Sequence Length: 340
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q3B7J2 | MKMLPGVGVFGTGSSARVLVPLLRAEGFTVEALWGKTEEEAKQLAEEMNIAFYTSRTDDILLHQDVDLVCISIPPPLTRQISVKALGIGKNVVCEKAATSVDAFRMVTASRYYPQLMSLVGNVLRFLPAFVRMKQLISEHYVGAVMICDARIYSGSLLSPSYGWICDELMGGGGLHTMGTYIVDLLTHLTGRRAEKVHGLLKTFVRQNAAIRGIRHVTSDDFCFFQMLMGGGVCSTVTLNFNMPGAFVHEVMVVGSAGRLVARGADLYGQKNSATQEELLLRDSLAVGAGLPEQGPQDVPLLYLKGMVYMVQALRQSFQGQGDRRTWDRTPVSMAASFEDGLYMQSVVDAIKRSSRSGEWEAVEVLTEEPDTNQNLCEALQRNNL | Function: Promotes matrix assembly.
Sequence Mass (Da): 42255
Sequence Length: 385
Subcellular Location: Secreted
EC: 1.-.-.-
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Q5BKK6 | MKTLPGIGVFGTGNTARVLISLLRADGFSIEALWGKTDEEAKELAEEMGIPFYTCHTDDVLLHQEVDLVCISIPPPLTRQIAVKALGIGKNVICEKAASSIDAFTMVKAARYYPKLMSLVGNALRFLPAFDRMRQLILEQNYVGEIRICDVRVYGGSLLSSNYSWICDDLMGGGGLHTLGTYLVDLLTHLTNKRAEKVHGFLKTFVKQNEAISGIRYVTSDDFCFFQMQMTGGACSTVTLNFNMPGTFVHEVMVVGSAGRLVVRGTELFGQKNSASEEKLLLSDPLTREIADISDFEKVPPPYLMGIAHMVKALRQSFQDQEDRRTWDQKPLSVAATFEDGLYMQRVVDAIKRSNRSGEWESVELTNDETDSNQNLSEVIQHNL | Function: Promotes matrix assembly.
Sequence Mass (Da): 42705
Sequence Length: 384
Subcellular Location: Secreted
EC: 1.-.-.-
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Q07982 | MTNKISSSDNLSNAVSATDDNASRTPNLTRRALVGGGVGLAAAGALASGLQAATLPAGASQVPTTPAGRPMPYAIRPMPEDRRFGYAIVGLGKYALNQILPGFAGCQHSRIEALVSGNAEKAKIVAAEYGVDPRKIYDYSNFDKIAKDPKIDAVYIILPNSLHAEFAIRAFKAGKHVMCEKPMATSVADCQRMIDAAKAANKKLMIGYRCHYDPMNRAAVKLIRENQLGKLGMVTTDNSDVMDQNDPAQQWRLRRELAGGGSLMDIGIYGLNGTRYLLGEEPIEVRAYTYSDPNDERFVEVEDRIIWQMRFRSGALSHGASSYSTTTTSRFSVQGDKAVLLMDPATGYYQNLISVQTPGHANQSMMPQFIMPANNQFSAQLDHLAEAVINNKPVRSPGEEGMQDVRLIQAIYEAARTGRPVNTDWGYVRQGGY | Cofactor: Binds 1 NADP(+) per subunit. The NADP(+) cannot dissociate.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Catalytic Activity: D-fructose + D-glucose = D-glucono-1,5-lactone + D-sorbitol
Sequence Mass (Da): 47190
Sequence Length: 433
Pathway: Carbohydrate metabolism; D-sorbitol biosynthesis; D-sorbitol from D-fructose and D-glucose: step 1/1.
Subcellular Location: Periplasm
EC: 1.1.99.28
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O53507 | MAGAITDQLRRYLHGRRRAAAHMGSDYDGLIADLEDFVLGGGKRLRPLFAYWGWHAVASREPDPDVLLLFSALELLHAWALVHDDLIDRSATRRGRPTAQLRYAALHRDRDWRGSPDQFGMSAAILLGDLAQVWADDIVSKVCQSALAPDAQRRVHRVWADIRNEVLGGQYLDIVAEASAAESIESAMNVATLKTACYTVSRPLQLGTAAAADRSDVAAIFEHFGADLGVAFQLRDDVLGVFGDPAVTGKPSGDDLKSGKRTVLVAEAVELADRSDPLAAKLLRTSIGTRLTDAQVRELRTVIEAVGARAAAESRIAALTQRALATLASAPINATAKAGLSELAMMAANRSA | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the sequential condensations of isopentenyl pyrophosphate (IPP) with dimethylallyl diphosphate (DMAPP) to yield geranyl diphosphate (GPP) and with GPP to yield (2E,6E)-farnesyl diphosphate (E,E-FPP).
Catalytic Activity: dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate
Sequence Mass (Da): 37781
Sequence Length: 352
Domain: Contains two aspartate-rich DDxxD motifs, designated as FARM (the first aspartate-rich motif) and SARM (the second aspartate-rich motif).
Pathway: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.
EC: 2.5.1.10
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Q9UWR6 | MLIDHYIMDFMSITPDRLSGASLHLIKAGGKRLRPLITLLTARMLGGLEAEARAIPLAASIETAHTFSLIHDDIMDRDEVRRGVPTTHVVYGDDWAILAGDTLHAAAFKMIADSREWGMSHEQAYRAFKVLSEAAIQISRGQAYDMLFEETWDVDVADYLNMVRLKTGALIEAAARIGAVAAGAGSEIEKMMGEVGMNAGIAFQIRDDILGVIGDPKVTGKPVYNDLRRGKKTLLVIYAVKKAGRREIVDLIGPKASEDDLKRAASIIVDSGALDYAESRARFYVERARDILSRVPAVDAESKELLNLLLDYIVERVK | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Probably involved in biosynthesis of the precursor for C25 (sesterterpanyl chain) moiety of C25-C25 diether (2,3-di-O-sesterterpanyl-sn-glycero) membrane lipid. Catalyzes the condensation of isopentenyl pyrophosphate with the allylic pyrophosphates to yield all-trans geranylfarnesyl diphosphate (GFPP). Geranylgeranyl diphosphate (GGPP) is the preferred substrate, however methylallyl diphosphate (DMAPP), farnesyl diphosphate (FPP) and geranyl diphosphate (GPP) can also be used as allylic substrate.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate
Sequence Mass (Da): 34982
Sequence Length: 318
EC: 2.5.1.81
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Q8PYS1 | MPVKVHGVILMNIEEWEEYRYVEAGIKESITLIEDPGLKKMVEHVCHSGGKRIRPIILLLVSEICSGSYSRSLNAALAVEMMHSASLIHDDLLDQGLVRRNLPSAPEKFGPSGALLCGDYLIAKSIAFISPYGEKVIQDFGKAGMDMAEGEVLDLKLEDESFGENDYFKCIYKKTASLFAISASIGAYTGGAEEELAERFSHFGNALGTAYQIVDDILEFLEVVEGKESKFTSETLPHIYMKSTSKEEALKKSIDCVKLHVAAAKETLETFRECPARDKLFQITDYITVDMLENL | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Involved in biosynthesis of the polyprenyl side-chain of methanophenazine, an electron carrier utilized for methanogenesis. Catalyzes the condensation of isopentenyl pyrophosphate with the allylic pyrophosphates to yield geranylfarnesyl diphosphate (GFPP). It prefers geranylgeranyl diphosphate (GGPP) and farnesyl diphosphate (FPP) as allylic substrate.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate
Sequence Mass (Da): 32747
Sequence Length: 295
EC: 2.5.1.81
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Q3IPL1 | MTSADHVESAIAERREIVNEAVSEQLPVQKPERLYSASRYLLDAGGKRLRPTILLLAAESLADVEPLSADYRQFPSLPGDEVDVLSAAVSIEVIQSFTLIHDDIMDDDDLRRGVPAVHREYDLETAILAGDTLYSKAFEYMLDTGAPAERSVEALDELATTCTEICEGQALDVDFENRSDVTTEEYLEMVEFKTAVLYAAAASIPAILLGSDDETVEALHGYGLDIGRAFQIQDDLLDLTAPSDELGKQRGSDLVENKRTVITLHARDQGIDVEGLVSDDPSDAEIEAAVQTLEDAGSIDFAREMALDLVTSGKERLDVLPENEARQLLEDIADFLVERSY | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Probably involved in biosynthesis of the precursor for C25 (sesterterpanyl chain) moiety of C20-C25 diether (2-O-sesterterpanyl-3-O-phytanyl-sn-glycer) membrane lipid. Catalyzes the condensation of isopentenyl pyrophosphate with the allylic pyrophosphates to yield geranylfarnesyl diphosphate (GFPP). Geranylgeranyl diphosphate (GGPP) is the preferred substrate, but dimethylallyl diphosphate (DMAPP) and farnesyl diphosphate (FPP) can also be used as allylic substrate.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate
Sequence Mass (Da): 37411
Sequence Length: 341
Subcellular Location: Cytoplasm
EC: 2.5.1.81
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Q06210 | MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDGGNDKDWEANACKIQLIKKKGKVKALDEEVHKQQDMDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDNRESQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEHKLSTDHIPILYRTARTQIGSKFTRWGSQGERGKDKKGSCNLSRVDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGDHPGRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE | Function: Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Regulates the circadian expression of clock genes BMAL1 and CRY1 (By similarity). Has a role in fine tuning the metabolic fluctuations of cytosolic UDP-GlcNAc and its effects on hyaluronan synthesis that occur during tissue remodeling .
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 78806
Sequence Length: 699
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1.
EC: 2.6.1.16
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P82808 | MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGLDGGNDKDWEANACKIQLIKKKGKVKALDEEVHKQQDMDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDNWESQDVSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEHKLSTDHIPILYRTGKDKKGSCGLSRVDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTARDHPGRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGMATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE | Function: Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Regulates the circadian expression of clock genes BMAL1 and CRY1 . Has a role in fine tuning the metabolic fluctuations of cytosolic UDP-GlcNAc and its effects on hyaluronan synthesis that occur during tissue remodeling (By similarity).
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 76827
Sequence Length: 681
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1.
EC: 2.6.1.16
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O94808 | MCGIFAYMNYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNHEVKERHIQLVKKRGKVKALDEELYKQDSMDLKVEFETHFGIAHTRWATHGVPSAVNSHPQRSDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNRETEDITFSTLVERVIQQLEGAFALVFKSVHYPGEAVATRRGSPLLIGVRSKYKLSTEQIPILYRTCTLENVKNICKTRMKRLDSSACLHAVGDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSASDDPSRAIQTLQMELQQIMKGNFSAFMQKEIFEQPESVFNTMRGRVNFETNTVLLGGLKDHLKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFISLVMFGLMMSEDRISLQNRRQEIIRGLRSLPELIKEVLSLEEKIHDLALELYTQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSKDDTESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE | Function: Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Sequence Mass (Da): 76931
Sequence Length: 682
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1.
EC: 2.6.1.16
|
Q9HJH3 | MMTVLEDMLRKTRNGKVHMTLIDPGAKPPQECARIAEEAEMAGTDFIMVGGSTDIDSRAMDEAISAIKAKTDLKVIIFPGSSLMISPKADAIFFMSLLNSGSLEYVVGHQVKAAIPLSAMKIEKIPMAYLVFDPGMTVGRVGKAHLIPRDDEKTALSYALAAQYFGFRLVYFEAGSGSPYHVGENVVRRVKQELDIPVIVGGGIRTPEAAKALAQAGADMIVTGTIAERSVNVYEALHPIVESIKEVGISKIQ | Cofactor: Cannot use Mn(2+) or Zn(2+).
Function: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids. Cannot use sn-glycerol-3-phosphate (G3P) as substrate.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate + sn-glycerol 1-phosphate = diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate
Sequence Mass (Da): 27252
Sequence Length: 253
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.5.1.41
|
Q5JDY1 | MLKLGKVETYIHEKLEREKLHFVLLDPDDVSPELAGELASMSEEVGVDAIMVGGSTGAEGEVLDSVVRAIKESSNLPVILFPGSHGGISKYADAIFFMSLLNSRNPFFITGAQALGAFQVKRYGIEPIPMAYLIIEPGETVGWVGDAKPIPRHKPKIAAAYALAGQYLGMRLVYLEAGSGAPQPVPPEMIGLVKRVIDVPLIVGGGIRTEEQARAAVKAGADIIVTGTAIEKAGSVEKAREKLEELNRGVKG | Function: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate + sn-glycerol 1-phosphate = diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate
Sequence Mass (Da): 26828
Sequence Length: 252
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.5.1.41
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A1RXV6 | MRGRVKNYILEKIREHGAIHMTLIDPEKTTPEVAARIAREVAEAGTSAIMVGGSIGVSEAMTDEVVLAIKRSTEVPVILFPGSPTALSRHADAVWFLSVLNSQNPYFITGAQMQGAPIVKRYGLEVLPLGYIIVGEGGAVSIVSYTRPLPFAKPEVVAAYALAAEYMGFQFVYLEGGSGGEPVPPKIVKMVKGVTTLPLIVGGGIRSPEVAKELAKAGADIIVTGTIVEESENIRETIGRIVRATREGALERSRE | Function: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate + sn-glycerol 1-phosphate = diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate
Sequence Mass (Da): 27211
Sequence Length: 255
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.5.1.41
|
D5BCE4 | MPKILDAIIKASKINKKLLAVLIDPEKFATENYSYFIEKLPEAVTHIFVGGSTATTAQSEVCVDFIKTKTNLPVILFPGDKEQITEKADGILLLSLISGRNPEYLIEQHIKAVPKLLNAGLEIIPTGYLLLDGGNQSAVARVSKTKPIQQDEIELIRNTALAGAMLGKQLVYLEAGSGALIPVSEKVIAEVKRDLNIPLIVGGGIRNATQLKKAYKAGADLVVIGTAFENGEFK | Function: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P).
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate + sn-glycerol 1-phosphate = diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate
Sequence Mass (Da): 25221
Sequence Length: 234
EC: 2.5.1.41
|
Q9SYL6 | MIDNNCLYKEELNRNSYSGLAKEASESILLPSESGFDGSRSPVCSSPDPNLNYRPVIGILSHPGDGASGRLTNDTSSTYIAASYVKFAEAGGARVIPLIYNEPEEVLFQKLELVNGVIFTGGWAKKYDYFEIVKKIFTKALERNDAGEHFPVYGICLGFELMSIIISQNRDILERFDAEDNASSLQFVDNVNNDGTLFQRFPPELLKKLSTDCLVMQKHKYGITPANFQANPALSSFFEILTTCIDENSKTYVSTVKAKRYPITGFQWHPEKNAFEWGSSAIPHSEDAIQVTQHAASYLVSEARKSLNRPESQKVLSNLIYNYKPTYCGYAGRGYDEVYIFTQPRSRF | Function: Cleaves the polyglutamate sidechains of folate polyglutamates in the vacuole. Is important for polyglutamyl tail length determination before vacuolar exit. Plays a role in folate stability and intracellular folate content.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
Sequence Mass (Da): 39057
Sequence Length: 348
Subcellular Location: Vacuole
EC: 3.4.19.9
|
O65355 | MWSYVWLPLVALSLFKDSIIMAKAATILLPSQTGFDISRSPVCSAPDPNLNYRPVIGILSHPGDGASGRLSNATDASSIAASYVKLAESGGARVIPLIFNEPEEILFQKLELVNGVILTGGWAKEGLYFEIVKKIFNKVLERNDAGEHFPIYAICLGFELLTMIISQNRDIFEKMDARNSASSLQFVENVNIQGTIFQRFPPELLKKLGTDCLVMQNHRFGISPQSFEGNIALSNFFKIVTTCVDDNGKVYVSTVQSTKYPVTGFQWHPEKNAFEWGSSKIPHSEDAIQVTQHAANHLVSEARKSLNRPESKKVLSNLIYNYKPTYCGYAGIGYDEVYIFTQQRSLL | Function: Cleaves the polyglutamate sidechains of folate polyglutamates in the vacuole. Is important for polyglutamyl tail length determination before vacuolar exit. Plays a role on folate stability and intracellular folate content. Has endopeptidase activity against 4-amino-10-methylpteroyl penta-, tetra-, tri- and di-gamma-L-glutamate substrates and is responsible for the production of folic acid, also called pteroylglutamic acid (PteGlu) from teroylpolyglutamates.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
Sequence Mass (Da): 38642
Sequence Length: 347
Subcellular Location: Vacuole
EC: 3.4.19.9
|
Q54LN4 | MNKLIVVIISIILMVGIVKVNGQTKINNRPIIGILTQPTDGDMTTFGSQYIAASYVKYIESAGARVVPILYDIDIKSLTELMGSINGVFFPGGGVDFNNQTVYTDTIQSIWSQVVEFNNNGDYFPLWGTCMGFQELALLSADNFNLLSSYNSENYTVPLNFTSLAAGSRLFSLASSSIMQSLASEPITMNNHQFGLSPQTYQQTSSINTFFDVLSTNVDRDGNTFISTIEAKNYPIYGTQWHPEKPIFEWWDQEVMNHSFDSIMANQYTSNFFVNECRKSLHSFSDPSVEASTLIYNYTPQYSESTVPDFEQIYYFN | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
Sequence Mass (Da): 35661
Sequence Length: 317
Subcellular Location: Secreted
EC: 3.4.19.9
|
Q54HL4 | MIKLFSLFIYLYLISNLKLINTINNTPVIGILTQPFPSSINIKYGDNYLMASYVKYVESAGARVVPIFYNQDDESLTTIFKQINGILLPGGDVDFKTEIQYVKTLTLIWDYVLDVNINGDYFPLWGTCLGLEEIVSLQAESFDVLTDFNAENYSIPLNFSNIALESKIMKNCPTNIINSLANDPITMNNHHFGISPNTFDNNSLLNQFFNVLATNNDKSGNEFISLIESKDYPIYAIIWHPEKSPYSWYSKDATDHSFNAILACQYMSNFFVNETRKSNHKFNDEEVLFKSLIYNYNPTYTFKETHVEQIYIFNTSTNNTKNDFNINQIFSKKLFIIIFILIILFFK | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
Sequence Mass (Da): 40072
Sequence Length: 347
Subcellular Location: Secreted
EC: 3.4.19.9
|
A7YWG4 | MARLGRLLSVLGLVLCGATGLGLSAPPAPTPKKPIIGILMQKCHNKNMRALGKYYIAASYVKFLESAGARVVPVRLDLKNEEYEKLFKSINGVLFPGGSVNLMRSGYARVAKMFYNLSIKSFGEGDYFPVWGTCLGFEELIYLVSGESLLTLTDTVGIKLPLNFSRGTLQSRMFQNFPADLLLSLAVEPLTAHFHKWSLSVMNFTKNEKLKAFFSILTTNTDGNIDFISTMEGYRYPIYGVQWHPEKAPYEWGQLRGISHAPNAVKAAFYLAEFFVAEARKSNHHFESDVEETKALIYQYRPTYTGNVSSFQQSYIFD | Function: Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates. Exhibits either endo- or exopeptidase activity depending upon the tissue of origin. When secreted, it acts primarily as an endopeptidase (By similarity).
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
Sequence Mass (Da): 35683
Sequence Length: 318
Subcellular Location: Secreted
EC: 3.4.19.9
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Q92820 | MASPGCLLCVLGLLLCGAASLELSRPHGDTAKKPIIGILMQKCRNKVMKNYGRYYIAASYVKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGGSVDLRRSDYAKVAKIFYNLSIQSFDDGDYFPVWGTCLGFEELSLLISGECLLTATDTVDVAMPLNFTGGQLHSRMFQNFPTELLLSLAVEPLTANFHKWSLSVKNFTMNEKLKKFFNVLTTNTDGKIEFISTMEGYKYPVYGVQWHPEKAPYEWKNLDGISHAPNAVKTAFYLAEFFVNEARKNNHHFKSESEEEKALIYQFSPIYTGNISSFQQCYIFD | Function: Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free glutamate . May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
Sequence Mass (Da): 35964
Sequence Length: 318
Subcellular Location: Secreted
EC: 3.4.19.9
|
K5BDL0 | MPHDPSFTPTQLAARAAYLLRGNDLGTMTTAAPLLYPHMWSWDAAFVAIGLAPLSVERAVVELDTLLSAQWRNGMIPHIVFANGVDGYFPGPARWATATLADNAPRNRLTSGITQPPVHAIAVQRILEHARTRGRSTRAVAEAFLDRRWGDLMRWHRWLAECRDRNERGRITLYHGWESGMDNSPRWDSAYANVVPGKLPEYQRADNVIITDPSQRPSDGEYDRYLWLLEEMKAVRYDDERLPSVMSFQVEDVFFSAIFSVACQVLAEIGEDYKRPHADVKDLYLWAERFRAGVVETTDQRTGAARDFDVLAEKWLVTETAAQFAPLLCGGLPHDRERALLKLLEGPRFCGHPDLKYGLIPSTSPVSRDFRPREYWRGPVWPVLTWLFSWCFARRGWAERARLLRQEGLRQASDGSFAEYYEPFTGEPLGSMQQSWTAAAVLDWLG | Function: Catalyzes the hydrolysis of glucosylglycerate (GG) to glycerate and glucose . Involved in recovery from nitrogen starvation by promoting the rapid mobilization of the glucosylglycerate that accumulates under these conditions . Can also hydrolyze mannosylglycerate (MG), with tenfold lower efficiency .
Catalytic Activity: (2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + H2O = (R)-glycerate + D-glucose
Sequence Mass (Da): 50769
Sequence Length: 446
EC: 3.2.1.208
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Q62867 | MASLGRLLCAWVLLLCGLASPGLSGSYERGSKRPIIGIIMQECYGNMTKLGRFYIAASYVKFIESAGARVVPIRLDLNDAQYETLFRSINGVLLPGGGANLTHSGYSRVAKIFFTKALESFDNGDYFPVWGTCLGLEELSVLVSNDNLLTLTNTSSVKLPLNFTRDSKQSRMFRNLPEELLNSLASENLTANFHKWSLSVKNFTENEKLKKFFNILTVNTDGKTEFISSMEGYKYPIYAVQWHPEKAPFEWKKLRGISHAPNAVKTSFYLAKFFISEALKNDHHFENELEETESLIYQFCPVYTGNISSFQQAYMFN | Function: Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates . Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates. Exhibits either endo- or exopeptidase activity depending upon the tissue of origin. When secreted, it acts primarily as an endopeptidase (By similarity).
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
Sequence Mass (Da): 35830
Sequence Length: 317
Subcellular Location: Secreted
EC: 3.4.19.9
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P28967 | MLTVLAALSLLSLLTSATGRLAPDELCYAEPRRTGSPPNTQPERPPVIFEPPTIAIKAESKGCELILLDPPIDVSYRREDKVNASIAWFFDFGACRMPIAYREYYGCIGNAVPSPETCDAYSFTLIRTEGIVEFTIVNMSLLFQPGIYDSGNFIYSVLLDYHIFTGRVTLEVEKDTNYPCGMIHGLTAYGNINVDETMDNASPHPRAVGCFPEPIDNEAWANVTFTELGIPDPNSFLDDEGDYPNISDCHSWESYTYPNTLRQATGPQTLLVGAVGLRILAQAWKFVGDETYDTIRAEAKNLETHVPSSAAESSLENQSTQEESNSPEVAHLRSVNSDDSTHTGGASNGIQDCDSQLKTVYACLALIGLGTCAMIGLIVYICVLRSKLSSRNFSRAQNVKHRNYQRLEYVA | Function: Chemokine-binding protein that inhibits neutrophils' chemotaxis.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 45270
Sequence Length: 411
Subcellular Location: Virion membrane
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P06484 | MSQGAMRAVVPIIPFLLVLVGVSGVPTNVSSTTQPQLQTTGRPSHEAPNMTQTGTTDSPTAISLTTPDHTPPMPSIGLEEEEEEEGAGDGEHLEGGDGTRDTLPQSPGPAFPLAEDVEKDKPNRPVVPSPDPNNSPARPETSRPKTPPTIIGPLATRPTTRLTSKGRPLVPTPQHTPLFSFLTASPALDTLFVVSTVIHTLSFLCIGAMATHLCGGWSRRGRRTHPSVRYVCLPSERG | Function: Chemokine-binding protein that inhibits neutrophils' chemotaxis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 25239
Sequence Length: 238
Subcellular Location: Virion membrane
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P81780 | MHAIAPRLLLLFVLSGLPGTRGGSGVPGPINPPNNDVVFPGGSPVAQYCYAYPRLDDPGPLGSADAGRQDLPRRVVRHEPLGRSFLTGGLVLLAPPVRGFGAPNATYAAHVTYYRLTRACRQPILLRQYGGCRGGEPPSPKTCGSYTYTYQGGGPPTRYALVNASLLVPIWDRAAETFEYQIELGGELHVGLLWVEVGGEGPGPTAPPQAARAEGGPCVPPVPAGRPWRSVPPVWYSAPNPGFRGLRFRERCLPPQTPAAPSDLPRVAFAPQSLLVGITGRTFIRMARPTEDGVLPPHWAPGALDDGPYAPFPPRPRFRRALRTDPEGVDPDVRAPRTGRRLMALTEDASSDSPTSAPEKTPLPVSATAMAPSVDPSAEPTAPATTTPPDEMATQAATVAVTPEETAVASPPATASVESSPPPAAAATPGAGHTNTSSASAAKTPPTTPAPTTPPPTSTHATPRPTTPGPQTTPPGPATPGPVGASAAPTADSPLTALPPATAPGPSAANVSVAATTATPGTRGTARTPPTDPKTHPHGPADAPPGSPAPPPPEHRGGPEEFEGAGDGEPPEDDDSATGLAFRTPNPNKPPPARPGPIRPTLPPGILGPLAPNTPRPPAQAPAKDMPSGPTPQHIPLFWFLTASPALDILFIISTTIHTAAFVCLVALAAQLWRGRAGRRRYAHPSVRYVCLPPERD | Function: Chemokine-binding protein that inhibits neutrophils' chemotaxis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 72061
Sequence Length: 697
Subcellular Location: Virion membrane
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