ids
stringlengths
6
10
seqs
stringlengths
11
1.02k
texts
stringlengths
108
11.1k
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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.-
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.-
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
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
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.-
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
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.-
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
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.-
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.-
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.-
O85467
MIWNWLRKKKKSNTSKLNETDNQEQHSNNQEDDNKEQTRSMKHNKGKNNEQKDSSQDKQQSAKQGDSSQDKQQNPKQEDSSQDKQQNPKQGDSSQDKQQSAKQKDPSQDKQQNPKQEDSSQDKQQSAKQGDSSQDKQQSAKQGDSSQDKQQNAKQDEPSQSKQQSSGGNSIYDFTKPEKDRIHSLQNLIEKLKKSSDFVNYHTSDDETMPYWISYYRPSLDGEKLQKYLMPTLLERPNASLEELKEHIPMSGITITNDLQKIEDMVLKGHAIIQLNQQDQKCMLANIAIDNYRAPTPPLNESTVIGPQEGFVEDIDTNINLVRKRLPVLDLQTKEMIIGEFSKTKVVMMYLDNLAEKDNVDFLEESLRALEYDQINDSAYLQELMGEKSIFPLYINTERTDRVTKALIDGKIAIFVDGSPSVLLTPVSYFDFFISPEDYNVSWMYATFSRILRLIAVLFSICATPLYVAVLNYHYELIPSDLLETLILSRAQVPFPPLIEALFLELAIDLLREAGARLPMKVGQTLGIVGGIVIGQASVQAGLTSNILLIIVALSALASFITPIYKMGNAVRLLRFPFLAFAEIGGLFGISLGFIFLFTHLFRLTSLRKPYALFYPTRQQSVKDSWIRFPLTMIDTRDVQARPQHVKKAAKGISTKHRSDFDD
Function: Required for inosine germination. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 75311 Sequence Length: 663 Subcellular Location: Cell membrane
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
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
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
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
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
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
Q93N68
MEMKHLLKIIMVMALTGFMSGCSELEEIEERGFVVGAAYDIVKEKKANPIMKGTYQMVLPSKLSQQGGQGGGDSENYINVSAKADSVFEQIRIIAKKISRTLFFPHIQVIIFSEELLSHPYILQNTLDVYIRDHEMRRNIRLFVSNKNAEAILKQSAKPENLPAQYIDMLAEHPPKNAQMIEAARIGEVQEKMISNRSFVLPILELTKQGVQMNGAALFRGKDNKCVGNLSGEETVGMNYIIGKKIGGFFTIRKKNQLITYEIHKLRRKIKVSTTNATKPKFDIHLSLEGTLAELHFSDHKKVLNEKRLEKDISEEMEKRIQKSIKLVQKKYKVDVLELGEVYKRHNYKEWKKVSKNWDQGENYFSNAEITVHVHPTIEHSGSALPKRVK
Function: Contributes to the L-alanine germination response. Location Topology: Lipid-anchor Sequence Mass (Da): 44597 Sequence Length: 390 Subcellular Location: Membrane
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
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.-.-
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.-.-
Q3B7J2
MKMLPGVGVFGTGSSARVLVPLLRAEGFTVEALWGKTEEEAKQLAEEMNIAFYTSRTDDILLHQDVDLVCISIPPPLTRQISVKALGIGKNVVCEKAATSVDAFRMVTASRYYPQLMSLVGNVLRFLPAFVRMKQLISEHYVGAVMICDARIYSGSLLSPSYGWICDELMGGGGLHTMGTYIVDLLTHLTGRRAEKVHGLLKTFVRQNAAIRGIRHVTSDDFCFFQMLMGGGVCSTVTLNFNMPGAFVHEVMVVGSAGRLVARGADLYGQKNSATQEELLLRDSLAVGAGLPEQGPQDVPLLYLKGMVYMVQALRQSFQGQGDRRTWDRTPVSMAASFEDGLYMQSVVDAIKRSSRSGEWEAVEVLTEEPDTNQNLCEALQRNNL
Function: Promotes matrix assembly. Sequence Mass (Da): 42255 Sequence Length: 385 Subcellular Location: Secreted EC: 1.-.-.-
Q5BKK6
MKTLPGIGVFGTGNTARVLISLLRADGFSIEALWGKTDEEAKELAEEMGIPFYTCHTDDVLLHQEVDLVCISIPPPLTRQIAVKALGIGKNVICEKAASSIDAFTMVKAARYYPKLMSLVGNALRFLPAFDRMRQLILEQNYVGEIRICDVRVYGGSLLSSNYSWICDDLMGGGGLHTLGTYLVDLLTHLTNKRAEKVHGFLKTFVKQNEAISGIRYVTSDDFCFFQMQMTGGACSTVTLNFNMPGTFVHEVMVVGSAGRLVVRGTELFGQKNSASEEKLLLSDPLTREIADISDFEKVPPPYLMGIAHMVKALRQSFQDQEDRRTWDQKPLSVAATFEDGLYMQRVVDAIKRSNRSGEWESVELTNDETDSNQNLSEVIQHNL
Function: Promotes matrix assembly. Sequence Mass (Da): 42705 Sequence Length: 384 Subcellular Location: Secreted EC: 1.-.-.-
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
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
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
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
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
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
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
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
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
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
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
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
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
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