ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q6CIB4 | MKVAGFILGALIQFSLTEGHVEQNENANLTEMWGEDWPFSGIQTFAHLPHHKCLIDMEKKFDIGVIGVPFDTAVSFRGGARFGPQAIRKASQRQTSMRGFNFRADINPYQDWASVVDCGDVPVTPMDNCLALKMMTAAYENLLSHESQTSDNNLPPRFVTLGGDHSIILPALRALRKTYGRLAVIHFDSHLDTWAPSKYPSFWHSDTSEFTHGSMLWIAHNEGLLTENNNIHAGLRTRLSGSSFEDYDDDDKVGFHRIEADEIMDGGIKSIVEKIKSKIPSDVPVYISVDIDVLDPSAAPGTGTMEVGGWMTRELIRIIR... | 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 ... |
Q9RR46 | MSKIKVEELTKIFGKKASKASSLLSQGKSKTDILKETGATIGVNKASFSVEEGEIFVIMGLSGSGKSTLVRLLNRLIEPTSGKIWLDGKELSSLNKKELLEVRRKSMSMVFQNFGLFPNRTINRNVEYGLEIQGMDKEEREKNAAESLALVGLAGYGDQYPSQLSGGMQQRVGLARALANNPDILLMDEAFSALDPLNRKDMQDQLLDLQDKMKKTIIFITHDLDEALRIGDHIMIMRDGSVVQTGSPEEILAHPANEYVEKFIEDVDRSKVYTASNVMIRPEIVNFEKDGPRVALKRMREAGTSSVFVVKRNRELVGIV... | 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:... |
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 Ma... |
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.
Loca... |
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: 3... |
O36362 | MAHTGSTVCAFLIFAVLKNVFCQTPTSSSEVEDVIPEANTVSDNIIRQQRNNTAKGIHSDPSAFPFRVCSASNIGDIFRFQTSHSCPNTKDKEHNEGILLIFKENIVPYVFKVRKYRKIVTTSTIYNGIYADAVTNQHVFSKSVPIYETRRMDTIYQCYNSLDVTVGGNLLVYTDNDGSNMTVDLQPVDGLSNSVRRYHSQPEIHAEPGWLLGGYRRRTTVNCEVTETDARAVPPFRYFITNIGDTIEMSPFWSKAWNETEFSGEPDRTLTVAKDYRVVDYKFRGTQPQGHTRIFVDKEEYTLSWAQQFRNISYCRWAHW... | 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 hos... |
P17471 | MAARGGAERAAGAGDGRRGQRRHLRPGRVLAALRGPAAPGAGGARAALAAALLWATWALLLAAPAAGRPATTPPAPPPEEAASPAPPASPSPPGPDGDDAASPDNSTDVRAALRLAQAAGENSRFFVCPPPSGATVVRLAPARPCPEYGLGRNYTEGIGVIYKENIAPYTFKAIIYYKNVIVTTTWAGSTYAAITNQYTDRVPVGMGEITDLVDKKWRCLSKAEYLRSGRKVVAFDRDDDPWEAPLKPARLSAPGVRGWHTTDDVYTALGSAGLYRTGTSVNCIVEEVEARSVYPYDSFALSTGDIIYMSPFYGLREGAH... | 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 hos... |
P03188 | MTRRRVLSVVVLLAALACRLGAQTPEQPAPPATTVQPTATRQQTSFPFRVCELSSHGDLFRFSSDIQCPSFGTRENHTEGLLMVFKDNIIPYSFKVRSYTKIVTNILIYNGWYADSVTNRHEEKFSVDSYETDQMDTIYQCYNAVKMTKDGLTRVYVDRDGVNITVNLKPTGGLANGVRRYASQTELYDAPGWLIWTYRTRTTVNCLITDMMAKSNSPFDFFVTTTGQTVEMSPFYDGKNKETFHERADSFHVRTNYKIVDYDNRGTNPQGERRAFLDKGTYTLSWKLENRTAYCPLQHWQTFDSTIATETGKSIHFVTD... | 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 hos... |
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
|
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-dihydroneopter... |
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: st... |
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: st... |
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: st... |
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: st... |
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: st... |
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: st... |
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: st... |
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: st... |
P0AEP8 | MAKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATAGNIGVCLGTSGPAGTDMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDVQVAEIEFDPDMYEPLPVYKPAASRMQIEKAVEMLIQAERPVIVAGGGVINADAAALLQQFAELTSVPVIPTLMGWGCIPDDHELMAGMVGLQTAHRYGNATLLASDMVFGIGNRFANRHTGSVEKYTEGRKIVHIDIEPTQIGRVLCPDLGIVS... | 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... |
Q9NP62 | MEPDDFDSEDKEILSWDINDVKLPQNVKKTDWFQEWPDSYAKHIYSSEDKNAQRHLSSWAMRNTNNHNSRILKKSCLGVVVCGRDCLAEEGRKIYLRPAICDKARQKQQRKRCPNCDGPLKLIPCRGHGGFPVTNFWRHDGRFIFFQSKGEHDHPKPETKLEAEARRAMKKVNTAPSSVSLSLKGSTETRSLPGETQSQGSLPLTWSFQEGVQLPGSYSGHLIANTPQQNSLNDCFSFSKSYGLGGITDLTDQTSTVDPMKLYEKRKLSSSRTYSSGDLLPPSASGVYSDHGDLQAWSKNAALGRNHLADNCYSNYPFPL... | 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 c... |
P70348 | MELDDFDPEDKEILSWDINDVKLPQNVKTTDWFQEWPDSYVKHIYSSDDRNAQRHLSSWAMRNTNNHNSRILKKSCLGVVVCSRDCSTEEGRKIYLRPAICDKARQKQQRKSCPNCNGPLKLIPCRGHGGFPVTNFWRHDGRFIFFQSKGEHDHPRPETKLEAEARRAMKKVHMASASNSLRMKGRPAAKALPAEIPSQGSLPLTWSFQEGVQLPGTYSTPLIANAPQQNSLNDCLSFPKSYDLGGSTELEDPTSTLDSMKFYERCKFSSSRIYGSEEQFQPPVPGTYGDYEDLQTWNKNVALGRNPSDDIYYPAYPLPV... | 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 med... |
O75603 | MPAAAVQEAVGVCSYGMQLSWDINDPQMPQELALFDQFREWPDGYVRFIYSSDEKKAQRHLSGWAMRNTNNHNGHILKKSCLGVVVCTQACTLPDGSRLQLRPAICDKARLKQQKKACPNCHSALELIPCRGHSGYPVTNFWRLDGNAIFFQAKGVHDHPRPESKSETEARRSAIKRQMASFYQPQKKRIRESEAEENQDSSGHFSNIPPLENPEDFDIVTETSFPIPGQPCPSFPKSDVYKATCDLATFQGDKMPPFQKYSSPRIYLPRPPCSYELANPGYTNSSPYPTLYKDSTSIPNDTDWVHLNTLQCNVNSYSSY... | 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) negati... |
O09102 | MPADSTQDEDAVLSYGMKLTWDINDPQMPQEPTHFDHFREWPDGYVRFIYSSQEKKAQRHLSGWAMRNTNNHNGHILKKSCLGVVVCARACALKDGSHLQLRPAICDKARLKQQKKACPNCHSPLELVPCRGHSGYPVTNFWRLDGNAIFFQAKGVHDHPRPESKSETEGRRSALKRQMASFYQPQKRRSEEPEARSTQDIRGHLNSTAALEPTELFDMTADTSFPIPGQPSPSFPNSDVHRVTCDLPTFQGDIILPFQKYPNPSIYFPGPPWGYELASSGVTGSSPYSTLYKDSSVVPDDPDWIPLNSLQYNVSSYGSY... | 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) negati... |
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 ac... |
Q9AR19 | MDSHSSHLNAANRSRSSQTPSPSHSASASVTSSLHKRKLAATTAANAAASEDHAPPSSSFPPSSFSADTRDGALTSNDELESISARGADTDSDPDESEDIVVDDDEDEFAPEQDQDSSIRTFTAARLDSSSGVNGSSRNTKLKTESSTVKLESSDGGKDGGSSVVGTGVSGTVGGSSISGLVPKDESVKVLAENFQTSGAYIAREEALKREEQAGRLKFVCYSNDSIDEHMMCLIGLKNIFARQLPNMPKEYIVRLLMDRKHKSVMVLRGNLVVGGITYRPYHSQKFGEIAFCAITADEQVKGYGTRLMNHLKQHARDVD... | 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... |
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 | MDELLSMLNFLGMKDPEELFSDIPKSVRKKSIGIGGGLDEYRVIDRAMEIGRKNKTDMINFLGNGIYDRVIPEAVNYILSKPEFLDSYTPYQPEISQGMLQSMFEYQSLISDLMGMDVTNASMYDGYSALGEAARMAYRINGHSKILVPESSYDSKISVLRNYIWGLNMKIMKYRIGEDGMIDLDDLSSKIDSDTSAIVVENPNGYGILDKNIFGVKDIKKDAVLISYVDPISLGVVKPPGEYGSDIAVAEGQQLGIPMNFGGPLLGLMSFKMEHIRRSPGRIIGESIDSNGKRAYVMTLQTREQHIRRAKATSNICSNQ... | 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)-l... |
Q5JGX5 | MGKHYIPNSAHKDEMLKEIGFSSIEDLFSDVPKGMVKEFNLPEGKSEYEVFTELNETLSKNKTVLEMPSFLGAGTYFHYVPAHVKYLIERSEFLTAYTPYQPEISQGMLQALFEYQSLIAELVGLPIVNSSMYDWGTAMAEAALMSARVTKRNKFVVPKHLSPEKKLVLKTYTAGPGLETVEVPWDERGQMDIEKLKEAVEGAAGVYIEMPNFFGLLEENIREIGEIAHDAGALFVVGVDPTILGIVEAPGELGADIVVGEAAYFGNPMNFGGPRAGIFAVRNDRKLIRQMPGRIIGMTKDADGKRAFVMTLQTREQHIR... | 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)-l... |
Q9WY56 | MNYPYIPHTDEDVRAMLDFIGVSSIEELFSSIPVSARSSLNIPESRDEFSVFKQLKEISEMNNSLEDYAVFLGAGVYKRYVPTVVYDLAMKPDFLTAYTPYQAEVSQGTLQALFEYQTMVCELTGMEVANASMYDGATALAEAALMSFRLTGKEKVVVARSVHPEYRAVLRTYLEKRGFTVVEAGYDETGRVLLEEVDEETAAIAVQYPNFFGIIEDLDYVRSRSGNALLIVVVEPVSLALLEPPGSYGADIVVGEGQSLGLPMWFGGYSLGIFATREEYVRQMPGRLIGQTVDQAGNTAYTMILQTREQHIRRARATSN... | 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)-l... |
Q3SMB8 | MPFIPHTEEDVSAMLGAIGAASIEDLFDEIPPALKTGKLKDVPDGLPEMAVARLMQERASQDGFWSNFIGAGVYEHHIPAAIWQITTRGEFYSAYTPYQAEASQGTLQLIYEYQTMMTRLTGLDVSNASLYDGASALAEAVLMAVRSHKSSRRVLVPKTVHPVYRSVVVTTVRNQGIDLVELEYDPATGKTVLPSEPGAFAGLVIPQPNFFGVLEDVHTMTDWTHANGGLAIALVNPTTLAVLEAPGKWGTKGADIAVGEGQPLGAPMASGGPYFGFMCCRQDFVRQMPGRIVGRTVDLDGKPGFALTLQAREQHIRRSK... | 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)-l... |
Q9YA18 | MWRQSRWNEPLITEMSRRGRRGALPPRPDEKVVKEVGPLKLPQSLARGSPPSLPEVSEVEVVRHYTRLSQMAYGVDNGPVPLGSCTMKYNPRVAARLAFDPRLETLHPLQDDETVQGVLEAIYMVQEWLRHITGMDACTVHPAAGSQGELAGVLMIKRFHEMRGDLDKRRVIIVPDSAHGTNPASAAMGGFQVVEVPTGDDGNVDMEALKAAVGGDTAGLMITNPSTLGLFEENILEISRLVHEAGGLLYYDGANLNGIIGRARPGDMEFDIAHVNLHKTFSVPHGGGGPGSGPVCVKRVEVVDGVTLEDLLPGPRVVYS... | 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)-l... |
Q0AVH9 | MSKVIFARSVAGGGGFFLPPCDVAEIEPAAEINPEFLRAEAPLLPELSEVEVVRHYVELSQRAYGVDNGFYPLGSCTMKYNPKINEWAARLPGFANLHPYQPEESVQGALELLYRAEKLCCEIGGMDRFTLQPAAGAHGELTGLMIIKAYHQHRQDLARTKILVPDSAHGTNPATAHVLGFEVVEVKSNEEGLVDLQDLKACMSSEVAGLMLTNPNTLGLFEKEIEEIATVVHADGGLLYYDGANLNGIVGVARPGDMGFDVLHFNLHKTFGTPHGGGGPGSGPVGVKDFLSGFLPHPLVEKKEEGYYLDYDRPLSIGKV... | 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)-l... |
Q4FMV1 | MLKNAQKDFIQRHIGPSVDEQNVMLKELGYQNLDDLIKDTVPEKILLKDDLDIGDPNSEYKALRKLKDISKKNKIYSSFIGMGYYGTYTPYVILRNILENPGWYTSYTPYQPEVAQGRLEMLLNFQQMIIDFTGMDIANASLLDEGTAAAEAMGLSYRISKSESKKVFVSKNCHPQTIDVIKTRAEPLGLEIIVGDEDKDIKEDIICGIIQYPGTLGDIKDPSEAISKIHKFNGKAVLACDLLALAKLKTPAELGADIAVGSSQRFGIPMGYGGPHAAFFATKDEYKRSMPGRIVGVSVDRHGKKAYRLALQTREQHIRR... | 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)-l... |
Q7V9K4 | MRNTKASKFSDRHLGLIEEAQVEILNALGHADINDFISSVVPEEILDAQPPDELLPKALNEIEALEELRSIAKKNQIKRSLIGLGYYGTYTPAVIQRHVFENPAWYTSYTPYQAEIAQGRLEALFNFQTLITELTGLPIANASLLDEGTAAAEAMSLSFAVNKQTKARKFIVDDQVLPQTLAVLKTRAEPLELDIEVVNLTDLVINETVFGLLIQLPGKSGQLWDPSSLIAQAHEFNALVTVAIDPLAQVLIAPMGQLGVDIAIGSSQRFGVPIGFGGPHAAFFAIKEEYKRLVPGRLVGQSIDSKGHSALRLALQTREQ... | 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)-l... |
Q46IC1 | MSKAELKDFTFKSRHIGPTNEDEALMLQHLGYENAEEFISSVIPNEIFDSENNGVSIPDGCDQNKALTEINIISKKNVEHRSLIGLGYHSTVIPPVIQRNVLENPNWYTAYTPYQAEISQGRLEALFNFQTLISELTGLPISNASLLDEATAAAEAISLSLTVRKNKNANKFLVDQEILPQTLDVLKTRCEPLGISLEMFDNNNFEIDKNVFGILIQLPGKNGRIWDPTKIINDAHKCNAIVTIAIDPLAQVLIKPMGEFGADIVVGSAQRFGVPIAFGGPHAAFFATKEIYKRQIPGRIVGQSVDVEGNQALRLALQTR... | 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)-l... |
Q7NFJ5 | MSDLKRTPLCAQHLQLGARLVPFGGWEMPLQYSTLTREHRAVRTAVGLFDISHMGKYTLSGPDVLAQIQRLVPSDLARLQPGQAQYTVLLNEQAGIIDDLIFYCRSPEHWVVIVNGATNDKDRRWLAEHLQGVHFDDLTGTHTLLALQGPAAVETLQPLVDIDLARLGRFEHAQVSLAGKPAFLARTGYTGEDGFEIMSLEPEGIALWQSLTAAGVPPCGLGARDTLRLEAAMHLYGQDMDESTTPLEASLGWVIDWDKPDYFGREILLAQKAQGTERRLVGLTVEGRQIARHGYGLFDGEQQVGVVTSGTLTPTVDRPI... | 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... |
Q9K934 | MTELKKTPLFDLYEQYGGKVIDFGGWALPVQFSSIKEEHEAVRTKAGLFDVSHMGEVEVTGAQALNYLQRLVTNDVSKIKDGQAQYTAMCYENGGTVDDLLIYRRSEDQYLLVINAANIDKDIAWMEKHAIDGVSITNVSNQTAQLALQGPVAENVLQTLTEEPLADIKFFRFVDGVNIAGVNVLLSRTGYTGEDGFELYCLAEDAPVLWKKLIEAGKEHGVVPCGLGARDTLRFEAKLPLYGQELTKDISPIEAGIGFAVKVDKEDFIGKEILKKQKEQGAPRKLVGLEMVDKGIPRTGYEVYVDNQKIGFVTTGTQSP... | 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... |
A1WWA3 | MPQRTPLYDQHVGAGARVVDFAGWEMPLHYGSQLAEHQAVRSDVGLFDVSHMAVTDLSGPGARALLREQLANDVAKLDGRPGQALYSCLLNGRGGVVDDLIVYLREDASYRVVSNAATREKVRPRLLEQAHAAGVTAEARDDLAMIAVQGPRAASVLEQLFGDQAAAALACKPFQAAAIGEIFAGRTGYTGEDGFELILPADQAPALWDRLTEAGAQPCGLGARDSLRLEAGLNLNGHEMDEETTPLEAALGWTVAWDPEDRDFIGRAALEEQRRHGAAWRLIGLLVEGRAPAREGYVVRTDAGDGVITSGAHSPTLGGP... | 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... |
Q5V230 | MTLRAPPLSAIHERADASFTDFGGWEMPVEFESIRIEHEAVRSEAGKFDVSHMGQITVAGPDAATLTQRLTTNDVTVLDPGEAQYGAITDEDGIMLDDTVVYRLPEGAADEFLFIPNAGHDGEMTERWLSERDERGLDATVTNRTEEYAMIAVQGPDAPDLLSAETDVSLTALSRFEVAAGAVAGVDSLIARTGYTGEPGFEILCPPDDAGVVWDALECQPCGLGARDTLRLEMGFLLSGQEFHPVDEPRTPYEAGIGWTVKLDTEFVARDALEGVAADGPEEKLIGIELVDRGVPRHGYDVTTPDGEPIGHITSGTMSP... | 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... |
B8D1D7 | MKKTPLFEIHKELGARLIEFHGWSMPVQYTSIIEEHKAVRNQCGLFDVSHMGEILVEGPGALESLQKIVTNNVARLKKGQVLYTPMCKDDGGIIDDLLVYCLGQDKYLMVVNASNIEKDFNWVRDNSNQRTEVVNESDNYALLALQGPNSKKILEKVSSVNLDSLKFYNFTTGTLKGAEVLISRTGYTGELGYELYLSPDKAVEVWQALMEAGSDLGLIPAGLGARDTLRLEKGYCLYGNDIDENTHPLEAGLGWTVKFDKASFIGKRALLKYKEEGLSRKLVGFKLKGRGIPRHGYPIKDNGDQIGVVTSGSMSPTLSE... | 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... |
P48728 | MQRAVSVVARLGFRLQAFPPALCRPLSCAQEVLRRTPLYDFHLAHGGKMVAFAGWSLPVQYRDSHTDSHLHTRQHCSLFDVSHMLQTKILGSDRVKLMESLVVGDIAELRPNQGTLSLFTNEAGGILDDLIVTNTSEGHLYVVSNAGCWEKDLALMQDKVRELQNQGRDVGLEVLDNALLALQGPTAAQVLQAGVADDLRKLPFMTSAVMEVFGVSGCRVTRCGYTGEDGVEISVPVAGAVHLATAILKNPEVKLAGLAARDSLRLEAGLCLYGNDIDEHTTPVEGSLSWTLGKRRRAAMDFPGAKVIVPQLKGRVQRRR... | 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... |
Q5QVA8 | MGSRTPLYEAHVKAGAKMVDFHGWDMPLNYGSQIEEHHAVRRDCGVFDVSHMTIVDVEGSQAQAFLRYLLANDVAKLKTEGKAQYTSMLNENGGVIDDLIVYFFSENAYRMVVNSATRDRDLAWIEKVAADFDVTTKERDDMGMLALQGPKAADKIQGVLTAEQYAEIDGMKPFVGKDVGDYFIATTGYTGEKGYEIVVPAEQLEALWNDLLKADVAPCGLGARDTLRLEAGMNLYGQDMDENITPLEANMGWSVAFEPADRDFIGRKALEQKKAEGHDKLVGLVMEEKGVLRHGQKVTVEGGEGIITSGTFSPTLGFSV... | 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... |
O86567 | MSSTELRRTALDATHRALGATMTDFAGWDMPLRYGSEREEHVAVRTRAGLFDLSHMGEITVTGPQAAELLNFALVGNIGTVKPGRARYTMICREDGGILDDLIVYRLEEAEYMVVANASNAQVVLDALTERAAGFDAEVRDDRDAYALLAVQGPESPGILASLTDADLDGLKYYAGLPGTVAGVPALIARTGYTGEDGFELFVKPEHAVGLWQALTGAGEAAGLIPCGLSCRDTLRLEAGMPLYGNELSTALTPFDAGLGRVVKFEKEGDFVGRAALTEAAERAASRPPRVLVGLVAEGRRVPRSGYRVVAGGEVIGEVT... | 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... |
B2FR21 | MTQKTLLNDTHRALGAKMVDFGGWDMPIHYGSQLDEHHLVRRESGVFDVSHMTVVDLRGDQVRPFLRRLLANSVDKLKVPGKALYSCMLNPRGGVIDDLIVYYLGDDFFRMVVNASTREKDLAWLREQAAPFGVSVEQRPDLAILAVQGPQARAIVIGLARESEREALTKLGRFAALQVQSDDGVELFVARTGYTGEDGFEILLPQDAVVAFWNRLLAAGVKPAGLGARDTLRLEAGMNLYGQDMDEEISPYEAALAWTVSLDEGRDFIGRDALEAQKAAGTARQMIGLVMDEKGVLRHGQAVTTAGGQGEILSGTFSPT... | 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... |
Q67N36 | MNESLKRTPLYELHLKLGARMVPFGGWEMPVQYSSVIEEHRAVREAAGLFDVSHMGEFEVRGPQALDLIQLVSTNDAAKLAVGRVQYALMCYENGTVVDDILIYRLDEHRYWLVVNAGNTQKDWEWINTARERAGLHNLELIDRSAEIALLALQGPKAEEILQPLATGVVLSQLEPFSLAKNVTVSGVPTLVLSRTGYTGEDGFEIYVKAEDVAALWEALLEAGDEQGLLPCGLGARDTLRFEAKLPLYGHEISDQHNPLEAGLGFAVKLKKGVDFIGRDALARIKEQGPTRKLVGIEMIDRGVPRQGYPVAVGGEVVGE... | 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... |
A6LP67 | MKYTPLYEEHVKLGAKMVDFAGFNMPIQYTSIKDEVLAVRKNVGMFDVSHMGEVIVEGKDSTKFVDFLITNDFKNLKPGEIVYTAMCNENGGFVDDLLAYKISEEKAMLVINASNIEKDFSWMKKISESFDVTLENKSDEYVLIAVQGPNAQKTLQKITNVDLEQIGYYTFTEGNVLDIKAIISRTGYTGEDGFEIYTTDKDGIIKIWKKLLNLNVIPAGLGARDCLRLEASLLLYGNDMDETITPLEVGIKWAVKFEKDFMGKEALKRQLEEGTSRRLKGFKIIDKGIARHGYKVFKDGKEIGYVTSGTFSPTLNQAIG... | 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... |
Q9WY54 | MKRTPLFEKHVELGAKMVDFAGWEMPLYYTSIFEEVMAVRKSVGMFDVSHMGEFLVKGPEAVSFIDFLITNDFSSLPDGKAIYSVMCNENGGIIDDLVVYKVSPDEALMVVNAANIEKDFNWIKSHSKNFDVEVSNISDTTALIAFQGPKAQETLQELVEDGLEEIAYYSFRKSIVAGVETLVSRTGYTGEDGFELMLEAKNAPKVWDALMNLLRKIDGRPAGLGARDVCRLEATYLLYGQDMDENTNPFEVGLSWVVKLNKDFVGKEALLKAKEKVERKLVALELSGKRIARKGYEVLKNGERVGEITSGNFSPTLGKS... | 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... |
Q9BSE5 | MLRLLASGCARGPGPGVGARPAAGLFHPGRRQSRQASDAPRNQPPSPEFVARPVGVCSMMRLPVQTSPEGLDAAFIGVPLDTGTSNRPGARFGPRRIREESVMLGTVNPSTGALPFQSLMVADLGDVNVNLYNLQDSCRRIQEAYEKIVAAGCIPLTLGGDHTITYPILQAMAKKHGPVGLLHVDAHTDTTDKALGEKLYHGAPFRRCVDEGLLDCKRVVQIGIRGSSTTLDPYRYNRSQGFRVVLAEDCWMKSLVPLMGEVRQQMGGKPIYISFDIDALDPAYAPGTGTPEIAGLTPSQALEIIRGCQGLNVMGCDLVE... | 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 aci... |
A2AS89 | MLRLLRSSWARGLGSGVATWRPSAGLFRPGCPGIRQASGASDTPHHQSPSSESPVQPVGVGVCSMMRLPLQSSPEGLDAAFIGVPLDTGTSNRPGARFGPCRIREESLMLGAVNPSTGALPFQSLRVADLGNVNVNLYNLQDSCLLIREAYQNVLAAGCIPLTLGGDQTITYPILQAVAKEHGPVGLVHVGAHTNTTDKPREEKVYHRTPFRRSVDEGLLDSKRVVQIGIRGSSRTLDPYRYSRSQGFRVVLAEDCWMKSLVPLMAEVRQQMGGKPLYISFAIDALDPAYAPGTGTPEIAGLTPSQALEIIRGCQGLNVV... | 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 aci... |
Q8TB36 | MAERQEEQRGSPPLRAEGKADAEVKLILYHWTHSFSSQKVRLVIAEKALKCEEHDVSLPLSEHNEPWFMRLNSTGEVPVLIHGENIICEATQIIDYLEQTFLDERTPRLMPDKESMYYPRVQHYRELLDSLPMDAYTHGCILHPELTVDSMIPAYATTRIRSQIGNTESELKKLAEENPDLQEAYIAKQKRLKSKLLDHDNVKYLKKILDELEKVLDQVETELQRRNEETPEEGQQPWLCGESFTLADVSLAVTLHRLKFLGFARRNWGNGKRPNLETYYERVLKRKTFNKVLGHVNNILISAVLPTAFRVAKKRAPKVL... | 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 Loca... |
O88741 | MARRQDEARAGVPLRVEGPPDKEVHLILYHWTHSFSSQKVRLVIAEKALKCEEHDVSLPLSEHNEPWFMRLNSAGEVPVLVHGENIICEATQIIDYLEQTFLDERTPRLMPDEGSMYYPRVQHYRELLDSLPMDAYTHGCILHPELTVDSMIPAYATTRIRSQIGNTESELKKLAEENPDLQEAYIAKQKRLKSKLLDHDNVKYLKKILDELEKVLDQVETELQRRNEETPEEGNQPWLCGESFTLADVSLAVTLHRLKFLGFARRNWGHGKRPNLETYYERVLKRKTFNKVLGHVNNILISAVLPTAFRVAKKRAPKVL... | 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 Loca... |
Q9LIN2 | METNLLLVKCVLLASCLIHPRACSPSCNFPAIFNFGDSNSDTGGLSASFGQAPYPNGQTFFHSPSGRFSDGRLIIDFIAEELGLPYLNAFLDSIGSNFSHGANFATAGSTVRPPNATIAQSGVSPISLDVQLVQFSDFITRSQLIRNRGGVFKKLLPKKEYFSQALYTFDIGQNDLTAGLKLNMTSDQIKAYIPDVHDQLSNVIRKVYSKGGRRFWIHNTAPLGCLPYVLDRFPVPASQIDNHGCAIPRNEIARYYNSELKRRVIELRKELSEAAFTYVDIYSIKLTLITQAKKLGFRYPLVACCGHGGKYNFNKLIKCG... | 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 + hexadecan... |
Q55EC7 | MAEADPGLPTQAIWDIPFESLEFNEKIGKGSFGSVFRGCYLGLDVAIKKIEKADDPEYLKYIDREVSMLQSLRHPFIVNFSGICVHSSGLYIVTEFVSGGDVRQLLKKTPPIGWDKRVSIAVDLAKAMVFLHAKKIIHRDLKSKNILLDEFQRIRLCDFGFARMSEQTKKSRHMTMCGTEGWVAPEILLGMSYDTSCDVFSYGVVLAELITGRKPGVDLWVRSPETCFDINPEELKQKSIPGCPSELISVCVECCLYEPLTRPKFDEILSQLKVCQNNLKVATAAAAAAAAAAAAAAAVVSTPTIQTPIIQTPNISFSPN... | 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 | MLPNNQWQIPINNGLTHQENMAAHAAVMKLRVHDLQSIISQLSLRKPRPQKSEHQKVVVESLRDPHHARQIYQMASNFPNGNYEMQKRPATTSQVRSHPYVLPSRSGASNHLVNHHYQQQQQQQPQPHNLLHQQMMASHHSHLQQQHHPSTVRWLTPELLEEQLRGSMRYGAPAAAAATNAPLHSSFPNHGRSSQQSLQKSEKSNRPKKMYADNFEPLPLPFYDVISVLLKPVELHSSDSPTLKQTKQLQFPFLLTAEHISKISYRADVTPLPRYELQLRFFNLTEPVQGPQKDDFPLNCYARVDDSVVQLPNVIPTNKT... | 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 t... |
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 ... |
B0XT72 | MKASAVTAALAVGASTVLAAPSIKARDDVTPITVKGNAFFKGDERFYIRGVDYQPGGSSDLADPIADADGCKRDIAKFKELGLNTIRVYSVDNSKNHDECMNALADAGIYLVLDVNTPKYSINRAKPKESYNDVYLQYIFATVDAFAGYKNTLAFFSGNEVINDGPSSSAAPYVKAVTRDLRQYIRSRKYREIPVGYSAADIDTNRLQMAQYMNCGSDDERSDFFAFNDYSWCDPSSFKTSGWDQKVKNFTGYGLPLFLSEYGCNTNKRQFQEVSSLYSTDMTGVYSGGLVYEYSQEASNYGLVEISGNNVKELPDFDAL... | 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 morphogen... |
B0Y8H9 | MLPTYVRLFTAVCALATTASAVVPIEVKGKDFVNSKTGDRFQILGVDYQPGGSSGFTKDKDPLSDPDACLRDAALMQRLGVNTIRIYNLSPSLNHDECASIFNAAGIYMILDVNSPLYGGYLDRTDPESTYNDVYFKQVFGVIEAFKNFPNTLAFFAGNEVINEQSVKNVPTYVRAIQRDMKDYIAKNLDRSIPVGYSAADIRPILMDTLNYFMCADDANSQSDFFGLNSYSWCGNSSYTKSGYDVLTKDFADASIPVFFSEYGCNEVQPRYFSEVQALYGQEMTQSFSGGLVYEYTQEENDYGLVQINDNGTVTLLVDY... | 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 morphogen... |
B0XT09 | MRYSLVVGVVLLSGCAIATGSKFFYANNGSEFYIRGVAYQEDYSGGGAGGTGQSEANYVDPLADGSKCERDIPYLLQLRTNVIRTYAVNPSLNHDACMQKLSDAGIYVITDLASPDESITSNSPVWTVDQYARYTSVIDAFQKYDNVIGFFAGNEVVNQANQSAGAAFVKAAARDMKAYIKTKGYRQSLAIGYATTDNPEIRLPLSDYLNCGDQADAVDFFGYNIYEWCGDKTFQTSGYQNRTEEYKDYSIPIFFSEYGCNTEKPRKFTDVPVLFGPQMDNVWSGGIVYMYFETTNDYGLVSVSGSAVTPEPDFTYLSSE... | 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 morphogen... |
O85467 | MIWNWLRKKKKSNTSKLNETDNQEQHSNNQEDDNKEQTRSMKHNKGKNNEQKDSSQDKQQSAKQGDSSQDKQQNPKQEDSSQDKQQNPKQGDSSQDKQQSAKQKDPSQDKQQNPKQEDSSQDKQQSAKQGDSSQDKQQSAKQGDSSQDKQQNAKQDEPSQSKQQSSGGNSIYDFTKPEKDRIHSLQNLIEKLKKSSDFVNYHTSDDETMPYWISYYRPSLDGEKLQKYLMPTLLERPNASLEELKEHIPMSGITITNDLQKIEDMVLKGHAIIQLNQQDQKCMLANIAIDNYRAPTPPLNESTVIGPQEGFVEDIDTNIN... | 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 | MPLFSKRKNNTDSKDKQNTDERNQEQQQEKERPVLISPSLAKNIAETKKEVGSSSDVIIREIKIGEQDHVHLAVIYISGLVDNNTIHESLIDPLVQDESIQNTHAIQQILEKTLPLGGVKAEKSWDKLFSELMLGNALIFADGHDEALICSTQGGEQRSIQEPSTQVSFRGPRQGFTESLQTNISMIRRYIKNPNLWVEKMKKGSVTNTDIALMYIQGICDEKVLKEVKQRLEKIDIDSILESGYIEQLIEDETFTTFPTMYHTERPDVVAGNLLEGRFAIIVDGTPFVLIAPALFVQFFQSVEDYYSRFDIATSIRILR... | 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 | MEKARISIRQLFVMIIIFELGSSLLITPGSMAGRDAWIAVLLGCAIGLFLFYLYQGIYQCYPNSSPKEYMDDMLGTKLSWLFSFLYILYFAYIAARVLRDFGEMLLTFAYHDTPIIIVNALLMVVSIYAVRKGIEVLARAAELLFGAMYLLGAIGLVLIIVSGTIDPHNLKPVLANGISPVLHSVFTQTMYVPFGEVVLFVMIFPNLNDRKDVKKMGMIAMAISGLIVALTVAINISVLDVDLTLRSQFPLLSTIQTIKVEEFLDRLDVFFMLALIIGGFFKVSLYLYATVVGTSTLFKEKNPSQLAYPMGLGILILSIT... | 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 | MVRKCLLAVLMLLSVIVLPGCWDKRELTDLAIISAIGIDRTNDSNYVLHLQIINPGNVAGGLQGGGAGDRPPVSVYSIEGNNITEALRKASMKVSRRLYFAHTNLVVINEKLAKEEGLDFVLDNLDRDTEFRTTATFVVAHKTKAENIVKILTPIDKIPSNKVNKTLDFTEAQYGRVVKINIQDVLKTLAANTMAPVIPGYMMIGDDKKGVSMENTQATDPKAILQADGLAVFDKAGYLKYWLEDDESVGAVWLMNKIQHTFINADWGKTKDAVSLQVTHQDTKLVPKMRNGRPYIHVKVSVEGIIDAVKYPFQLSDPKV... | 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 | MTADRWAGRTVLVTGALGFIGSHFVRQLDARGAEVLALYRTERPEIQAELAALNRVRLVRTELRDESDVRGAFKYLAPSIDTVVHCAAMDGNAQFKLERSAEILDSNQRTISNLLNCVRDFGVGEVVVMSSSELYSASPTVAAREEDDFRRSMRYTDNGYVLSKTYGEILARLHREQFGTNVFLVRPGNVYGPGDGFDCSRGRVIPSMLAKADAGEEIEIWGDGSQTRSFVHVADLVRASLRLLETGKYPEMNVAGAEQVSILELAGMVMAVLGRPERIRLDPSRPVGAPSRLLDLSRMSEVIDFDPQPLRAGLEETARW... | 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 t... |
Q93N70 | MGKLLELEGNLFEVMKEIRDELGSPNDLTIREVALAGSFTRCAVVFLCGLTDKDNVYKYVVRTLQYEEVQNEAAVVQTLLDRFISIAEVGKKTTFPDIINAILAGDTVILIDNIQTAIIINSRAWEKRSLEPPVTEDLIRGPRVGLNEDINVNKMLIRRSLRDPKLRFQSYIMGKRSQKEVTLVYIEDIINPHIVKELDRRLQSIVTDVVLETGTIEQLIQDNNLSPFPQFLNTERPDNIIASLAKGKAAILVDGSPFALIAPLVFVDIFQSVEDHYERWVIGTLLRFLRMGSGIIAVLLPAMYVALVSYHQGLIPSKLA... | 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 | MKPFEYGDEEIGSREIGFAVSSTIIGIGALSMPRDIANQTLFSDGWIILLLGGLICAVLGWFVTRVAILFPKQNFVQYTSAHLTKPVAYTISSILVLTFAALTAYESRMISVISQTYLFSDTPIQLLSFFFLLVVIYGIAGSRAALLRLNVLFLPIVLIAIVLLSLLNINLMEINNLLPAFQTKVSQYAVGVKNSIFTFIGFEVALFYAVLLNNKTAKKAPMAVAKAVMVNVLSYILIYVTCISVFTYMTTRGLTYPTIELGKEIEIGGGFLERFDAIFFTTWIITIYNTTAMYYDVASLLFCAMFPKVKKQIFIFISAP... | 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 | MEMKHLLKIIMVMALTGFMSGCSELEEIEERGFVVGAAYDIVKEKKANPIMKGTYQMVLPSKLSQQGGQGGGDSENYINVSAKADSVFEQIRIIAKKISRTLFFPHIQVIIFSEELLSHPYILQNTLDVYIRDHEMRRNIRLFVSNKNAEAILKQSAKPENLPAQYIDMLAEHPPKNAQMIEAARIGEVQEKMISNRSFVLPILELTKQGVQMNGAALFRGKDNKCVGNLSGEETVGMNYIIGKKIGGFFTIRKKNQLITYEIHKLRRKIKVSTTNATKPKFDIHLSLEGTLAELHFSDHKKVLNEKRLEKDISEEMEKR... | 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 | MEFEFFFQIALILLSTKLAGDLSVRLGQPSVLGKLIVGIVIGPAVLGWIENSELLTQLSNVGVILLMFMAGLETDLEELNANRNSSLAVALGGIILPFVGGYVSGLVMGMEQGNAVFLGLLLCATSVSISVQTLRDLGKMKTRESTTMLGAAVFDDILVVILLAFAMSFLGTDDVNLTMVILKKVVFFASIILIGWKGVPAIMRWLSPLRVSESIVSAALIICFSFAYFGELLGIAGIIGAFAAGIAISQTNYKHEVEKKVEPIAYAMFVPVFFVSIGMNITFDGIGNQIWFILALTVIAVLTKLIGCGFGARMTGFDAK... | 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 spor... |
Q6FKZ9 | MDLTVEPNLKSLITSSTHKWIFVGGKGGVGKTTSSCSIAIQMALAQPHKKFLLISTDPAHNLSDAFGEKFDKDARKVTGMDNLSCMEIDPSAALKDMNDMAVSSAGENGNDDLGGLLQGGALADLTGSIPGIDEALSFMEVMKHIKKQEQGDGESFDTVIFDTAPTGHTLRFLQLPTTLSKLLDKFSEITGRLGPMLNSMMGSGNVDIAGKLNELKANVETIKEQFTDPDLTTFVCVCISEFLSLYETERLIQELISYDMDVNSIIVNQLLFAEFDQEHNCKRCQSRWKMQKKYLDQIDELYEDFHVVKMPLCAGEIRGL... | 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 ... |
Q2GXW1 | MSATLINVDDGDAMEPTLQSILDQRSLRWIFVGGKGGVGKTTTSCSLAIQLAKVRRSVLLISTDPAHNLSDAFSQKFGKEARLIDGFENLSAMEIDPNGSIQDLLAGQGEGDAGADMGGMGGMMQDLAFAIPGIDEAMSFAEVLKQVKSLSYETIIFDTAPTGHTLRFLQFPSVLEKALAKVSQLSNQYGPLLNGFLGSNGTLPNGQNLNEMMEKLETLRATISEVNTQFKDERLTTFVCVCIPEFLSLYETERMIQELASYGIDTHSIVVNQLLFPKPGSDCEQCTARRRMQKKYLEQIEELYDEFNVVKMPLLVEEVR... | 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 ... |
Q3B7J2 | MKMLPGVGVFGTGSSARVLVPLLRAEGFTVEALWGKTEEEAKQLAEEMNIAFYTSRTDDILLHQDVDLVCISIPPPLTRQISVKALGIGKNVVCEKAATSVDAFRMVTASRYYPQLMSLVGNVLRFLPAFVRMKQLISEHYVGAVMICDARIYSGSLLSPSYGWICDELMGGGGLHTMGTYIVDLLTHLTGRRAEKVHGLLKTFVRQNAAIRGIRHVTSDDFCFFQMLMGGGVCSTVTLNFNMPGAFVHEVMVVGSAGRLVARGADLYGQKNSATQEELLLRDSLAVGAGLPEQGPQDVPLLYLKGMVYMVQALRQSFQG... | Function: Promotes matrix assembly.
Sequence Mass (Da): 42255
Sequence Length: 385
Subcellular Location: Secreted
EC: 1.-.-.-
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Q5BKK6 | MKTLPGIGVFGTGNTARVLISLLRADGFSIEALWGKTDEEAKELAEEMGIPFYTCHTDDVLLHQEVDLVCISIPPPLTRQIAVKALGIGKNVICEKAASSIDAFTMVKAARYYPKLMSLVGNALRFLPAFDRMRQLILEQNYVGEIRICDVRVYGGSLLSSNYSWICDDLMGGGGLHTLGTYLVDLLTHLTNKRAEKVHGFLKTFVKQNEAISGIRYVTSDDFCFFQMQMTGGACSTVTLNFNMPGTFVHEVMVVGSAGRLVVRGTELFGQKNSASEEKLLLSDPLTREIADISDFEKVPPPYLMGIAHMVKALRQSFQD... | Function: Promotes matrix assembly.
Sequence Mass (Da): 42705
Sequence Length: 384
Subcellular Location: Secreted
EC: 1.-.-.-
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Q07982 | MTNKISSSDNLSNAVSATDDNASRTPNLTRRALVGGGVGLAAAGALASGLQAATLPAGASQVPTTPAGRPMPYAIRPMPEDRRFGYAIVGLGKYALNQILPGFAGCQHSRIEALVSGNAEKAKIVAAEYGVDPRKIYDYSNFDKIAKDPKIDAVYIILPNSLHAEFAIRAFKAGKHVMCEKPMATSVADCQRMIDAAKAANKKLMIGYRCHYDPMNRAAVKLIRENQLGKLGMVTTDNSDVMDQNDPAQQWRLRRELAGGGSLMDIGIYGLNGTRYLLGEEPIEVRAYTYSDPNDERFVEVEDRIIWQMRFRSGALSHGA... | 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: 43... |
O53507 | MAGAITDQLRRYLHGRRRAAAHMGSDYDGLIADLEDFVLGGGKRLRPLFAYWGWHAVASREPDPDVLLLFSALELLHAWALVHDDLIDRSATRRGRPTAQLRYAALHRDRDWRGSPDQFGMSAAILLGDLAQVWADDIVSKVCQSALAPDAQRRVHRVWADIRNEVLGGQYLDIVAEASAAESIESAMNVATLKTACYTVSRPLQLGTAAAADRSDVAAIFEHFGADLGVAFQLRDDVLGVFGDPAVTGKPSGDDLKSGKRTVLVAEAVELADRSDPLAAKLLRTSIGTRLTDAQVRELRTVIEAVGARAAAESRIAALT... | 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 + isopenten... |
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... |
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... |
Q3IPL1 | MTSADHVESAIAERREIVNEAVSEQLPVQKPERLYSASRYLLDAGGKRLRPTILLLAAESLADVEPLSADYRQFPSLPGDEVDVLSAAVSIEVIQSFTLIHDDIMDDDDLRRGVPAVHREYDLETAILAGDTLYSKAFEYMLDTGAPAERSVEALDELATTCTEICEGQALDVDFENRSDVTTEEYLEMVEFKTAVLYAAAASIPAILLGSDDETVEALHGYGLDIGRAFQIQDDLLDLTAPSDELGKQRGSDLVENKRTVITLHARDQGIDVEGLVSDDPSDAEIEAAVQTLEDAGSIDFAREMALDLVTSGKERLDVL... | 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 ge... |
Q06210 | MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDGGNDKDWEANACKIQLIKKKGKVKALDEEVHKQQDMDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDNRESQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEHKLSTDHIPILYRTARTQIGSKFTRWGSQGERGKDKKGSCNLSRVDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGDHP... | 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 c... |
P82808 | MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGLDGGNDKDWEANACKIQLIKKKGKVKALDEEVHKQQDMDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDNWESQDVSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEHKLSTDHIPILYRTGKDKKGSCGLSRVDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTARDHPGRAVQTLQMELQQIMKGN... | 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-Gl... |
O94808 | MCGIFAYMNYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNHEVKERHIQLVKKRGKVKALDEELYKQDSMDLKVEFETHFGIAHTRWATHGVPSAVNSHPQRSDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNRETEDITFSTLVERVIQQLEGAFALVFKSVHYPGEAVATRRGSPLLIGVRSKYKLSTEQIPILYRTCTLENVKNICKTRMKRLDSSACLHAVGDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSASDDPSRAIQTLQMELQQIMKG... | 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 Lengt... |
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. Cann... |
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)-geranylgera... |
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)-geranylgera... |
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
... |
Q9SYL6 | MIDNNCLYKEELNRNSYSGLAKEASESILLPSESGFDGSRSPVCSSPDPNLNYRPVIGILSHPGDGASGRLTNDTSSTYIAASYVKFAEAGGARVIPLIYNEPEEVLFQKLELVNGVIFTGGWAKKYDYFEIVKKIFTKALERNDAGEHFPVYGICLGFELMSIIISQNRDILERFDAEDNASSLQFVDNVNNDGTLFQRFPPELLKKLSTDCLVMQKHKYGITPANFQANPALSSFFEILTTCIDENSKTYVSTVKAKRYPITGFQWHPEKNAFEWGSSAIPHSEDAIQVTQHAASYLVSEARKSLNRPESQKVLSNLI... | 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,... |
O65355 | MWSYVWLPLVALSLFKDSIIMAKAATILLPSQTGFDISRSPVCSAPDPNLNYRPVIGILSHPGDGASGRLSNATDASSIAASYVKLAESGGARVIPLIFNEPEEILFQKLELVNGVILTGGWAKEGLYFEIVKKIFNKVLERNDAGEHFPIYAICLGFELLTMIISQNRDIFEKMDARNSASSLQFVENVNIQGTIFQRFPPELLKKLGTDCLVMQNHRFGISPQSFEGNIALSNFFKIVTTCVDDNGKVYVSTVQSTKYPVTGFQWHPEKNAFEWGSSKIPHSEDAIQVTQHAANHLVSEARKSLNRPESKKVLSNLIY... | 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... |
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
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Q54HL4 | MIKLFSLFIYLYLISNLKLINTINNTPVIGILTQPFPSSINIKYGDNYLMASYVKYVESAGARVVPIFYNQDDESLTTIFKQINGILLPGGDVDFKTEIQYVKTLTLIWDYVLDVNINGDYFPLWGTCLGLEEIVSLQAESFDVLTDFNAENYSIPLNFSNIALESKIMKNCPTNIINSLANDPITMNNHHFGISPNTFDNNSLLNQFFNVLATNNDKSGNEFISLIESKDYPIYAIIWHPEKSPYSWYSKDATDHSFNAILACQYMSNFFVNETRKSNHKFNDEEVLFKSLIYNYNPTYTFKETHVEQIYIFNTSTNNT... | 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
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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 metab... |
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 meta... |
K5BDL0 | MPHDPSFTPTQLAARAAYLLRGNDLGTMTTAAPLLYPHMWSWDAAFVAIGLAPLSVERAVVELDTLLSAQWRNGMIPHIVFANGVDGYFPGPARWATATLADNAPRNRLTSGITQPPVHAIAVQRILEHARTRGRSTRAVAEAFLDRRWGDLMRWHRWLAECRDRNERGRITLYHGWESGMDNSPRWDSAYANVVPGKLPEYQRADNVIITDPSQRPSDGEYDRYLWLLEEMKAVRYDDERLPSVMSFQVEDVFFSAIFSVACQVLAEIGEDYKRPHADVKDLYLWAERFRAGVVETTDQRTGAARDFDVLAEKWLVTET... | 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 .
Catalyti... |
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 meta... |
P28967 | MLTVLAALSLLSLLTSATGRLAPDELCYAEPRRTGSPPNTQPERPPVIFEPPTIAIKAESKGCELILLDPPIDVSYRREDKVNASIAWFFDFGACRMPIAYREYYGCIGNAVPSPETCDAYSFTLIRTEGIVEFTIVNMSLLFQPGIYDSGNFIYSVLLDYHIFTGRVTLEVEKDTNYPCGMIHGLTAYGNINVDETMDNASPHPRAVGCFPEPIDNEAWANVTFTELGIPDPNSFLDDEGDYPNISDCHSWESYTYPNTLRQATGPQTLLVGAVGLRILAQAWKFVGDETYDTIRAEAKNLETHVPSSAAESSLENQST... | 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 | MHAIAPRLLLLFVLSGLPGTRGGSGVPGPINPPNNDVVFPGGSPVAQYCYAYPRLDDPGPLGSADAGRQDLPRRVVRHEPLGRSFLTGGLVLLAPPVRGFGAPNATYAAHVTYYRLTRACRQPILLRQYGGCRGGEPPSPKTCGSYTYTYQGGGPPTRYALVNASLLVPIWDRAAETFEYQIELGGELHVGLLWVEVGGEGPGPTAPPQAARAEGGPCVPPVPAGRPWRSVPPVWYSAPNPGFRGLRFRERCLPPQTPAAPSDLPRVAFAPQSLLVGITGRTFIRMARPTEDGVLPPHWAPGALDDGPYAPFPPRPRFRR... | 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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