ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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P58142 | MTGEAVSGQDVSNPGKSSWRVTVLGGGAWGTALALAMLRAGHKVRLFARDPQTVAAIGQGQNPRYLPGIAIAPGIEATSDIAAALSGADCVLAVTPAQSLRATLAVAKDNMPDGIPLVLCAKGIERDTGALLSAIVEEILPRNPVAALSGPSFATDVARGLPTAVVVAARDEALAADLAARFSAQNLRCYSSDDLIGVEIGGALKNVFAIAAGAVTGAGLGASAQAAMVTRGFVELRRIGAAFGARPETLMGLSGLGDLLLTCSSAQSRNFAYGLTLGQGKALAGLPLAEGVPTAAIAARIAVERGIDAPIIAAVAAILDGAITISQAVTALMTRPLKTETND | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 34438
Sequence Length: 343
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
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Q9R9L6 | MSGKSKSAPKIVVVGAGAFGTALSAVAAAKDKANVTLLARREEAAAECRRTGRNDAVLPGIPLPPGLVYSSQAAALEDADIVLFAMPSQAHRDAARSYGPAIGARAIVVTCAKGMEQSTGQLLTDVLEEELPGRRIGVLSGPGFAADIASGLPTAMVIAAPDTAIATELAEALSGRTFRLYPSADRTGVQLGGALKNVLAIACGIVEGAGLGDSARAALISRGLAEMSRFIVARGGEADTVRGLSGLGDLVLTATSHQSRNLRFGIALGKDGRAAAGSSELVEGAFAASVAARVAGALGIEMPVTEAVAAIVDGKLDVRSALEQLMSRPITHE | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 33674
Sequence Length: 333
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
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Q7Y208 | MNSRPSNPTKLVIRSSTLLFCGVVLIHLFAAQIDAQRSTSRWQTLNGDAPLVIARGGFSGLYPDSSIAAYQLATLTSVADVVLWCDLQLTKDGLGICFPDLNLANASTIDRVYPNREKSYSVNGVTTKGWFPNDFSLTELQNFLLIRGILSRTDRFDGNGYLISTIEDVVTTLNREGFWLNVQHDAFYEQQNLSMSSFLLSVSRTVSIDFISSPEVNFFKKITGSFGRNGPTFVFQFLGKEDFEPTTNRTYGSILSNLTFVKTFASGILVPKSYILPLDDEQYLVPHTSLVQDAHKAGLQVYVSGFANDVDIAYNYSSDPVSEYLSFVDNGDFSVDGVLSDFPITASAAVDCFSHIGRNATKQVDFLVISKDGASGDYPGCTDLAYEKAIKDGADVIDCSVQMSSDGVPFCLRSIDLRNSIAALQNTFSNRSTSVPEISSVPGIFTFSLTWPEIQSLTPAISNPFRVYRIFRNPREKNSGKLISLSQFLDLAKTYTSLSGVLISVENAAYLREKQGLDVVQAVLDTLTEAGYSNGTTTTKVMIQSTNSSVLVDFKKQSKYETVYKIEETIGNIRDSAIEDIKKFANAVVINKDSVFPNSDSFLTGQTNVVERLQKSQLPVYVELFRNEFVSQAYDFFSDATVEINAYIYGAGINGTITEFPFTAARYKRNRCLGREEVPPYMLPVNPGGLLNVMSPLSLPPAQAPNQDFIEADVTEPPLSPVIAKAPTSTPGTPSTIAQAPSGQTRLKLSLLLSVFFLSLLLL | Function: Hydrolyzes glycerolphosphoglycerol, glycerophosphocholine and glycerophosphoethanolamine in vitro.
Catalytic Activity: a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-glycerol 3-phosphate
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 83788
Sequence Length: 763
Subcellular Location: Cell membrane
EC: 3.1.4.46
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Q9SZ11 | MRGLLRASSLLLCGVILIQLLAAQIHAQSKKPKSPWPTLTGDPPLVIARGGFSGLFPDSSYDAYNFAILTSVPDAVLWCDVQLTKDALGICFPDLTMRNSSSIEAVYPTRQKSYPVNGVPTSGWFTIDFSLKDLKDVNLIRGILSRSEKFDGNSNPIMTVQSVSTQMKPSFFWLNVQHDAFYAQHNLSMSSFLVAASKTVLIDFISSPEVNFFKKIAGRFGRNGPSLVFRFLGQDEFEPTTNRTYGSILSNLTFVKTFASGILVPKSYILPLDDQQYLLPHTSLVQDAHKAGLEVFVSGFANDIDIAHDYSFDPVSEYLSFVDNGNFSVDGVLSDFPITASASLDCFSHVGRNATKQVDFLVITKDGASGDYPGCTDLAYKKAIKDGADVIDCSVQLSSDGTPFCLSSIDLGNSTTVSLTAFRNRSTTVPELGSLGAIYTFSLTWAEIQTLTPAISNPYRVTSLFRNPKQKNAGKLFSLSDFLSLAKNSTSLSGVLISVENAAYLREEQGLDVVKAVLDTLTQTGYSNSTATKVMIQSTNSSVLVDFKKQSQYETVYKVEENIRDILDSAIEDIKKFADAVVIQKLSVFPVAQSFITTQTNVVEKLQKSQLPVYVELFQNEFLSQPYDFFADATVEINSYITGAGINGTITEFPFTAARYKRNLCLGRKETIPYMAPAQPGALLTLVSPTAFPPAEAPNPVFTDADVTEPPLPPVTAKAPTSSPGTPSTNAQAPSGQTRITLSLLLSVFAMVLASLLLL | Function: Involved in primary cell wall organization. Required for the accumulation of crystalline cellulose.
Catalytic Activity: a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-glycerol 3-phosphate
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 82562
Sequence Length: 759
Subcellular Location: Cell membrane
EC: 3.1.4.46
|
F4JEQ1 | MACPRVIFLILITFFILQTAFSSSWQTLSGKPPAVIARGGFSGMFPDSSIQAYQLVNITTSPDVMLWCDLQLTKDGVGICFPNLKLDNGSNVIRIDPHYKERFSVDFTWKELSDVKLAQGVVSRPYIFDDVSSILAIEEVAKLTASGLWLNIQDSAFYAKHNLSMRNSVVSLSRRLKVNFISSPGISFLKSMKNSVKPTVTKLIFRFLKQEHIEPFTNQSYGSLAKNLSYIRTFSSGILVPKSYIWPVDSALYLQPHTSLVTDAHKEGLQVFASEFANDFVIAYNYSYDPTAEYLSFIDNGNFSVDGFLSDFPVTPYRAINCFSHVDPKRAKEQAKITIISKNGASGDFPGCTDLAYQRAASDGADILDCNVQMSKDKIPFCMSSFDLINSTNVIETSFRNLSSVVSEINPRRSGIYTFSLTMSQIQTLKPTISNLEKDSGLFRNPRNNKAGKFLTLSEFLFLPNRYSSLLGLLIEVENAAYLVEHQGISVVDAVLDELKRATTQQNKTSARTILIQSTDKSVLMKFKEKNKMNHDELVYRVDDNIRDVADSAIKDIKNFAGSIVISKKSVFPYKGFIILEKETNIASKLKSNGLRVYVERFSNECVTHAFDFYDDPTLEIDSFVRDVQIDGIITDFPATTARYRKNKCYGEFGLTTTGELITFANPMLLPPAEAPYPALLDSDVTEPPLPEARSQPPASSPSKAEEKAIEVPFAFIAMAILVCFFISV | Catalytic Activity: a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-glycerol 3-phosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 81360
Sequence Length: 729
Subcellular Location: Membrane
EC: 3.1.4.46
|
Q9FGT9 | MLRFFILFSLFLHSSVAAPKTPAAAAAVPAKKWLTLNGQEPAVVARGGFSGLFPESSISANDLAIGTSSPGFTMLCNLQMTKDGVGLCLSDIRLDNATTISSVFPKAQKTYKVNGQDLKGWFVIDYDADTIFNKVTLVQNIFSRPSIFDGQMSVSAVEDVLGTKPPKFWLSVQYDAFYMEHKLSPAEYLRSLRFRGINVISSPEIGFLKSIGMDAGRAKTKLIFEFKDPEAVEPTTNKKYSEIQQNLAAIKAFASGVLVPKDYIWPIDSAKYLKPATTFVADAHKAGLEVYASGFANDLRTSFNYSYDPSAEYLQFVDNGQFSVDGVITDFPPTASQSITCFSHQNGNLPKAGHALVITHNGASGDYPGCTDLAYQKAIDDGADIIDCSVQMSKDGIAFCHDAADLSASTTARTTFMSRATSVPEIQPTNGIFSFDLTWAEIQSVKPQIENPFTATGFQRNPANKNAGKFTTLADFLELGKAKAVTGVLINIQNAAYLASKKGLGVVDVVKSALTNSTLDKQSTQKVLIQSDDSSVLSSFEAVPPYTRVLSIDKEIGDAPKTSIEEIKKHADAVNLLRTSLITVSQSFATGKTNVVEEMHKANISVYVSVLRNEYIAIAFDYFSDPTIELATFIAGRGVDGVITEFPATATRYLRSPCSDLNKDQPYAILPADAGALLTVADKEAQLPAIPPNPPLDAKDVIDPPLPPVAKLASNGTEGGPPQTPPRSGTVAIAANLSLSLLAMMALGLLYTA | Catalytic Activity: a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-glycerol 3-phosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 80902
Sequence Length: 753
Subcellular Location: Membrane
EC: 3.1.4.46
|
P90795 | MSWVRFTKTGVAVVATSAAAVLALDMTNERRFQRQVKDHFRTVHADRLAELNKRAPSALPTRKDILTNLSKGEEFDVLIIGGGATGAGVALDAQTRGLKTALVELDDFSSGTSSRSTKLIHGGVRYLQAAIMKLDLEQYRMVKEALFERHNLLEIAPHLSSPLPIMLPIYKLWQVPYYWSGIKAYDFVSGKRVLKNSFFINKSQALERFPMLRNESLKGALIYYDGQHNDARMNLAIILTAIRHGAACANHVRVEKLNKDETGKVIGAHVRDMVTGGEWDIKAKAVINATGPFTDSIRLMGDPETARPICAPSSGVHITLPGYYSPSNTGLLDPDTSDGRVIFFLPWERMTIAGTTDAPSDVTLSPQPTDHDIEFILQEIRGYLSKDVSVRRGDVMSAWSGLRPLVRDPNKKDTKSLARNHIIEVGKSGLITIAGGKWTTYRHMAEETVDRVVEVHGLKTENGCVTPGLLLEGAHDWNSLQYIHLVQDYGMEVDVAQHLSNTYGDRAFVVARMCKMTGKRWPIVGQRLHPEFPYLDAEVRYAVREYACTAIDVIARRMRLAFLNTYAAHEVLPDVVRVMGQELGWSSAEQRAQLEKARTFIDMEMGQNAKQTAVSNVALNLTKEEMQRAKERFQQLDKDRKGHITVNDLRKHFREHNQKIDERVLHELLNEVDLNKNGEIEIAEFFQLYSGLKGGQLTGNRLVGYLDEIHGTPSVNRACGGI | Catalytic Activity: a quinone + sn-glycerol 3-phosphate = a quinol + dihydroxyacetone phosphate
Sequence Mass (Da): 80807
Sequence Length: 722
Pathway: Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route): step 1/1.
Subcellular Location: Mitochondrion
EC: 1.1.5.3
|
Q54QC1 | MNQLLSKSFKPLVVAGVAVIGISAFSGNRAYDEYRKERESISKKMINDLNENKITMFDYFQECKTLGRDEQLSKLNKLSKVYNKQKLNEQENQEELIDLDLIVIGGGATGTGVALDAQSRGMKVALFEKYDFSSGTSSKSTKLVHGGIRYLESAIMKLKPSELTLVKEALRERSNLLNNAPHLSRQLPIVIPAYSIFDASKFWIGCKLYDFFYPFNDIPKSYLQTSAQTYKEFPFLREGLVSSVVYYDGQHNDSRMNVSLALTAAQQGALTLNYTEVVELIKDDKINNNNKQQQLKGVVIRDRLTGKKYSVPAKCVVNATGPYCDSIRNLDDPRADPIITASSGVHIMLPGNLIPSDKGFLNPKTKDGRVLFILPFEGKTLVGTTDDPSPIIENPQPLEKDVEFILDSIKEYSNPNVKLDKSQVLACWSGIRPLVSDEPAAQGDNKKSTSQVTRSHSLRMSESGLITIVGGKWTTYRSMAEATVNLVCSKHDIFTPKGCITKNLPLIGGEKYYNTLNQYLIKNFNLPEDIAEHLAHSYGDQAPFVAKLANENGSNKRLVEGYPYIEAEVTYGVKKEYACTAEDIIGRRTRLSFLDHDKAEIALPKIINIMAPLLKWSNERKKEELKNSQNYLKTMTSK | Catalytic Activity: a quinone + sn-glycerol 3-phosphate = a quinol + dihydroxyacetone phosphate
Sequence Mass (Da): 71425
Sequence Length: 638
Pathway: Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route): step 1/1.
Subcellular Location: Mitochondrion
EC: 1.1.5.3
|
P43304 | MAFQKAVKGTILVGGGALATVLGLSQFAHYRRKQMNLAYVKAADCISEPVNREPPSREAQLLTLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLQKAIMKLDIEQYRMVKEALHERANLLEIAPHLSAPLPIMLPVYKWWQLPYYWVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYGAATANYMEVVSLLKKTDPQTGKVRVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKMDDKDAAAICQPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTDVTHHPIPSEEDINFILNEVRNYLSCDVEVRRGDVLAAWSGIRPLVTDPKSADTQSISRNHVVDISESGLITIAGGKWTTYRSMAEDTINAAVKTHNLKAGPSRTVGLFLQGGKDWSPTLYIRLVQDYGLESEVAQHLAATYGDKAFEVAKMASVTGKRWPIVGVRLVSEFPYIEAEVKYGIKEYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDYKKQEQLETARKFLYYEMGYKSRSEQLTDRSEISLLPSDIDRYKKRFHKFDADQKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMSAIQKGRVSGSRLAILMKTAEENLDRRVPIPVDRSCGGL | Function: Calcium-responsive mitochondrial glycerol-3-phosphate dehydrogenase which seems to be a key component of the pancreatic beta-cell glucose-sensing device.
Catalytic Activity: a quinone + sn-glycerol 3-phosphate = a quinol + dihydroxyacetone phosphate
Sequence Mass (Da): 80853
Sequence Length: 727
Pathway: Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route): step 1/1.
Subcellular Location: Mitochondrion
EC: 1.1.5.3
|
P32191 | MFSVTRRRAAGAAAAMATATGTLYWMTSQGDRPLVHNDPSYMVQFPTAAPPQVSRRDLLDRLAKTHQFDVLIIGGGATGTGCALDAATRGLNVALVEKGDFASGTSSKSTKMIHGGVRYLEKAFWEFSKAQLDLVIEALNERKHLINTAPHLCTVLPILIPIYSTWQVPYIYMGCKFYDFFAGSQNLKKSYLLSKSATVEKAPMLTTDNLKASLVYHDGSFNDSRLNATLAITAVENGATVLNYVEVQKLIKDPTSGKVIGAEARDVETNELVRINAKCVVNATGPYSDAILQMDRNPSGLPDSPLNDNSKIKSTFNQIAVMDPKMVIPSIGVHIVLPSFYCPKDMGLLDVRTSDGRVMFFLPWQGKVLAGTTDIPLKQVPENPMPTEADIQDILKELQHYIEFPVKREDVLSAWAGVRPLVRDPRTIPADGKKGSATQGVVRSHFLFTSDNGLITIAGGKWTTYRQMAEETVDKVVEVGGFHNLKPCHTRDIKLAGAEEWTQNYVALLAQNYHLSSKMSNYLVQNYGTRSSIICEFFKESMENKLPLSLADKENNVIYSSEENNLVNFDTFRYPFTIGELKYSMQYEYCRTPLDFLLRRTRFAFLDAKEALNAVHATVKVMGDEFNWSEKKRQWELEKTVNFIKTFGV | Catalytic Activity: a quinone + sn-glycerol 3-phosphate = a quinol + dihydroxyacetone phosphate
Sequence Mass (Da): 72389
Sequence Length: 649
Pathway: Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route): step 1/1.
Subcellular Location: Mitochondrion inner membrane
EC: 1.1.5.3
|
D5V0N9 | MIVVQVSDTHIKSKGKLAYNKVDIHKALYNCILHINNLKPKPDLVIFTGDITDNGTNEEYKLFKETVKLLDVPFYVIPGNHDNAENLKREFEEYDWFEENNHLSLVIEDFPIRIIGLDSSIKGKSYGGLSEERLLWLEKQLNKFPDKKVLLFIHHPPVKIGIEHMDVQNLQIGRERLADLLGKYEQVLALACGHVHRVSTTLWNKIIVLTAASPSHQVALDLRKDAKAEFVMEPPSVQLHYWTEEQGLTTHTSYIGKFEGPYPFYNEKGELID | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Catalyzes the hydrolysis of the 3'-5' phosphodiester bond of glycerophosphodiesters such as glycerophosphorylethanolamine (GPE), a typical phospholipid metabolite.
Catalytic Activity: a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 31373
Sequence Length: 273
EC: 3.1.4.46
|
Q6XBH1 | MLLAHISDTHFRSRGEKLYGFIDVNAANADVVSQLNALRERPDAVVVSGDIVNCGRPEEYQVARQILGSLNYPLYLIPGNHDDKALFLEYLQPLCPQLGSDANNMRCAVDDFATRLLFIDSSRAGTSKGWLTDETISWLEAQLFEGGDKPATIFMHHPPLPLGNAQMDPIACENGHRLLALVERFPSLTRIFCGHNHSLTMTQYRQALISTLPGTVHQVPYCHEDTRPYYDLSPASCLMHRQVGEQWVSYQHSLAHYAGPWLYDENISCPTEER | Cofactor: Binds 2 Fe(2+) ions per subunit . Active in the presence of various divalent cations such as Fe(2+), Zn(2+), Cd(2+), Co(2+) and Mn(2+) . Fe(2+) is probably the native metal ion .
Function: Catalyzes the hydrolysis of the 3'-5' phosphodiester bond of glycerophosphodiesters such as glycerophosphorylethanolamine (GPE), a typical phospholipid metabolite which is probably the natural substrate of the enzyme . In addition, exhibits a broad substrate specificity and can catalyze the hydrolysis of various phosphomonoesters, diesters, triesters and phosphothiolates . Preferentially hydrolyzes the phosphate diesters over the phosphonate monoesters . Can hydrolyze the model substrates p-nitrophenyl phosphate (pNPP), bis-(p-nitrophenyl phosphate) (bis(pNPP)) and ethyl p-nitrophenyl phosphate (EtpNPP) . Also exhibits activity towards some organophosphate pesticides and is capable of hydrolyzing a close analog of EA 2192, the most toxic and persistent degradation product of the nerve agent VX .
Catalytic Activity: a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 30840
Sequence Length: 274
EC: 3.1.4.46
|
Q8L1Z7 | MERTLVLIRHGQSEWNLKNLFTGWKDPGLTEKGRTEAIAAGKKLKETGLKFDIAYTSALQRAQKTAQNILEQMEQSDLELIKTPALNERNYGDLSGLNKDEVRQKWGEQQVQIWRRSYTIAPPNGESLRDTGARVWPYYLHHIQPHILRSQTVLIAAHGNSLRALIMALEGLNSEEIISQELATGIPIVYTFNSDSTISSKTIITP | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 23252
Sequence Length: 206
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.11
|
Q1LTL3 | MTLNKLVLIRHGESKWNNENRFTGWTDIDLSDQGRIEAKNAGQLLKQAGFIFDFAYTSVLKRAIHTLWYILDELDQAWLPVEKSWRLNERHYGALQGLNKKKITVEYGEEQVQQWRRSLNITPPELSDNDKRLPIYDIRYAKLSLDQLPKAESLAMTINRIIPYWKGEILPRINNGERVIIAAHGNSIRAIITLLDQLSENELIQLNIPTGVPIIYEFNSQIKTIKHYYLSIVNKDY | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 27619
Sequence Length: 237
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.11
|
Q6MJP3 | MYKLVLIRHGESVWNQENRFTGWQDVDLSEKGRAEALKGGKALREKGFSFDVAYTSVLKRAIKTLNFVLDEVDQVWLPVHKDWRLNERHYGALQGLNKAETAARHGEEQVKIWRRSYDTPPPPMEVSDPRHPSHDPRYKNVDAQLLPSNESLKDTVARFLPLWDGTIAPAVKSGKNVLIVAHGNSLRALMQHLEGMTPDEIMGVNMPTGIPMMYELDANLKVLKKEFIGDPDEVKAAIEAVANQGKAK | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 27958
Sequence Length: 248
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.11
|
Q492W5 | MHITKLVLIRHGESQWNKENRFTGWVDVDLSEKGRSEAQCAGRILKKNGFFFNYGYTSVLKRAIHTLWIILDQLDQAWLPIEKSWRLNERHYGALQGLNKDEAIKEYGYKTIQKWRRSFNVIPPNICGGNNQFIATNDNRYANISTDELPSSESLELTLKRVIPYWNQSIIPHIKKGQTIIIVAHGNSIRAIIKFLNHLNESEIFQINVPTGVPLIYEFDKKANTVQHYYLK | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 26998
Sequence Length: 232
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.11
|
O51602 | MYKLVLVRHGESEWNKENLFTGWTDVKLSDKGIDEAVEAGLLLKQEGYSFDIAFSSLLSRANDTLNIILRELGQSYISVKKTWRLNERHYGALQGLNKSETAAKYGEDKVLIWRRSYDVPPMSLDESDDRHPIKDPRYKHIPKRELPSTECLKDTVARVIPYWTDEIAKEVLEGKKVIVAAHGNSLRALVKYFDNLSEEDVLKLNIPTGIPLVYELDKDLNPIKHYYLGDESKIKKAMESVASQGKLK | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 28379
Sequence Length: 248
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.11
|
Q8TN93 | MSYLIIVRHGESGWNVDGRFGGWVDVPLTGKGIKEALLCAAELEGIDLDVTFTSKLIRAQETLFLILSKQKKIGVFVHEEAGTGEDRTEREDGSRKDRKEKRYAYPPNTEKNLIPIHSNEALNERYYGILQGKKKDKMKAKYGEEQILHWCRSFDEGPPEGESLKDIYRRAVPYFEKEIFPILQDGKNVIVCAHQNSLRALIKHIEGISNEDIRKIRLANARPVIYTFSGGRLVRENAETDPSVKRNL | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 28313
Sequence Length: 248
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.11
|
P30798 | MPTLVLSRHGQSEWNLENRFTGWWDVNLTEQGVQEATAGGKALAEKGFEFDIAFTSVLTRAIKTTNLILEAGKTLWVPTEKDWRLNERHYGGLTGLNKAETAAKHGEEQVHIWRRSYDVPPPPMEKGSKFDLSGDRRYDGVKIPETESLKDTVARVLPYWEERIAPELKAGKRVLIGAHGNSLRALVKHLSKLSDEEIVKFELPTGQPLVYELNDDLTPKDRYFLNER | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 25938
Sequence Length: 228
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.11
|
Q2S026 | MDSSKRHLLLILDGWGLADDPSVSAVEQADTPFVDHLYDEYPHGVLKASGLEVGLPDGQMGNSEVGHTNLGAGRVVYQEILRISKAIEDGSFFENDALVRAARHAKASDQKLHLMGCFSDGGVHSHLEHLYGLLELARREGLAPAQVNVHAFTDGRDTDPHGGVDYVEQFQKKADEIGVGRLASIVGRYYAMDRDERWARTERAYRLLTDGTGAAFDDPVTALKASYDDGVTDEFVEPRRIRADDADAFGDHGTRIEDGDAVVYYNFRSDRARQLTRAFTEADFDGFERERPDDLLFVTMSPYDDEFDLPVAFEKLNLEGTLGEVLSARGGRQLRAAETEKYAHVTYFFSGGREAPFDGEDRVLVPSPKVDTYDQQPEMSAPELADRVSRSLREADYTLAVLNFANPDMVGHTGDFEAAVAACEAVDRGARQVVEAARDQGYSVSIIADHGNADRLQNPDGSPHTAHTTALVPHIILKDGFEGPVRDGKLGDVAPTILTLLGEDVPDAMDGEVLVPAERAAAS | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 57178
Sequence Length: 523
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.12
|
Q9F1Y5 | MTTETTTATATAKIPAPATPYQEDIARYWNNEARPVNLRLGDVDGLYHHHYGIGPVDRAALGDPEHSEYEKKVIAELHRLESAQAEFLMDHLGQAGPDDTLVDAGCGRGGSMVMAHRRFGSRVEGVTLSAAQADFGNRRARELRIDDHVRSRVCNMLDTPFDKGAVTASWNNESTMYVDLHDLFSEHSRFLKVGGRYVTITGCWNPRYGQPSKWVSQINAHFECNIHSRREYLRAMADNRLVPHTIVDLTPDTLPYWELRATSSLVTGIEKAFIESYRDGSFQYVLIAADRV | Function: Catalyzes the SAM-dependent methylation of geranyl diphosphate (GPP) to yield (E)-2-methylgeranyl diphosphate (2-MeGPP).
Catalytic Activity: (2E)-geranyl diphosphate + S-adenosyl-L-methionine = (E)-2-methylgeranyl diphosphate + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32824
Sequence Length: 292
EC: 2.1.1.255
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Q58GE8 | MFKLAQRLPKSVSSLGSQLSKNAPNQLAAATTSQLINTPGIRHKSRSSAVPSSLSKSMYDHNEEMKAAMKYMDEIYPEVMGQIEKVPQYEEIKPILVRLREAIDYTVPYGKRFKGVHIVSHFKLLADPKFITPENVKLSGVLGWCAEIIQAYFCMLDDIMDDSDTRRGKPTWYKLPGIGLNAVTDVCLMEMFTFELLKRYFPKHPSYADIHEILRNLLFLTHMGQGYDFTFIDPVTRKINFNDFTEENYTKLCRYKIIFSTFHNTLELTSAMANVYDPKKIKQLDPVLMRIGMMHQSQNDFKDLYRDQGEVLKQAEKSVLGTDIKTGQLTWFAQKALSICNDRQRKIIMDNYGKEDNKNSEAVREVYEELDLKGKFMEFEEESFEWLKKEIPKINNGIPHKVFQDYTYGVFKRRPE | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Geranyl diphosphate synthase involved in pheromone biosynthesis.
Catalytic Activity: dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate
Sequence Mass (Da): 48324
Sequence Length: 416
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Pheromone biosynthesis.
EC: 2.5.1.1
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O05572 | MIPAVSLGDPQFTANVHDGIARITELINSELSQADEVMRDTVAHLVDAGGTPFRPLFTVLAAQLGSDPDGWEVTVAGAAIELMHLGTLCHDRVVDESDMSRKTPSDNTRWTNNFAILAGDYRFATASQLASRLDPEAFAVVAEAFAELITGQMRATRGPASHIDTIEHYLRVVHEKTGSLIAASGQLGAALSGAAEEQIRRVARLGRMIGAAFEISRDIIAISGDSATLSGADLGQAVHTLPMLYALREQTPDTSRLRELLAGPIHDDHVAEALTLLRCSPGIGKAKNVVAAYAAQAREELPYLPDRQPRRALATLIDHAISACD | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the addition of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranyl pyrophosphate (GPP) . Is probably involved in the biosynthesis of decaprenyl diphosphate, which is required for mycobacterial cell wall synthesis . Could be required for host endothelial-cell invasion and/or intracellular survival .
Catalytic Activity: dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate
Sequence Mass (Da): 34757
Sequence Length: 325
Domain: Contains two aspartate-rich motifs, designated as FARM (the first aspartate-rich motif) and SARM (the second aspartate-rich motif). Rv0989c contains arginine in place of the second Asp in its FARM and first Asp in its SARM. The primary role of the FARM and SARM is the chelation of the divalent magnesium ion cofactors that assist substrate binding and catalysis, but it may also play a role in determining product chain length.
Pathway: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.
EC: 2.5.1.1
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P32784 | MPAPKLTEKFASSKSTQKTTNYSSIEAKSVKTSADQAYIYQEPSATKKILYSIATWLLYNIFHCFFREIRGRGSFKVPQQGPVIFVAAPHANQFVDPVILMGEVKKSVNRRVSFLIAESSLKQPPIGFLASFFMAIGVVRPQDNLKPAEGTIRVDPTDYKRVIGHDTHFLTDCMPKGLIGLPKSMGFGEIQSIESDTSLTLRKEFKMAKPEIKTALLTGTTYKYAAKVDQSCVYHRVFEHLAHNNCIGIFPEGGSHDRTNLLPLKAGVAIMALGCMDKHPDVNVKIVPCGMNYFHPHKFRSRAVVEFGDPIEIPKELVAKYHNPETNRDAVKELLDTISKGLQSVTVTCSDYETLMVVQTIRRLYMTQFSTKLPLPLIVEMNRRMVKGYEFYRNDPKIADLTKDIMAYNAALRHYNLPDHLVEEAKVNFAKNLGLVFFRSIGLCILFSLAMPGIIMFSPVFILAKRISQEKARTALSKSTVKIKANDVIATWKILIGMGFAPLLYIFWSVLITYYLRHKPWNKIYVFSGSYISCVIVTYSALIVGDIGMDGFKSLRPLVLSLTSPKGLQKLQKDRRNLAERIIEVVNNFGSELFPDFDSAALREEFDVIDEEEEDRKTSELNRRKMLRKQKIKRQEKDSSSPIISQRDNHDAYEHHNQDSDGVSLVNSDNSLSNIPLFSSTFHRKSESSLASTSVAPSSSSEFEVENEILEEKNGLASKIAQAVLNKRIGENTAREEEEEEEEEEEEEEEEEEGKEGDA | Function: Dual substrate-specific glycerol-3-phosphate/dihydroxyacetone phosphate sn-1 acyltransferase, catalyzing the first and committed reaction in the de novo synthesis of glycerophospholipids and triacylglycerols (TAGs). Prefers Gly-3-P over dihydroxyacetone phosphate and has a marked preference for 16-carbon fatty acyl chains. Transfers a fatty acid from fatty acyl-CoA to the sn-1 position of glycerol-3-phosphate to produce lysophosphatidic acid (LysoPA). These lipids not only are precursors of glycerolipids, but also are dynamic components of signal transduction systems that control cell physiology . SCT1 is the primary supplier of diacylglycerols (DAG), used mainly in TAG synthesis and phosphatidylcholine (PC) synthesis through the CDP-choline pathway . Regulates fatty acid desaturation, that is, the ratio of unsaturated versus saturated fatty acyl chains, by competing with the desaturase OLE1 for the common substrate C16:0-CoA. Sequesters C16:0-CoA into lipids, thereby shielding it from desaturation by OLE1 .
Catalytic Activity: an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85694
Sequence Length: 759
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.15
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Q94B38 | MLSSIKPSSSSFSTAISGSVRRSIPTKLKFSPLLIIKNCHNQSFNANVVSHQKPLHISSASNFKREVKVEAYEADRSRPLDINIELPDEQSAQKLKIGIYFATWWALNVVFNIYNKKVLNAFPYPWLTSTLSLACGSLMMLVSWATRIADAPKTDLEFWKTLFPVAVAHTIGHVAATVSMSKVAVSFTHIIKSGEPAFSVLVSRFFMGETFPLPVYLSLLPIIGGCALAAITELNFNITGFMGAMISNLAFVFRNIFSKKGMKGKSVSGMNYYACLSMMSLVILTPFSIAVEGPQMWAAGWQNAVSQVGPNFVWWVVAQSVFYHLYNQVSYMSLDQISPLTFSIGNTMKRISVIVASIIIFHTPIQPVNALGAAIAIFGTFLYSQAKQ | Function: Glucose 6-phosphate (Glc6P) transporter . Transports also inorganic phosphate, 3-phosphoglycerate, triose phosphates and, to a leser extent, phosphoenolpyruvate . Responsible for the transport of Glc6P into plastids of heterotrophic tissues where it can be used as a carbon source for starch biosynthesis, as substrate for fatty acid biosynthesis or as substrate for NADPH generation via the oxidative pentose phosphate pathway (OPPP) . Required for dynamic acclimation of photosynthesis and partitioning of Glc6P between the chloroplast and the cytosol . May modulate the sensing of sugar status during early seedling development .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42754
Sequence Length: 388
Subcellular Location: Plastid
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P36148 | MSAPAADHNAAKPIPHVPQASRRYKNSYNGFVYNIHTWLYDVSVFLFNILFTIFFREIKVRGAYNVPEVGVPTILVCAPHANQFIDPALVMSQTRLLKTSAGKSRSRMPCFVTAESSFKKRFISFFGHAMGGIPVPRIQDNLKPVDENLEIYAPDLKNHPEIIKGRSKNPQTTPVNFTKRFSAKSLLGLPDYLSNAQIKEIPDDETIILSSPFRTSKSKVVELLTNGTNFKYAEKIDNTETFQSVFDHLHTKGCVGIFPEGGSHDRPSLLPIKAGVAIMALGAVAADPTMKVAVVPCGLHYFHRNKFRSRAVLEYGEPIVVDGKYGEMYKDSPRETVSKLLKKITNSLFSVTENAPDYDTLMVIQAARRLYQPVKVRLPLPAIVEINRRLLFGYSKFKDDPRIIHLKKLVYDYNRKLDSVGLKDHQVMQLKTTKLEALRCFVTLIVRLIKFSVFAILSLPGSILFTPIFIICRVYSEKKAKEGLKKSLVKIKGTDLLATWKLIVALILAPILYVTYSILLIILARKQHYCRIWVPSNNAFIQFVYFYALLVFTTYSSLKTGEIGVDLFKSLRPLFVSIVYPGKKIEEIQTTRKNLSLELTAVCNDLGPLVFPDYDKLATEIFSKRDGYDVSSDAESSISRMSVQSRSRSSSIHSIGSLASNALSRVNSRGSLTDIPIFSDAKQGQWKSEGETSEDEDEFDEKNPAIVQTARSSDLNKENSRNTNISSKIASLVRQKREHEKKE | Function: Dual substrate-specific glycerol-3-phosphate/dihydroxyacetone phosphate sn-1 acyltransferase, catalyzing the first and committed reaction in the de novo synthesis of glycerophospholipids and triacylglycerols (TAGs). Can use both Gly-3-P and dihydroxyacetone phosphate with similar efficiencies and has a broad fatty acyl-CoA specificity profile. Transfers a fatty acid from fatty acyl-CoA to the sn-1 position of glycerol-3-phosphate to produce lysophosphatidic acid (LysoPA). These lipids not only are precursors of glycerolipids, but also are dynamic components of signal transduction systems that control cell physiology.
PTM: Phosphorylatied at a conserved motif involving Ser-664, Ser-668 and Ser-671. This phosphorylation plays a critical role for efficient TAG mobilization. Phosphorylation deficiency at this motif increases the enzyme activity and consequently induces de novo formation of phosphatidic acid.
Location Topology: Multi-pass membrane protein
Catalytic Activity: an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA
Sequence Mass (Da): 83645
Sequence Length: 743
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
Subcellular Location: Lipid droplet
EC: 2.3.1.15
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A0A098CZ12 | MGKPDIYNSSANVEKSPYYKAMQHRAPNVLTAVDKKAHGMRRRILSQGLSDSSTRAFGNTIKKHIERLCQKIEGHSDPNTQWSESYDMARWFSYLTFDIMADVVFGQPYNLLGNSEYRYVVDSIEGSNIRTGVLIQAPEAYTWRLDKRLFPASIRHRNTFVKFISSLVQERLTTKPLERDDIISHLLTAKDSETGQGFTKNEVAAESSTLIVAGTDTSSTALAATLFYLTQYPNMYRRAVAEVRSSFAKSQDVKLGRALNECVFTRACIEESMRLSPPAASALWRRVQVGGQTVDGHAIQAGCNIGVCIYAIHHNELYYPDPFVFNPDRWLQNDKQAQSAFSPFSVGPRSCIGKGFAMAELMLAVATILVKFDIRRAPGDQGCIGQGHLEGEDGRRMVDEYQLHDHVTAFKQGPVLQFRRRDTVVQSEAE | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of gramillins A and B, bicyclic lipopeptides that induce cell death in maize leaves but not in wheat leaves . The nonribosomal peptide synthetase GRA1 incorporates respectively a glutamic adic (Glu), a leucine (Leu), a serine (Ser), a hydroxyglutamine (HOGln), a 2-amino decanoic acid, and 2 cysteins (CysB and CysA) (Probable). The biosynthesis of 2-amino decanoic acid incorporated in gramillins could be initiated by a fatty acid synthase composed of the alpha and beta subunits FGSG_00036 and FGSG_11656 (Probable). The cytochrome P450 monooxygenase FGSG_15680 could hydroxylate the fatty acid chain (Probable). Subsequent oxidation to the ketone by the oxidoreductase FGSG_00048 and transamination by aminotransferase FGSG_00049 could form 2-amino-decanoic acid (Probable). On the other hand, FGSG_15680 could also be responsible for the HO-modified glutamine at the gamma-position (Probable). Whether hydroxylation occurs on the fully assembled product or on the Gln residue prior to assembly into the gramillins requires further proof (Probable). The thioredoxin FGSG_00043 could also be required for the disulfide-bond formation between CysA and CysB (Probable). The specific involvement of the remaining proteins from the cluster is more difficult to discern, but could have broader regulatory (FGSG_00040 and FGSG_11657) or enzymatic functions (FGSG_00044 and FGSG_00045) (Probable). The final C-domain of GRA1 does not possess the expected sequence of a termination CT domain, often implicated in macrocyclization and release of a cyclopeptidein fungal NRPs; and the thioesterase FGSG_00047 may act in concert with the terminal C-domain of GRA1 to catalyze the formation of the macrocyclic anhydride and release of the products (Probable).
Sequence Mass (Da): 48265
Sequence Length: 430
Pathway: Mycotoxin biosynthesis.
EC: 1.-.-.-
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P12544 | MRNSYRFLASSLSVVVSLLLIPEDVCEKIIGGNEVTPHSRPYMVLLSLDRKTICAGALIAKDWVLTAAHCNLNKRSQVILGAHSITREEPTKQIMLVKKEFPYPCYDPATREGDLKLLQLMEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSASWSDTLREVNITIIDRKVCNDRNHYNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCEGVFRGVTSFGLENKCGDPRGPGVYILLSKKHLNWIIMTIKGAV | Function: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse . It cleaves after Lys or Arg . Once delivered into the target cell, acts by catalyzing cleavage of gasdermin-B (GSDMB), releasing the pore-forming moiety of GSDMB, thereby triggering pyroptosis and target cell death . Cleaves APEX1 after 'Lys-31' and destroys its oxidative repair activity . Cleaves the nucleosome assembly protein SET after 'Lys-189', which disrupts its nucleosome assembly activity and allows the SET complex to translocate into the nucleus to nick and degrade the DNA .
Catalytic Activity: Hydrolysis of proteins, including fibronectin, type IV collagen and nucleolin. Preferential cleavage: -Arg-|-Xaa-, -Lys-|-Xaa- >> -Phe-|-Xaa- in small molecule substrates.
Sequence Mass (Da): 28999
Sequence Length: 262
Subcellular Location: Secreted
EC: 3.4.21.78
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P11032 | MRNASGPRGPSLATLLFLLLIPEGGCERIIGGDTVVPHSRPYMALLKLSSNTICAGALIEKNWVLTAAHCNVGKRSKFILGAHSINKEPEQQILTVKKAFPYPCYDEYTREGDLQLVRLKKKATVNRNVAILHLPKKGDDVKPGTRCRVAGWGRFGNKSAPSETLREVNITVIDRKICNDEKHYNFHPVIGLNMICAGDLRGGKDSCNGDSGSPLLCDGILRGITSFGGEKCGDRRWPGVYTFLSDKHLNWIKKIMKGSV | Function: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse. It cleaves after Lys or Arg. Cleaves APEX1 after 'Lys-31' and destroys its oxidative repair activity. Cleaves the nucleosome assembly protein SET after 'Lys-189', which disrupts its nucleosome assembly activity and allows the SET complex to translocate into the nucleus to nick and degrade the DNA.
Catalytic Activity: Hydrolysis of proteins, including fibronectin, type IV collagen and nucleolin. Preferential cleavage: -Arg-|-Xaa-, -Lys-|-Xaa- >> -Phe-|-Xaa- in small molecule substrates.
Sequence Mass (Da): 28599
Sequence Length: 260
Subcellular Location: Secreted
EC: 3.4.21.78
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A1IIX2 | MNDMSHAPQPAQTKPHVRLVGRVAGVADLFRSSARQTEEARRVPASHIAALRGIGYFDIVKPRAFGGQGGEFAELVEANIELSAACASTGWVAGLLSAHQWLLAMFPEEAQADVWDENPDALLCGSYAPVKMAEAADGGYRLSGKWAFASGCENAQWSLCAAILPPQAKGRPVPAFLLVPASQYAIEDTWHVVGLAGTVSKTLVLDDVFVPKHRVLTFPDATSGHTPGGRFYAQEGLFNMPLLTGIPSCLASTGVGAAKGALAAYVDHVGGRVTRGAVAGGNNRMAEFPTIQLRVAEAAASVDAACEILLRDVARAQALSQARLEGRAEFSVDDRLLSRRGQSFSVSFSLRAVQALNDSTGGVGLDLSNPVQRAWRDANAVGRHISMNWDAVGTMIGQSMLGLEPKGQY | Function: Involved in the gamma-resorcylate (2,6-dihydroxybenzoate) catabolism . Oxygenase component of the resorcinol hydroxylase, which catalyzes the FADH(2)-dependent conversion of resorcinol to hydroxyquinol .
Catalytic Activity: FADH2 + O2 + resorcinol = benzene-1,2,4-triol + FAD + H(+) + H2O
Sequence Mass (Da): 43305
Sequence Length: 409
Pathway: Aromatic compound metabolism.
EC: 1.14.14.27
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P10144 | MQPILLLLAFLLLPRADAGEIIGGHEAKPHSRPYMAYLMIWDQKSLKRCGGFLIRDDFVLTAAHCWGSSINVTLGAHNIKEQEPTQQFIPVKRPIPHPAYNPKNFSNDIMLLQLERKAKRTRAVQPLRLPSNKAQVKPGQTCSVAGWGQTAPLGKHSHTLQEVKMTVQEDRKCESDLRHYYDSTIELCVGDPEIKKTSFKGDSGGPLVCNKVAQGIVSYGRNNGMPPRACTKVSSFVHWIKKTMKRY | Function: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse . It cleaves after Asp . Once delivered into the target cell, acts by catalyzing cleavage of gasdermin-E (GSDME), releasing the pore-forming moiety of GSDME, thereby triggering pyroptosis and target cell death . Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution. Cleaves caspase-3, -9 and -10 (CASP3, CASP9 and CASP10, respectively) to give rise to active enzymes mediating apoptosis . Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair (By similarity).
Catalytic Activity: Preferential cleavage: -Asp-|-Xaa- >> -Asn-|-Xaa- > -Met-|-Xaa-, -Ser-|-Xaa-.
Sequence Mass (Da): 27716
Sequence Length: 247
Subcellular Location: Secreted
EC: 3.4.21.79
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P04187 | MKILLLLLTLSLASRTKAGEIIGGHEVKPHSRPYMALLSIKDQQPEAICGGFLIREDFVLTAAHCEGSIINVTLGAHNIKEQEKTQQVIPMVKCIPHPDYNPKTFSNDIMLLKLKSKAKRTRAVRPLNLPRRNVNVKPGDVCYVAGWGRMAPMGKYSNTLQEVELTVQKDRECESYFKNRYNKTNQICAGDPKTKRASFRGDSGGPLVCKKVAAGIVSYGYKDGSPPRAFTKVSSFLSWIKKTMKSS | Function: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse . It cleaves after Asp . Once delivered into the target cell, acts by catalyzing cleavage of gasdermin-E (GSDME), releasing the pore-forming moiety of GSDME, thereby triggering pyroptosis and target cell death (By similarity). Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution (By similarity). Cleaves caspase-3 and -9 (CASP3 and CASP9, respectively) to give rise to active enzymes mediating apoptosis . Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair .
Catalytic Activity: Preferential cleavage: -Asp-|-Xaa- >> -Asn-|-Xaa- > -Met-|-Xaa-, -Ser-|-Xaa-.
Sequence Mass (Da): 27470
Sequence Length: 247
Subcellular Location: Secreted
EC: 3.4.21.79
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P18291 | MKLLLLLLSFSLAPKTEAGEIIGGHEAKPHSRPYMAYLQIMDEYSGSKKCGGFLIREDFVLTAAHCSGSKINVTLGAHNIKEQEKMQQIIPVVKIIPHPAYNSKTISNDIMLLKLKSKAKRSSAVKPLNLPRRNVKVKPGDVCYVAGWGKLGPMGKYSDTLQEVELTVQEDQKCESYLKNYFDKANEICAGDPKIKRASFRGDSGGPLVCKKVAAGIVSYGQNDGSTPRAFTKVSTFLSWIKKTMKKS | Function: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse (By similarity). It cleaves after Asp . Once delivered into the target cell, acts by catalyzing cleavage of gasdermin-E (GSDME), releasing the pore-forming moiety of GSDME, thereby triggering pyroptosis and target cell death (By similarity). Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution (By similarity). Cleaves caspase-3 and -9 (CASP3 and CASP9, respectively) to give rise to active enzymes mediating apoptosis . Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair (By similarity).
Catalytic Activity: Preferential cleavage: -Asp-|-Xaa- >> -Asn-|-Xaa- > -Met-|-Xaa-, -Ser-|-Xaa-.
Sequence Mass (Da): 27326
Sequence Length: 248
Subcellular Location: Secreted
EC: 3.4.21.79
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A1IIX3 | MDMKTTGDDGYFVEERSAETVIARMRDCDDPRLKEIMAVVTRKLHEAVKEIEPTEEEWMKAIHFLTEVGQICNEWRQEWILFSDILGVSMLVDAINHRKPSGASESTVLGPFHVADAPEMPMGANICLDGKGEDMLVTGRILDTDGVPVAGARIDVWQANDEGFYDVQQKGIQPDFNLRGVFVTGEDGRYWFRAAKPKYYPIPDDGPVGQLLRAMGRHPYRPAHLHYIVSAEGFTTLVTHIFDPDDPYIRSDAVFGVKESLLADFQRVEDAQRAQELGFANGWFWSVDHDFVLAR | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Involved in the gamma-resorcylate (2,6-dihydroxybenzoate) catabolism . Catalyzes the conversion of hydroxyquinol to malelylacetate .
Catalytic Activity: benzene-1,2,4-triol + O2 = 2 H(+) + maleylacetate
Sequence Mass (Da): 33350
Sequence Length: 295
Pathway: Aromatic compound metabolism.
EC: 1.13.11.37
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P08882 | MPPVLILLTLLLPLRAGAEEIIGGNEISPHSRPYMAYYEFLKVGGKKMFCGGFLVRDKFVLTAAHCKGSSMTVTLGAHNIKAKEETQQIIPVAKAIPHPDYNPDDRSNDIMLLKLVRNAKRTRAVRPLNLPRRNAHVKPGDECYVAGWGKVTPDGEFPKTLHEVKLTVQKDQVCESQFQSSYNRANEICVGDSKIKGASFEEDSGGPLVCKRAAAGIVSYGQTDGSAPQVFTRVLSFVSWIKKTMKHS | Function: This enzyme is probably necessary for target cell lysis in cell-mediated immune responses.
Sequence Mass (Da): 27311
Sequence Length: 248
Subcellular Location: Cytolytic granule
EC: 3.4.21.-
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A1IIX4 | MQPFVYTTAPARIVFGTGSSVGVAEEIRRLGLSRALVLSTPHQKGDAEALAARLGPLAAGVFSDAAMHTPVEVTKRAVEAYRAAGADCVVSLGGGSTTGLGKAIALRTDAPQIVIPTTYAGSEVTPILGQTENGVKTTLRGPEILPEVVIYDAELTLGLPVGISMTSGLNAMAHAAEALYARDRNPIASMMAVEGLRAMIEALPGVRMEPQDTKARETALYGAWLCGTVLGAVGMSLHHKLCHTLGGSLDLPHAETHAVLLPYTIAYVEQAVPDQLAPLAALVGGRAGTGLYDFAARLGAPASLAALGVGGEDLDAMAELATANPYWCPRPVEKTAIRALLQRAFEGARPE | Function: Involved in the gamma-resorcylate (2,6-dihydroxybenzoate) catabolism . Catalyzes the reduction of maleylacetate to 3-oxoadipate .
Catalytic Activity: 3-oxoadipate + NAD(+) = H(+) + maleylacetate + NADH
Sequence Mass (Da): 36406
Sequence Length: 351
Domain: Each subunit consists of two domains: an N-terminal NADH-binding domain adopting an alpha/beta structure and a C-terminal functional domain adopting an alpha-helical structure.
Pathway: Aromatic compound metabolism.
EC: 1.3.1.32
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Q4WID9 | MKRKAEKQQATAPVSAFAARKARQQQARLLEPEKTAQNEPAVEPPSKRARRSPEEGAARQAANENDRVQTRRSARTKAETLSSAELAEKQPQESAAAARAQTAERTPPPEKGDADTFDAAEEEEEEEKEEDILERENGVGVIAVEDDAEGYESPADDVPQVQNFPLSKTRLNKSNIVSSDERTLCVRIKEKMTLVLLGHYDLWVKRGVISLMGAKLHPSPRLYRVYAPSTHSLPVIKCVAGVDGESEIEVKSCNSGIYRLRHLSPLYQRIWNGKHTAADKLTLKKVSASTKRTFSVLYTSSDDSWNRHLRPLHLEKQWSSAIRSLSQRGGRLKVLICGPKASGKSTFSRYLLNHLLSPAPQTENNHRNTDGVAFLDLDPGQPEFCPMGQVYLAHLRSPFFGPPFTHPSLAESQDGSIIRSHHIGAISPKEDPDHYVLAAMDLMDRYRALLASYPQCPLIINYPGWIFGLGLEVATWLVKSLGLSDVVYMSEKGPAEVVEPLGHAAQEARVPLTTLPSQPTDFVSRSSAQLRSMQVQSYFHMSHPSEIHNPQWLDTTMSRTRPLVVDYAGPRQGIRGIMVMGSQISPNLLHEALDGALVGVVAVESPNAIMGQADAAGFSGSSHGDATQGAEDLSSAASDIDMNDVTDACHGDVAPTSSSSFESMIIRTPNEDLPYLFVGSGSCNPLDPKASNCLGLALVRSIDVPSRKLELITPIPASKLRDALEQGHGIVLVRGMLDNPSWAISEDYYAARAAERRHQELVAKARKETNTRDGQDAAVDADTQGMVSALLKDRIRRASNVPWMTVIEDNSRRHREAAQRKKSLWKLRKKAYPGSESETDW | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 92574
Sequence Length: 841
Subcellular Location: Nucleus
EC: 2.7.1.-
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Q59U11 | MSAFAALKNNPFGESIFNNTSNGDNHSRDDVEEDEVVQYIANSSDEDDDDDNDDNDNDQGNEDNNLFPLEISAPVDTSISSTPAPILNSRITQSNYTPNESNLKFSDNHVTITLNPSEYIIISGQCNLKIIKGSIKINQCHCLTSEDNKSYNIIALQSQSLPIISHYTTPEMEEDGVTSVSIIQLENSFSGIENISQIEPAFKNLISGQPNVEEPSLFKNYSFDIVLTETNGGYGLDINSYWINELNLLKSNKDDPTPKIIMIIGNKNTGKSTFCKSLINELLLTNPNRPVSYLEIDPGQSEYSTPCALSLSEIVQAQFGLAALPHKNNNIVKSRVEHYFGFTSAVNAPTRYVEIIEELFNHHQTKFSQRNHLIINTPGWVKGYGKELLNQITKIINPDKLILLSNNLNQEYPDNANILQDLTYQSLSIIPGVYQLSKYSAPQIRTINKLLYFHQTTTTGTFNFNDHLLDSSPLKISYACGNSPNNPGIYSTTIINHNIDNEFSHRDLCSLVEVSIYGIYSIKSNGNTKFDEMSCFRRDDGNSPFYLNPDDFDNLLSNETITSKFIGLIMVHSINPNDHYMNIYAPDIIINRLRKVLSTNSNQTNDYKLIMIRGEGDIPNCEMLYPEFINKKIDYLKSIKKRKAATTSRKLVDLKLPYISFETKSKVGGIWKVRKNIKRRGHHQKG | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 77356
Sequence Length: 686
Subcellular Location: Nucleus
EC: 2.7.1.-
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Q6FW56 | MAETDLNALAYKDSDSTDTSSSSSSDEEYQAEVKVSNQNEKQVDYDSDTDLNTDNKVSSVDAYKPCVGENLIIRDSNIIILLRAKEKLCLSGLFDLKIEKGGLLYNDIHFNASSKTYHYWHPLSNSIPEIKSSFYAGFEDVDISAFYAAYDISPNNDYETVLKISNHKSKSLIDGEILMPSLKSLWITKEDFLQKNGYTNFSFDIIMPATLQEITTLNISKSWTNCLQKLKFINQNSIHDTRIMVIGGKNSGKSTFLRSLVEKVLYSHDISDKSVSEMLYLDLDPGQPEFSHPDCISMTRLTSNDMNFGQSFGQASPEVLKQYYIGSPSPQEYPTRYLNMVNKLITEFEDTMFAGISCINLPGWVKGFGLNILQKVLEIYKPTDIVYLESPSTVRHFSELRIPKSFSSTMMTEYSPRSYRIPAEFSNAAINNSPEIKFAPSDIRTYKLLCLFHRSDTSNVPTFDFRPLIAKSPKKISYGRAGIHTIIINIEFALVPSHELIQALEGTIVAIYHEENTDDEHDSSSDIRVLSNDDLETAKFITLGLVHSVDEERKYFNIYVPENMVATLKNLGNRFMIERLSTETPFCELSPPNKVLKTDQTSPFISFKTRKKYEHVWKIRKNIKRKGHHL | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 71688
Sequence Length: 630
Subcellular Location: Nucleus
EC: 2.7.1.-
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P0CM79 | MSALAARRATAAAASPKPEQPESSIEEVSVSGALTLPSPKRRKTRQTSPKPRSKARYSDDVPTSRQFFQATESLAEQRTGRFSPSAPDSDGGTSSSSVGDSDEDMAQEDEFEDRREVDGERDQRKVSVAANMSSSGPFKSLDLMPVDITSQFNPKDNVNFCRITEGQLASAEMNDGHPGPGVIVSLARNESLTIAGLFLLTPLQNTLSIYSTALSPSMSSFPVYAPTSHPLPVISPASTQAPGKESDKTLLLIRENRCGIDGLRNGAVPGFSNIWLEDNGPWGLRGVHPVVGSFPVPVYPYCTPPSWSHAISSLSSSDVNLQTPFVGLVKGPKRSGKSTFARALLNNLLRRFRKVAWLECDLGQGEFGSGAVVGLWILDKPALGPPFTHPLLPSRSHYLGTYTPLTCPDEYLVAIRHLIEHYKYELQYTSEYSALHTTVHDKISTHVPLVINTQGWMKGLGEELLNVIESMAQPTRVFSFESQSEEVYSGQGWTSTPPWQATQLPYDPAYPTTEPVETEVTQTYSLETAPVSALQARYTPADLRVLSAITYFHASLHPTQSVPVTWDISSPLVCTIPWEVELGIGKALEKVYLIGEGSEGVLEEDLPIALNGAIVALAEMLGSYEDEPTVYEQGRSPPPTDLVNILGLAVIRSLSSGNSVNPGLKLQLLTPLPPSYLSRARILIKSGALELPLPGMIDWRRGGINEEGMLGKGWEEIPFLDVGGLDVIGGERRRFRKNIMRKGM | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 81009
Sequence Length: 744
Subcellular Location: Nucleus
EC: 2.7.1.-
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Q6BQV7 | MSAYAALQKMSGASSILYGINGESDNDESGTIGYLRNSSDEEVEAEEAEVPTTSTMAPTPNIIRTPSIVPKINSFICESNFIPNDDNFIVFHDHIIIGLKANEYILINGQSKMTIQRGAILINTGHYMFAHPNNCIPIIASQSQSLPIISSTQVVDRSGIKDSKTDENMHLFSSNYKSIIKLENLYTGLEKIGTYHPPFKRLFYSHAVIEDEDLTEYERLFKTYSFEIILRDRGCIGISIEKLWLNQIQLLISDIHEDLIPKTIMIIGNKNSGKSTLSKTLLNSLILANQNTVSYLDLDPGQSEFSMPYCLSLTNHSKPIIGMNVPKVSGDEDSVSHYYGFTTPQSQPSQYVSIIKALFREYDQVYRPRGHHLIINTPGWIKGYGKELLNELTAFINPNQLILLSNNTDNDNMDNSDNLSGLTFQNSRCFQGIYQTSKYSPFQLRMYNKLSYFHQVDTLKFDFNSHILLRSPLKLSYETVNSSKDFKGINMVSVLNYDTGLNFELNDLLSMIDTSIMGLYLIDHEYYSSLKASLKKSEDCDYLPQYLNSTDYVNLINYSSSNNIFMGLCMVHSINTKDEFFNIYLPGHNQHRLTEMITKRDYKMLLVKGDGDIPSPDLLMFDMLLKQQEDLKRLNKKRKKNPNVDDKDVLKIPYVTFENKNKIGGIWKTRRNVMRRSHQR | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 77674
Sequence Length: 680
Subcellular Location: Nucleus
EC: 2.7.1.-
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Q5B4D1 | MMKRKADRQTAAAAPVSAFAARKARLQQTQTQVQTVVASEKTTHTDVAAEPPSKRPRRSLQESQAQSTSEEDTKRTSKRSAAKTEKVQRVDSGTITRTRETRMKDSEIEVEDLEKERSSNEESEGEDAVEENAAGVVAVPAAEDGYESPADNTMTVVFPLSKIRLNKNNIVYSDEDTLCVRIQEKLSIVLIGQYDLWVKRGVVSVMGAKLHPSPRVYRVYAPSTHSLPVIKCVTGVNGAAEVEFKSCHSGITRLRDLSPLYQRLWNSGNTPADKLSLKAVGQDARRTFSVLHTSADDPLKRHLRPLHLEKQWSAAIKVLSQRAGRLQVLICGPKASGKSTFGRYLLNHLLSPAPQPELNYTNTDGVAFLDLDPGQPEFLPMGQVYLAHLRSPVFGPPFTHPSLNNEREGTIIRAHHIGATSPKEDPDHYVLAAANLMEQYRTLLATYPQCPLIINYPGWIFGLGLEVATYLIQSLGLSDVVYMSEKGPTEVVEPLSQAASLARVSLTILPSQPTEFVSRSSAQLRSMQMQSYFHMAQPAGVSHPTWLENPVSKNRPFRVRYAGENRGVHGVMTLDSQIIPDLLCESLEGALVGVVAIESPNALPIPSSNAPPANEEEATSNADDDVDMENETEHNRNATISHLTTLTISTKESLPYITSGPGTSTPLHPSSSSMLGLALIRSINPDTQTLDLVTPIPSTRLIQSLERGHALVLVRGVLDNPNWAVAEEYYAARAEERRVRRGIRGRKEAGVGEQGDESVEQRLLGLLKERIRRAKDVPFMTVVEDHGRRKQEEAAQRALWKLRKKAGIESEDEVGY | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 89980
Sequence Length: 816
Subcellular Location: Nucleus
EC: 2.7.1.-
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Q4IR18 | MSSNKKRRIDEKPMSALSALQARRREAAASPVQTTQTGSESDEKSVTTSVNPYQLLRKDSSQSTAPKTPKKNVVKDQYLPRGAESPASRSRGVVIASGNTDTLNPELAGASQKVVREYSSFRLSKQNHRVKTGGVVELNLSNSERFLVLGSFGIRVIQGEVSLAGATLYPSETIEWVHAPHCHAVPMLRTIDETILELHPDRNARGIRQLGRLSPLFRKIWNESPETNSSKTSKESTFEIIYTSEDAPKKCIIQKLVSPPEWNKKLSSLVATSRKKPSLSTLICGPKSAGKSTFSRLFLNGLLTDRSQKQGARSVVILDLDPGQPEYAPPGTLSLVFVTKPNLGTPFTHPSLKNSAFTVVRSHSMASATPAPNPDLYLACATDLFDTYSKHYSGAPLIVNTPGWIQGTGLDLLSSLIEKIKPQEVLYMSEAGPDEAVNALRAATKLMFTELPSQPSEFTSRTAAHLRAMQTMSYFHLQNTALKTSNLLDTSTRLKWDASPLSSRAPLLVQYSSSKRGVLGLLSYDYQCSPELLADTVNGLVLAAVEIEDRKAFSNFPQEVAPPPLVSTSPENIPFIPNYDDVALDPRYSRTIGLVLLRGIDTKSETLQLVTPIPLEEFRSIKSQGRSIVLLHGKFDTPNWAYTEELYERAGTEEGNDMVLEVTEEDTEDDQSGVEPEGADGVSDLTEVPWVEVLKGSQRRPVGSQVWRPLRHLGRNNTGD | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 79096
Sequence Length: 720
Subcellular Location: Nucleus
EC: 2.7.1.-
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Q6CQ06 | MSEDILTYTANTDSDDSDVEQREIEKKYKTSSETPVVQLYDGDDYDNDDIRETNGNDFPNEEDESNQLYSPVVDMNFFTLSDECTEVIICLEKNQHLLICGQFNLQIIKGGITYNNVHYNSGYKNWEFWHPACNAISPIVSSFYAGWESKLFLNREYQHFTTQIESYDCVLKISNGCNITELSSLLPELRDMWGPLNISLLPGIARKQLTFNIISKISDSVRILDISTEWSTVIDEMRIFHANSSQDMRVMVIGGKNSGKSTLMRLLVQKFLHSNNDLSYEAIHYLDIDPGQPEYSPPESISWNKVDPKSMSLGQHLCQGRFTTIKQHFIGSSSPQDWPETYSNAVESLLKEWQTENFMGTSFLNIPGWIKGFGVKIINHALDHFKPTHIIFLSYNGLPFSSEIKVPDAFSTTQRSTYKPIILQLHSPAVGKHISHALQRFNAAKIRQFKITAYLHKKYDRNFVINPLVMQKPQLTSIGNRGIVGFEFLQYSNSSLYHDDIKLSLDGTVVALHRADSTPDVLFKGIFPVMKNYSKINTEFVGLALIHSIDLEQSLIYMYIPENLFRALRETENKWVLVRGKTETPICELYPNNGIFKSEVDIPYVSLYQKKRHEHVWKVRKNVMRRGHHMK | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 72566
Sequence Length: 631
Subcellular Location: Nucleus
EC: 2.7.1.-
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Q9UU96 | MVKRQRIESSNVPLSAFAVRQLTLSKAARKKDNSSGKKRSVSEEESQDKYEDEMKTEGEFPSYKHTLVQVVVPGVDHRTKLHSESSKNDSEITPDINRSKVNPQEYSEFSVASPQTISPSLPLNLDDETVSENVPHSPQSSNDAIPVIKITEENSFRVKDTLYVGLHKDQKLAMVGTFIFRSVRGKFQLFGATYSSACMSWFPLNAPLAFATPVFSAIDNALPAMQISEYEEDSLNLRSFAVPSYSPKEHEYELEPKDILPNFETVIAFRENENGLSKIARVLPFAKRLFSFKNLLQDASSISNNFEITPESWCSFSNQLLFSTSKSDYVVPRLMVCGPKGSGKSSFSRYITNRLLQQYRHIAYLDLDPGQPEVVPSGHISLYYINSPLQGPVFARMLFPTYMLRLHLGDISPQKDPDHYIACVTRLFAEYKDYIFNQEISQKEIIPLIINCPGWIRGGGAELLSSIVDICQPTEVVYMSREDMKSSHREKKSIYQHKEYMPDFLSSRDEFQLTLLESTWQYLPDPNVNKVTSADNRMLGLLSYLYFNCNLQRWDFTTSLTACQPIATAFKGSSKGIDAVNIIGEPLNVNDVAKTINGTLMALYACDTASLDNSNTQRIVSSPEGIPLIINDGLPLDPNTSHCLGLIVLRTIDLKRNEFHFVGPLNLELIKDAYAKSLKIVLERGRLELPVYAMLDHRLAQYSELPYLDRNHDRVAVGAHRRRVRRNIIRRSTFVG | Function: Polynucleotide 5'-kinase required for both rRNA processing and heterochromatic gene silencing.
Sequence Mass (Da): 83251
Sequence Length: 736
Subcellular Location: Nucleus
EC: 2.7.1.-
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Q6C5P9 | MTKRKSALSALKPTKKQVISSEDSDPEVVVVTNPPLDSPDAEESFISITEEDEAVRQLSTFDFSAKNTKVVRDETRGRSRVFHGMKFKETIVLRGAYVVTVWSGVIHINGALVNINSPVDIPVFAPASHALPQIEAAAGAPETRESGDEDVMEALHQLEGSSVIVEIAAMPRRSENPLITVSNFGKMSSGNIVPFVRQLWHCSEDDGSNYSRIYNTASVVTKSQAAVIPGIYDEWAEVCDDIRRLKHSSTMVVGSQNTGKSTFCKYLSAFMTTKKTGTSVAFVDLDPSNCEFTAPGQVSVTVIGAGHLSPYSILGPSFTHVTAPTYSRFVGYNNPKDDTRGYIEACKAVIDFAKGLKLPLVFNTCGWVRAAGHDLLRQLIDHVKPSDVVFTRDPGVDADQARLAESVKARSHVLDAPDAEPPRFTGAEQHSLQTVTYLHGGNLASHLSDLPALEVGLESVYVGILDSEGVDLADVALSTNSTLLAVMTMDKKTVKHAEITPDGLQYLPNFDIPQGECLGQAMVQFAGASVRLHTPVSASLLNAQLAADKAIVLVRGRIPLPVYELWDSRKGGEQAYVSFDVNSGVGSEAWVARRGLKRK | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 64810
Sequence Length: 599
Subcellular Location: Nucleus
EC: 2.7.1.-
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Q07845 | MVIDSKQDLPQYTKDSGSESDSDSSNNFIVESPSIPSSKSATVVLNSEEYEDDEGDDLNGLDAELIDNITYEGDEDETMFVGLKEKQKLHLSGVFRLQVVKGGIVYNNVHYNASREILTFWHPLSQSIPTIDFSHFAGWQDTFFMPRNNRFKIRDEEFKSFPCVLRVFNSNHTGLLEAGHLYRDVNYLWKPKEPYFPLNERTTYHLLHESDRIQSLSVPGYWSTPLEKLYLSHKNAAYDTRIMVIGGKNSGKSTFLRLLLEKFTQDIRDSTTSQEELVYLDLDPGQPEYSLPDSISLNKILSSPISLGQHLCQGSNFQTLLQFYAGSSSPQDEPTSYLNCADKLIDHLEEQAFFGTSLLNLPGWIKGFGMQILNHIIRKYKPTHLLFLETANSKRHLDELTIPQSFSTSLRDAYAPEVVRVPAHSLNHTLSSRFHASQLRTFKILALFHKITQFDYDFAPLLKSAPLQISYGKGKSGIKGIQFPMEFQDLNPQDIKSALEGTVIGIYTYSGEDSLEVKSLNTFPILQSCTSSSKNFITLGLIHSIDTSQQIMNIYVPPCHTQILDKQPEDAQWIIVRNKTETPFCDFLPSPRTITWDDNIQIPFATFERRKKLEHVWKVRKNVMRRGQFMKR | Function: Polynucleotide 5'-kinase involved in rRNA processing. Required for the efficient termination by RNA polymerase I and the processing of the IST2 pre-rRNA internal transcribed spacer localized between the 5.8S and 25S rRNAs. May act by maintaining the phosphorylated status of the downstream RNT1 cleavage product, which in turn allows the torpedo activity of RAT1 to efficiently terminate Pol I transcription. In vitro, displays polynucleotide kinase activity on both single- and double-stranded RNA and on single-stranded DNA alone, but not double-stranded DNA alone.
Sequence Mass (Da): 72258
Sequence Length: 632
Subcellular Location: Nucleus
EC: 2.7.1.-
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Q47878 | MSDIKQMIGKTFMEIADAIETGSFAGKVKVGITTLGSEHGVENLVKGAELAAKDAAGFDIVLIGPKVETSLEVVEVATEEEAHKKMEELLDSGYIHSCVTVHYNFPIGVSTVGRVVTPGMGKEMFIATTTGTSAAQRVEAMVRNALYGIITAKSMGIENPTVGILNLDGARAVERALKELAGNGYPITFAESLRADGGSVMRGNDLLGGAADVMVTDSLTGNIMMKVFSSYTTGGSYEGLGYGYGPGIGDGYNRTILILSRASGVPVAANAIKYAAKLAQNNVKAIAAAEFKAAKAAGLESILAGLSKDTKKASTEEEVKMPPKEVVTGTISGVDVMDLEDAQKVLWKAGIYAESGMGCTGPIVMVNEAKVEEAAKILKDAGIVA | Function: In the first step of glycine, betaine and sarcosine reductases, the substrate is bound to component PB via a Schiff base intermediate. Then the PB-activated substrate is nucleophilically attacked by the selenol anion of component PA to transform it to a carboxymethylated selenoether and the respective amine. By action of component PC, acetyl phosphate is formed, leaving component PA in its oxidized state. Finally component PA becomes reduced by the thioredoxin system to start a new catalytic cycle of reductive deamination.
Catalytic Activity: [thioredoxin]-disulfide + acetyl phosphate + H2O + NH4(+) = [thioredoxin]-dithiol + glycine + H(+) + phosphate
Sequence Mass (Da): 40054
Sequence Length: 385
EC: 1.21.4.2
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Q9R4G7 | MRLEIGNIFIKDIQFGEQTKVENGVLYVNKDEMIKKLSVIEHIKSVDLDIARPGESVRITPVKDVIEPRVKVEGPGGIFPGVISKVETDGSGRTHVLKGAAVVTTGKVVGFQEGIVDMSGVGAEYTPFSKTLNLVVIAEPEDGIEQHRHEEVLRMVGLNAGVYIGEAGRSVTPDEVKVYETDTIFEGAAKYPNLPKVGYVYMLQTQGLLHDTYVYGVDAKKIVPTILYPTEVMDGAILSGNCVSSCDKNPTYVHCNNPMVEELYAMHGKEINFVGVIITNENVYLADKERSSDWTAKLCKFLGLDGAIVSQEGFGNPDTDLIMNCKKIEMEGVKTVISTDEYAGRDGASQSLADADVRANAVVSNGNANMVIVLPPMDKTIGHIQYIDTIAGGFDGSLRADGSIEVEIQAITGATNELGFGYLSAKGY | Function: In the first step of glycine reductase, the substrate is bound to component PB via a Schiff base intermediate. Then the PB-activated substrate is nucleophilically attacked by the selenol anion of component PA to transform it to a carboxymethylated selenoether and the respective amine. By action of component PC, acetyl phosphate is formed, leaving component PA in its oxidized state. Finally component PA becomes reduced by the thioredoxin system to start a new catalytic cycle of reductive deamination.
PTM: The peptide chain is cleaved into beta and alpha chains, and the alpha chain N-terminal cysteine is deaminated and oxidized to form a reactive pyruvoyl group.
Catalytic Activity: [thioredoxin]-disulfide + acetyl phosphate + H2O + NH4(+) = [thioredoxin]-dithiol + glycine + H(+) + phosphate
Sequence Mass (Da): 46263
Sequence Length: 428
EC: 1.21.4.2
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O86186 | MKKLKVVHYINNFFAGVGGEEKANIPPEMREGAVGPGMALAAALGDEAEVVATVICGDSYYGENMDSARKEILEMIKDAQPDAFVAGPAFNAGRYGVACGSIAKAVEEDLGIPSVTGMYVENPGVDMYRKDIQIIETGNSAADLRNSMPKLAKLVMKKAKGELVGPPEVEGYHMMGIRTNFFHEKRGSERAIDMLVNKLNGEKFETEYPMPVFDRVPPNPAVKDMSKVKVAIVTSGGIVPHDNPDRIESSSATRYGIYDITGMDSMSADDFTSIHGGYDRAFVVKDPNLVVPLDVMRDLEREGVIGELANYFVSTTGTGTSVGNAKGFGESFSKKLIEDGVGAVILTSTUGTCTRCGATMVKEIERAGIPVVHLATVVPISLTIGANRIVPAIGIPHPLGDPALDAKGDKKLRRELVMRGLKALQTEVDEQTVFEG | Function: In the first step of sarcosine reductase, the substrate is bound to component PB via a Schiff base intermediate. Then the PB-activated substrate is nucleophilically attacked by the selenol anion of component PA to transform it to a carboxymethylated selenoether and the respective amine. By action of component PC, acetyl phosphate is formed, leaving component PA in its oxidized state. Finally component PA becomes reduced by the thioredoxin system to start a new catalytic cycle of reductive deamination.
Catalytic Activity: [thioredoxin]-disulfide + acetyl phosphate + H2O + methylamine = [thioredoxin]-dithiol + H(+) + phosphate + sarcosine
Sequence Mass (Da): 46779
Sequence Length: 436
EC: 1.21.4.3
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O69406 | MKLELGNFYVEEIVFGEKTSFKDGVLTINKQEALDYVMEDENITHAELHIVKPGDMVRLCPVKEAIEPRIKLDGRTYFPGVTDEELTRCGEGRTHALKGCSVLVVGKHWGGFQDGLIDMGGEGAKYTYYSTLKNIVLVGDTNEDFEKNEQQKKNKALRWAGHKLAEYIGKTVKDMEPQEVETYELEPVTQRSEEVTKLPGVVFVMQPQSQMEELGYNDMVYGWDMNRMVPTYMHPNEVLDGAIISGSFMPCSSKWSTYDFQNFPALKRLYAEHGKTVNFLGVIMSNLNVALQQKQRSALFVAQMAKSLGAQGAIVAEEGYGNPDADFIACIVALENEGIKTVGLTNECTGRDGFSQPLVTLDEKANAIVSCGNVSELVELPPMPVVLGELEALARDGLSGGWAGDEILGSSVKADGSVIMENNAMFCGDQVVGWSTKTMKEF | Function: In the first step of betaine reductase, the substrate is bound to component PB via a Schiff base intermediate. Then the PB-activated substrate is nucleophilically attacked by the selenol anion of component PA to transform it to a carboxymethylated selenoether and the respective amine. By action of component PC, acetyl phosphate is formed, leaving component PA in its oxidized state. Finally component PA becomes reduced by the thioredoxin system to start a new catalytic cycle of reductive deamination.
Catalytic Activity: [thioredoxin]-disulfide + acetyl phosphate + H2O + trimethylamine = [thioredoxin]-dithiol + glycine betaine + H(+) + phosphate
Sequence Mass (Da): 48765
Sequence Length: 442
EC: 1.21.4.4
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Q12068 | MSVFVSGANGFIAQHIVDLLLKEDYKVIGSARSQEKAENLTEAFGNNPKFSMEVVPDISKLDAFDHVFQKHGKDIKIVLHTASPFCFDITDSERDLLIPAVNGVKGILHSIKKYAADSVERVVLTSSYAAVFDMAKENDKSLTFNEESWNPATWESCQSDPVNAYCGSKKFAEKAAWEFLEENRDSVKFELTAVNPVYVFGPQMFDKDVKKHLNTSCELVNSLMHLSPEDKIPELFGGYIDVRDVAKAHLVAFQKRETIGQRLIVSEARFTMQDVLDILNEDFPVLKGNIPVGKPGSGATHNTLGATLDNKKSKKLLGFKFRNLKETIDDTASQILKFEGRI | Function: Catalyzes the irreversible reduction of the cytotoxic compound methylglyoxal (MG, 2-oxopropanal) to (S)-lactaldehyde as an alternative to detoxification of MG by glyoxalase I GLO1. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation. Also catalyzes the reduction of 3-methylbutanal to 3-methylbutanol. Acts as a suppressor of 3-methylbutanol-induced filamentation by modulating the levels of 3-methylbutanal, the signal to which cells respond by filamentation. Also involved in ergosterol metabolism.
PTM: The N-terminus is blocked.
Catalytic Activity: (S)-lactaldehyde + NADP(+) = H(+) + methylglyoxal + NADPH
Sequence Mass (Da): 38170
Sequence Length: 342
Subcellular Location: Cytoplasm
EC: 1.1.1.283
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P19493 | MRIICRQIVLLFSGFWGLAMGAFPSSVQIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVENFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDFNTPMVTKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQDMPTLGNDTAAIENRTVVVTTIMESPYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDADTKIWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEPEDGKEGPSDQPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFTRTTAEGVARVRKSKGKFAFLLESTMNEYTEQRKPCDTMKVGGNLDSKGYGVATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKLTFSEATRNKARLSITGSVGENGRVLTPDCPKAVHTGTAIRQSSGLAVIASDLP | Function: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate (By similarity).
PTM: Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-611 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-837 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 100758
Sequence Length: 902
Domain: The M4 transmembrane segment mediates tetramerization and is required for cell surface expression.
Subcellular Location: Cell membrane
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Q61627 | MEALTLWLLPWICQCVTVRADSIIHIGAIFEENAAKDDRVFQLAVSDLSLNDDILQSEKITYSIKVIEANNPFQAVQEACDLMTQGILALVTSTGCASANALQSLTDAMHIPHLFVQRNPGGSPRTACHLNPSPDGEAYTLASRPPVRLNDVMLRLVTELRWQKFVMFYDSEYDIRGLQSFLDQASRLGLDVSLQKVDKNISHVFTSLFTTMKTEELNRYRDTLRRAILLLSPQGAHSFINEAVETNLASKDSHWVFVNEEISDPEILDLVHSALGRMTVVRQIFPSAKDNQKCMRNNHRISSLLCDPQEGYLQMLQISNLYLYDSVLMLANAFHRKLEDRKWHSMASLNCIRKSTKPWNGGRSMLDTIKKGHITGLTGVMEFREDSSNPYVQFEILGTTYSETFGKDMRKLATWDSEKGLNGSLQERPMGSRLQGLTLKVVTVLEEPFVMVAENILGQPKRYKGFSIDVLDALAKALGFKYEIYQAPDGRYGHQLHNTSWNGMIGELISKRADLAISAITITPERESVVDFSKRYMDYSVGILIKKPEEKISIFSLFAPFDFAVWACIAAAIPVVGVLIFVLNRIQAVRSQSATQPRPSASATLHSAIWIVYGAFVQQGGESSVNSVAMRIVMGSWWLFTLIVCSSYTANLAAFLTVSRMDNPIRTFQDLSKQLEMSYGTVRDSAVYEYFRAKGTNPLEQDSTFAELWRTISKNGGADNCVSNPSEGIRKAKKGNYAFLWDVAVVEYAALTDDDCSVTVIGNSISSKGYGIALQHGSPYRDLFSQRILELQDTGDLDVLKQKWWPHTGRCDLTSHSSTQTEGKSLKLHSFAGVFCILAIGLLLACLVAALELWWNSNRCHQETPKEDKEVNLEQVHRRINSLMDEDIAHKQISPASIELSALEMGGLAPSQALEPTREYQNTQLSVSTFLPEQSSHGTSRTLSSGPSSNLPLPLSSSATMPSIQCKHRSPNGGLFRQSPVKTPIPMSFQPVPGGVLPEALDTSHGTSI | Function: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 112210
Sequence Length: 1009
Subcellular Location: Cell membrane
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Q68Y21 | MKVFPAVLFLITFWSLEWEPVLPDSIIHIGAIFDESAKKDDEVFRMAVADLNLNNEILETEKITVSVEFVDGNNPFQAVQEACELMNRGILALVSSIGCMSAGSLQSLADAMHIPHLFIQRAPAGTPRSSCPPTTRAQPDDYTLFVRPPVYLNDVIFQVVMEYTWQKFIIFYDTDYDIRGIENFLDQTSQQGMDVSLQKVESNINMMITGMFRTMRVEELHRYRDTLRRAVLFMSPATAKAFITEVVETNLVAFDCQWIIINEEISDMDVQELVMKSIGRLTLVRQTFPLPQNTSQRCVRNNHRINTSLCDPKDPKAQMLEITNRYIYDTVLLLANTFHRKLEDRKWHSMASLSCIRKGSKPWQGGKSMLETVKKGGVSGLTSLLEFNDNGSNPNIHFEILGTNYGEDRGRGVSRLATWDPIHGLNGTLTDRKLENNMRGVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALANYLGFKYEIYVAPDHKYGSQQADGTWNGLIGELVFKRADVGLSALTITPERESVVDFTTRYMDYSVGVLLRKAERTVDMFACLAPFDLSLWACIAGTVLLVGTLVYLLNWLNPPRLPMGSVSSTTLYNSMWFVYGSFVQQGGEVPYTTLATRMMMGVWWLFALIVISSYTANLAAFLTISRIENSIQSLQDLAKQTDLPYGTVLDSAVYDQVRSKGMNPFERDPMYSQMWRMINRTGGAENNVEESKEGIRKVKYGRFAFVWDAAVLEYVAINDEDCSLYTVSNNVADRGYGMAMQHGSPYRDIFSQRILELQQNGDMDILKLKWWPRDSPCDLYSPVGTRKSGSALDIHSFAGVFFVLAAGVVLSCLIATVETWWTRRKGSRVPSKEDDKEIDLEHLHHRVNSLCTEDESPHKQFSTSSIDLTPLDMDSLPAARQALEQISDFRNTHITTTTFIPEQIQTLSRSLSAKAAAGFAFGAVQDHRTGGPFRQRAPNGGFFRSPVKTMSSIPYQPTPAPNFSYGNDPDRGTSI | Function: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 113625
Sequence Length: 1009
Subcellular Location: Cell membrane
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O43424 | MEVFPFLLVLSVWWSRTWDSANADSIIHIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQSLADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLHDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDKVSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEINDVDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSTLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKWHSMASLSCIRKNSKPWQGGRSMLETIKKGGVSGLTGELEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNGSLTDKKLENNMRGVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSVGVLLRRAEKTVDMFACLAPFDLSLWACIAGTVLLVGLLVYLLNWLNPPRLQMGSMTSTTLYNSMWFVYGSFVQQGGEVPYTTLATRMMMGAWWLFALIVISSYTANLAAFLTITRIESSIQSLQDLSKQTEIPYGTVLDSAVYEHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFYTIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWPKNGQCDLYSSVDTKQKGGALDIKSFAGVFCILAAGIVLSCFIAMLETWWNKRKGSRVPSKEDDKEIDLEHLHRRVNSLCTDDDSPHKQFSTSSIDLTPLDIDTLPTRQALEQISDFRNTHITTTTFIPEQIQTLSRTLSAKAASGFTFGNVPEHRTGPFRHRAPNGGFFRSPIKTMSSIPYQPTPTLGLNLGNDPDRGTSI | Function: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. Promotes synaptogenesis and mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis of cerebellar parallel fiber-Purkinje cell (PF-PC) synapses through the beta-NRX1-CBLN1-GRID2 triad complex .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 113356
Sequence Length: 1007
Domain: The PDZ-binding motif mediates interaction with GOPC.
Subcellular Location: Cell membrane
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Q61625 | MEVFPLLLFLSFCWSRTWDLATADSIIHIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQSLADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNEVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDKVSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFISEVVETNLVAFDCHWIIINEEINDVDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSSLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKWHSMASLSCIRKNSKPWQGGRSMLETIKKGGVNGLTGDLEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNGSLTDKKLENNMRGVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSVGVLLRRAEKTVDMFACLAPFDLSLWACIAGTVLLVGLLVYLLNWLNPPRLQMGSMTSTTLYNSMWFVYGSFVQQGGEVPYTTLATRMMMGAWWLFALIVISSYTANLAAFLTITRIESSIQSLQDLSKQTDIPYGTVLDSAVYQHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQSGDMDILKHKWWPKNGQCDLYSSVDAKQKGGALDIKSLAGVFCILAAGIVLSCLIAVLETWWSRRKGSRVPSKEDDKEIDLEHLHRRVNSLCTDDDSPHKQFSTSSIDLTPLDIDTLPTRQALEQISDFRNTHITTTTFIPEQIQTLSRTLSAKAASGFAFGSVPEHRTGPFRHRAPNGGFFRSPIKTMSSIPYQPTPTLGLNLGNDPDRGTSI | Function: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. Promotes synaptogenesis and mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis of cerebellar parallel fiber-Purkinje cell (PF-PC) synapses through the beta-NRX1-CBLN1-GRID2 triad complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 113082
Sequence Length: 1007
Domain: The PDZ-binding motif mediates interaction with GOPC.
Subcellular Location: Cell membrane
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B1VTI5 | MVHVRKNHLTMTAEEKRRFVHAVLEIKRRGIYDRFVKLHIQINSTDYLDKETGKRLGHVNPGFLPWHRQYLLKFEQALQKVDPRVTLPYWDWTTDHGENSPLWSDTFMGGNGRPGDRRVMTGPFARRNGWKLNISVIPEGPEDPALNGNYTHDDRDYLVRDFGTLTPDLPTPQELEQTLDLTVYDCPPWNHTSGGTPPYESFRNHLEGYTKFAWEPRLGKLHGAAHVWTGGHMMYIGSPNDPVFFLNHCMIDRCWALWQARHPDVPHYLPTVPTQDVPDLNTPLGPWHTKTPADLLDHTRFYTYDQ | Cofactor: Binds 2 copper ions per subunit.
Function: Involved in the biosynthesis of the parasiticide antibiotic grixazone. Catalyzes the oxidation of 3-amino-4-hydroxybenzoate (3,4-AHBOA) to yield the corresponding quinone imine which is then non-enzymatically conjugated with the thiol group of N-acetylcysteine. The resultant compound is oxidized to its quinone imine enzymatically and is then dimerized non-enzymatically with another quinone imine oxidized by GriF to yield grixazone B. 3-amino-4-hydroxybenzaldehyde (3,4-AHBAL) can also be used as substrate to yield grixazone A. In the grixazone biosynthetic pathway, it can also function as an o-aminophenol oxidase that catalyzes the formation of the phenoxazinone chromophore from alpha-aminophenol. It can also use 2-amino-4-methylphenol, and to a lesser extent, 3,4-dihydroxybenzaldehyde, catechol and 3,4-dihydroxy-L-phenylalanine (L-DOPA) as substrates. In contrast to tyrosinases, it does not display monophenolase activity.
Catalytic Activity: 2 3-amino-4-hydroxybenzoate + H(+) + N-acetyl-L-cysteine + 2 O2 = CO2 + grixazone B + 4 H2O
Sequence Mass (Da): 35583
Sequence Length: 306
EC: 1.10.3.15
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B1VTI7 | MSSSPSPSPSSSSSSSASSSASSSPSSSSKLTWLDIRSVGEARAAIVQEALHHRVEALVADDPAHLADLPPTVAKVLLVVGKQIPEEFGEATVVVVDPSKHGVTPAELALKHPEIEFGRFVEIIDAPTLEDACESSRTEKWSVLLFRDPTKIPLEIVIAAAARASGSMVTIAQDLEEAEILFGVLEHGSDGVMMAPKTVGDAAELKRIAEAGIPNLNLTELRVVETSHIGMGERACVDTTTHFGEDEGILVGSHSKGMILCVSETHPLPYMPTRPFRVNAGAIHSYTLGRDERTNYLSELKTGSKLTAVDIKGNTRLVTVGRVKIETRPLISIDAEAPDGRRVNLILQDDWHVRVLGPGGTVLNSTELKPGDTVLGYLPVEDRHVGYPINEFCLEK | Function: Catalyzes the cyclization of 2-amino-4,5-dihydroxy-6-one-heptanoic acid-7-phosphate to yield 3-amino-4-hydroxybenzoic acid (3,4-AHBA).
Catalytic Activity: 2-amino-4,5-dihydroxy-6-oxo-7-(phosphooxy)heptanoate = 3-amino-4-hydroxybenzoate + H(+) + 2 H2O + phosphate
Sequence Mass (Da): 42438
Sequence Length: 396
EC: 4.1.99.20
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B1VTI8 | MAPNAPFARSLRLQRLHHHDPDRLFIVPLDHSITDGPLSRAHRLDPLVGELASHHVDGIVLHKGSLRHVDPEWFTRTSLIVHLSASTVHAPDPNAKYLVSSVEESLRMGADAVSVHVNLGSEGERHQIADMAAVAEACDRWNVPLLAMMYPRGPKIDDPRDPALVAHAVQVAVDLGADLVKTLYVGSVAAMAEITAASPVPVVVVGGPRDSDESRILAYVDDALRGGAAGVAMGRNVFQAPDPGAMADKLSDLIHNSGTRGAARAPAGAAAGAA | Function: catalyzes aldol condensation between L-aspartate-4-semialdehyde (ASA) and dihydroxyacetone phosphate (DHAP), to form 2-amino-4,5-dihydroxy-6-oxo-7-(phosphonooxy)heptanoate.
Catalytic Activity: 2-amino-4,5-dihydroxy-6-oxo-7-(phosphooxy)heptanoate = dihydroxyacetone phosphate + L-aspartate 4-semialdehyde
Sequence Mass (Da): 28851
Sequence Length: 274
EC: 4.1.2.56
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O95267 | MGTLGKAREAPRKPSHGCRAASKARLEAKPANSPFPSHPSLAHITQFRMMVSLGHLAKGASLDDLIDSCIQSFDADGNLCRSNQLLQVMLTMHRIVISSAELLQKVITLYKDALAKNSPGLCLKICYFVRYWITEFWVMFKMDASLTDTMEEFQELVKAKGEELHCRLIDTTQINARDWSRKLTQRIKSNTSKKRKVSLLFDHLEPEELSEHLTYLEFKSFRRISFSDYQNYLVNSCVKENPTMERSIALCNGISQWVQLMVLSRPTPQLRAEVFIKFIQVAQKLHQLQNFNTLMAVIGGLCHSSISRLKETSSHVPHEINKVLGEMTELLSSSRNYDNYRRAYGECTDFKIPILGVHLKDLISLYEAMPDYLEDGKVNVHKLLALYNHISELVQLQEVAPPLEANKDLVHLLTLSLDLYYTEDEIYELSYAREPRNHRAPPLTPSKPPVVVDWASGVSPKPDPKTISKHVQRMVDSVFKNYDHDQDGYISQEEFEKIAASFPFSFCVMDKDREGLISRDEITAYFMRASSIYSKLGLGFPHNFQETTYLKPTFCDNCAGFLWGVIKQGYRCKDCGMNCHKQCKDLVVFECKKRAKNPVAPTENNTSVGPVSNLCSLGAKDLLHAPEEGPFTFPNGEAVEHGEESKDRTIMLMGVSSQKISLRLKRAVAHKATQTESQPWIGSEGPSGPFVLSSPRKTAQDTLYVLPSPTSPCPSPVLVRKRAFVKWENKDSLIKSKEELRHLRLPTYQELEQEINTLKADNDALKIQLKYAQKKIESLQLEKSNHVLAQMEQGDCS | Function: Functions as a calcium- and diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP . Activates the Erk/MAP kinase cascade . Regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras . Regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways . Functions in mast cell degranulation and cytokine secretion, regulating FcERI-evoked allergic responses. May also function in differentiation of other cell types .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 90402
Sequence Length: 797
Domain: The phorbol-ester/DAG-type zinc finger is the principal mediator of the targeting to membranes and is required for functional activation through DAG-binding.
Subcellular Location: Cytoplasm
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Q6NTL4 | MGTVGKKKDRPAHGCSTIPKLALELKQIIHSTTHPKVPAVTPLRVMMPLGKLSKGASLDELIQMCIQAFDLDGNMGQNNELLQIMLTMHGFLIPSTELLIKLRTLYQDAMQNRSFSFCLRICYFIRYWITELWVMFKMDAKLTQTMEEFQELVRSHGEELHWRLIDTAQINSRDWSRKLTQRIQSNCSKKRKVSLLFDHLEPQELAEHLTYLEFKAFRRISFSDYQNYIVNGCVKDNPTMERSIALCNGISQWVQLMVLSRPTPQLRAEVLTKFIHVAQKLHQLQNFNTLMAVIGGLCHSSISRLKDTSSHVSHDVTKVLNEMTELLSSCRNYDNYRRAYNECTNFKIPILGVHLKDLIALHEAMPDFLEESKINVPKLHSLYNHINELIQLQNIAPPLEANMDLVHLLTLSLDLYYTEDEMYELSYAREPRNYRAPPVTPSKPPVVADWASGVSPKPDPKTISKHVQRMVDSVFKNYDLDQDGYISQEEFEKIAASFPFSFCVMDKDREGLISRQEITAYFMRASSICSKLGLGFLHNFQETTYLRPTFCDNCAGFLWGVIKQGYRCKDCGMNCHKQCKELVVFECKKRSKCSMGENNTLSDAGQLEVIPAGGKGLTNDCLGADEGPYSYPNGDGDIHTEVSKDRTIMLMGSSAQKISVRLQPAVKHRATQTENETQSLCLQVPSPPRSRTPDLTSHLPISPMPSPCPSPVPTRKKAYAKWENKDSIRKARAELRGGKAGIQELEKEKVFLKEENTALKIQLKDAHRRVETLRAELRKYVLDSDTHQKGS | Function: Functions as a diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 90172
Sequence Length: 791
Domain: The phorbol-ester/DAG-type zinc finger is the principal mediator of the targeting to membranes and is required for functional activation through DAG-binding.
Subcellular Location: Cytoplasm
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Q94529 | MANKVLRKVTHCVFDMDGLLLDTERLYTVATEMILEPYGKTYPFEIKEQVMGLQTEPLARFMVEHYELPMSWEEYARQQRANTEILMRNAQLMPGAERLLRHLHANKVPFCLATSSGADMVELKTAQHRELFSLFNHKVCGSSDKEVVNGKPAPDIFLVAAGRFGVPPKPSDCLVFEDSPNGVTAANSAGMQVVMVPDPRLSQEKTSHATQVLASLADFKPEQFGLPAFTD | Function: Dephosphorylates pseudouridine 5'-phosphate, a potential intermediate in rRNA degradation.
Catalytic Activity: H2O + psi-UMP = phosphate + pseudouridine
Sequence Mass (Da): 25785
Sequence Length: 231
EC: 3.1.3.96
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B7GIK0 | MNFTKSEQLYQEALEHIVGGVNSPSRSYKAVGGGAPVVMERAQGAYFWDVDGNKYIDYLAAYGPIITGHAHPHITKAIQHAAENGVLYGTPTPYEITFAKMLKEAIPSLEKVRFVNSGTEAVMTTIRVARAYTGRDKIVKFAGCYHGHSDLVLVAAGSGPSTLGTPDSAGVPKSIAQEVITVPFNDVDAFKQAMDRWGNEVAAVLVEPIVGNFGIVEPKPGFLQAINDIAHAVGALVIYDEVITAFRFMYGGAQNLLGIEPDLTALGKIIGGGLPIGAYGGRKDIMEQVAPLGPAYQAGTMAGNPASILAGIACLEVLQQEGVYEHLDHLGAMLEAGILTHAKTYDIPITINRLKGALTVYFTTEKVENYEQAERTDGEMFAKFFKLMLHQGINLAPSKYEAWFITLAHTEEDIEYTIEAVERAFKSLKNE | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 46612
Sequence Length: 431
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
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P42799 | MSATLTGSGTALGFSCSSKISKRVSSSPASNRCCIKMSVSVDEKKKSFSLQKSEEAFNAAKNLMPGGVNSPVRAFKSVGGQPVLIDSVKGSKMWDIDGNEYIDYVGSWGPAIIGHADDEVLAALAETMKKGTSFGAPCLLENVLAEMVISAVPSIEMVRFVNSGTEACMGVLRLARAFTNKEKFIKFEGCYHGHANAFLVKAGSGVATLGLPDSPGVPKAATSDTLTAPYNDLEAVEKLFAAHKGEISAVILEPVVGNSGFIPPTPEFINGLRQLTKDNGVLLIFDEVMTGFRLAYGGAQEYFGITPDLTTLGKIIGGGLPVGAYGGRRDIMEMVAPAGPMYQAGTLSGNPLAMTAGIHTLKRLKQAGTYEYLDKITKELTNGILEAGKKTGHPMCGGYISGMFGFFFAEGPVYNFADSKKSDTEKFGRFFRGMLEEGVYFAPSQFEAGFTSLAHTPEDIQLTIAAAERVLSRI | Cofactor: Can use both pyridoxamine 5'-phosphate (PMP) and pyridoxal 5'-phosphate (PLP) as cofactors.
Function: Transaminase converting glutamate 1-semialdehyde (GSA) to 5-aminolevulinate (ALA). Involved in the biosynthesis of tetrapyrroles.
Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 50370
Sequence Length: 474
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Plastid
EC: 5.4.3.8
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Q3B1A1 | MPTHTRSAELFEKAKKFIPGGVNSPVRAFKSVGGNPIFMAKGQGAYMTDVDGNTYLDYVGSWGPFILGSMHPRITAALEHTLTKIGTSFGTPIEMEIEIAELLTKIVPSIEMVRMVNSGTEATMSAVRLARGCTGRDKIIKFEGCYHGHGDSFLIKAGSGALTLGAPDSPGVTKGTAEDTLNAKYNDIKSVELLVAENKGNIAAIIIEPVAGNTGVIPAKKEFLQALRDLCDREGIVLIFDEVMCGFRVALGGAQELYGITPDLTTMGKIIGGGLPVGAFGGKRSLMENVAPLGGVYQAGTLSGNPLALTAGIETLKILMEENPYPELDRKGAFLEAGFRDNMQKLGLNFVQNRVGSMACLFFTETPVESYDSAITADTEKFGKYFSSMLEQGIYLAPSQFEAMFTSTMHTDADLEKTVKANYVALQAATK | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 46116
Sequence Length: 431
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
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A1BJG8 | MLQHTKSAELFEKAKQFIPGGVNSPVRAFKSVGGTPIYMAKGRGAYLTDVDGNSYLDYVGSWGPFILGSMHPRITAALEYTLKNIGTSFGTPIEMEIEIAELLCKIVPSLEMVRMVNSGTEATMSAVRLARGYTGRDKIIKFEGCYHGHGDSFLIKAGSGALTLGAPDSPGVTKGTALDTLNATYNDIESVKLLVEENKNNIAAIIIEPVAGNTGVIPAKPGFLADLRNLCDQNGIVLIFDEVMCGFRVALGGAQSLYGVTPDLTTMGKIIGGGLPVGAFGGKRKIMERVAPLGDVYQAGTLSGNPLALTAGLETLKILMDENPYPELERKAAILEAGFRDNMQKLGLNFVQNRVGSMACLFFTETPVESYASAITADIRKYGKYFHSMLEQGIYLAPSQFEAMFTSSMHTDEDLDKTIKANFNALQIACS | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 46315
Sequence Length: 431
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
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Q9JRW9 | MLNCSNQKHTVTFEEACQVFPGGVNSPVRACRSVGVTPPIVSSAQGDIFLDTHGREFIDFCGGWGALIHGHSHPKIVKAIQKTALKGTSYGLTSEEEILFATMLLSSLKLKEHKIRFVSSGTEATMTAVRLARGITNRSIIIKFIGGYHGHADTLLGGISTTEETIDNLTSLIHTPSPHSLLISLPYNNSQILHHVMEALGPQVAGIIFEPICANMGIVLPKAEFLDDIIELCKRFGSLSIMDEVVTGFRVAFQGAKDIFNLSPDITIYGKILGGGLPAAALVGHRSILDHLMPEGTIFQAGTMSGNFLAMATGHAAIQLCQSEGFYDHLSQLEALFYSPIEEEIRSQGFPVSLVHQGTMFSLFFTESAPTNFDEAKNSDVEKFQTFYSEVFDNGVYLSPSPLEANFISSAHTEENLTYAQNIIIDSLIKIFDSSAQRFF | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 47956
Sequence Length: 440
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
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A6Q2X6 | MLSKSEAAYKEALRYIPGGVDSPVRAFKSVGGVPPFIDRGEGAFLYDIDGNRYIDYVQSWGPLIFGHADKETLEAVCEQAQKGLSFGTPTLLETELAREIVELFDNIDKIRFVSSGTEAVMSAIRLARGYTGRDDIVKFEGCYHGHSDSLLVSAGSGAATFGNPSSPGVPADFTKHTLLARYNDIESVKRCFQASDNIACVIIEPIAGNMGLVPAEEEFLQDLRKLCDEHGALLIFDEVMSGFRASLKGAQGFTSVVPDMVTFGKVIGGGMPVGAFGARAEIMAHLSPEGPVYQAGTLSGNPVAMVAGLSVIRRLKNDPSIYEVLEARAKGLVGGFKKIADSFGVPLQVDVRGSMFGFFFNEKPVKNFDDAKQSDLEFFAKFHQEMIKRGIYFACSQFEAGFICTPLDEKLIDETLEKIEEGLKKIV | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 46394
Sequence Length: 427
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
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Q5YP79 | MSASPRATHASAAASARLFDRAAQVIPGGVNSPVRAFRSVGGTPRFIASADGYTLTDADGNEYVDLVCSWGPMILGHAHPAVVDAVRRAATGGLSFGAPTEAEVELAEHIVARVAPVDRVRLVNSGTEATMSAVRLARGFTGRTKIIKFAGCYHGHVDALLADAGSGVATLGLPTSPGVTGAQAADTIVLPYNDLDAVAAAFEANPGEIACVITEAAAGNMGAVAPLPGFNAGLRELTENHGALLIMDEVMTGFRVSRSGWYGREGVAGDLYTFGKVMSGGLPAAAFGGRAEVMNQLAPLGPVYQAGTLSGNPVAVAAGLATLRAADDAVYAALDRNAERLGGLLTEALTAAGVEHQVQFAGNMVSVFFSDRPVTDYATAKASQTWRFPAFFHALLDGGVYAPPSAFEAWFVSAALDEDAFARIAAALPAAARAAAAATPEGSRA | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 45484
Sequence Length: 445
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
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B2T6C2 | MSRNETLFERAQRTIPGGVNSPVRAFRSVGGTPRFIERAQGPYFWDADGQRYIDYIGSWGPMILGHVHPEVLEAVQRVLGNGFSFGAPTESEVEIAEEICKLVPSIEQVRMVSSGTEATMSALRLARGFTNRSRIVKFEGCYHGHADSLLVKAGSGLLTFGNPTSAGVPADIAKHTTVLEYNNVAELEEAFKAFGNEIASVIVEPVAGNMNLVRATPEFLQALRRLCTEHGSVLIFDEVMCGFRVALGGAQEVYGITPDLTCLGKVIGGGMPAAAFGGRRDIMAHLAPLGGVYQAGTLSGNPIAVAAGLKTLQLIQAPGFYDTLATRTARLVQGLANVAREAKVPFAADSLGGMFGLYFTDSIPTSFAEVTKSDVPRFNAFFHKMLDAGVYFAPSAYEAGFVSIVHDDAIVDATIDAARGAFASLAA | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 45462
Sequence Length: 427
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
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Q6MAC7 | MISRPISQQIYSNLNRVIPGGVNSPVRACANMGQIPMIIDHAYRDTLVDVDGKTYVDYCGSWGALIHGHAHPSILEAVQQRMKKGTSFGITTSIEGELAQEVIKLIDSVEKIRFVSSGTEATMSAVRLARGYTNKEFIVKFNGNYHGHADFFLVQAGSGVLEVSPSASSAGIPADIVKQTLCLPYNDIEACRQIFHHSDYRHKIAAIILEPIAGNMGVIPASQEFMQFLRKETLAMGALLIFDEVMTGFRVALKGAQDIYPVEPDLTCFGKIIGGGFPAAAFGGREEIMNLLAPLGSVYQAGTLSGNPIAMEAGLQSLRLIQQPGFYEELHRKTDLLLNPIKETIKKNNWPICIQQAGSMFTLFFCKNRVRNLEDALKANTTIFANFFRKLFDQGIYIPPSQHEAWFISQAHEESNLIKTQSAILTFLEENF | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 47738
Sequence Length: 432
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
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Q9KUG5 | MSKFAERLQTVANKPEVFQKFSRGLERESLRYTPEGALTQTPHPKALGAALTHRWITTDFAESLLEFITPVSHEVDTLLAQMSDIHHFAQTKLGDEKLWPLSMPCYVGSEEGIVLAQYGSSNTGKMKTLYREGLKRRYGSLMQIISGVHFNFSFPESFWDALFGEQEESARQASKSAAYFGVIRNYYRFGWLIPYLFGASPALCSSFLQGRKTDLPFESIGKTLYLPYATSLRLSDLGYTNSAQSVLQIGFNSIEQYLQGLNEAIRTPSAEFAKLGVKVEGEYRQLNSNVLQIENELYAPIRPKRVTQSGERPSQALARAGVEYIEVRSLDVNPFSPIGINEDQVRFLDLFLAWTALSDSDPMDGCELACWRDNWRKVVLEGRKPGLELQIGCHGEVLTLQAWAKRVFADLRVIAETMDAALGGDAYQAVCAKLETWIENPELTLSAQILAEIKQHGGLGKTGCALGNEYRAVNLQHQYQFYSQDEMEQEVRRSTQAQADIEAKETLNFDAYLTQYFAYLQAVS | Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 58961
Sequence Length: 524
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
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Q8D2V5 | MIPKVSKIIPWIKDNKKFLKKTYKGIERESLRIDIDGNISKKPHPIIFGSPLTHNWITTDFSESLLELITPVSNSKKYTINFLNDLHIFIIKNLINENLWPMSMPCKINNDSSIIIAQYGNSKLGRTKTIYRNGLKNRYGAKMQIISGVHYNFSFHKDFWKKYNNFYKIQDKFSSIGYFNLIRNYYRFGWIIPYFFGASPIAHSSFFKGLNTDLIFKKNKFGDIYLPFSTSLRLSEIGYINKVQKKIKLKFNNIEEYVDIVKKAMKTPYLNYKKIELKNNEKNLQINVNLLQKENELYSHVRPKRSLNKNKYKLEDLIYKGIEYIEIRSLDVNPFSPIGIKINQIYFLDIFLIWCILIESPKINDEELRSINENWNRVILYGRNPKIKLINFFKKKEKKLSEILKFILNDLQILVESLAFKKNNKIYQKIFFDLHKMTDNPNKTLSGKLLEESIEYGVERLGLDMSKSHKINIENKKLKVINYQSLIKEAEKSIKEQIVLEKNET | Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 59745
Sequence Length: 505
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
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P32477 | MGLLALGTPLQWFESRTYNEHIRDEGIEQLLYIFQAAGKRDNDPLFWGDELEYMVVDFDDKERNSMLDVCHDKILTELNMEDSSLCEANDVSFHPEYGRYMLEATPASPYLNYVGSYVEVNMQKRRAIAEYKLSEYARQDSKNNLHVGSRSVPLTLTVFPRMGCPDFINIKDPWNHKNAASRSLFLPDEVINRHVRFPNLTASIRTRRGEKVCMNVPMYKDIATPETDDSIYDRDWFLPEDKEAKLASKPGFIYMDSMGFGMGCSCLQVTFQAPNINKARYLYDALVNFAPIMLAFSAAAPAFKGWLADQDVRWNVISGAVDDRTPKERGVAPLLPKYNKNGFGGIAKDVQDKVLEIPKSRYSSVDLFLGGSKFFNRTYNDTNVPINEKVLGRLLENDKAPLDYDLAKHFAHLYIRDPVSTFEELLNQDNKTSSNHFENIQSTNWQTLRFKPPTQQATPDKKDSPGWRVEFRPFEVQLLDFENAAYSVLIYLIVDSILTFSDNINAYIHMSKVWENMKIAHHRDAILFEKFHWKKSFRNDTDVETEDYSISEIFHNPENGIFPQFVTPILCQKGFVTKDWKELKHSSKHERLYYYLKLISDRASGELPTTAKFFRNFVLQHPDYKHDSKISKSINYDLLSTCDRLTHLDDSKGELTSFLGAEIAEYVKKNKPSIESKC | Function: Catalyzes the ATP-dependent condensation of cysteine and glutamate to form the dipeptide gamma-glutamylcysteine (gamma-GC), the first and rate-limiting step in the production of glutathione (GSH).
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 78254
Sequence Length: 678
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
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Q8ZBU2 | MIPDVSHALTWLEAHPKALKGIRRGIERETLRVTADGHLASTGHPESLGAALTHQWITTDFAEALLEFITPVDGDIDHLLTFLRDIHRYTARKLGDERMWPLSMPCFIEAEQDIELAKYGSSNIGRFKTLYREGLKNRYGALMQTISGVHYNFSLPLEFWQAWAGVTDEQSGKEEISAGYFRLIRNYYRFGWVIPYLFGASPAICSSFLQGRETALPFERNGKGMCYLPYATSLRLSDLGYTNKSQSNLGITFNDLHTYVDALKRAIQTPSEEYVALGLKDGDRHLQLNTNVLQIENELYAPIRPKRVTRAGESPSDALLRGGIEYIEVRSLDINPFSPIGVDAVQARFLDLFLIWCVLADAPEMSSDELLCTRKNWDRVILEGRKPGQTIGIGCSDSRQPLETVGKALFADLRRVAEVLDGSESASYQQVCDELVASFDDPELTFSARILKVMQEKGSGGVGLELAEHYREMLQNEPLELLTEEQLSAERDASRQRQHELELKDKLSFEEYLALHGGQ | Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 58471
Sequence Length: 519
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
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Q8XK30 | MVNLDKGLLKIIKDESLEDYFIKANFGLEKENVRVTESGNLALTPHPKAFGDREKNAYIKTDFSESQLEMVTPVCNTLEEVYSFICNLNKVVSLEIMKNGEFLWPQSNPPILPREEEIPIAKLSNREDELYRENLSYKYGKKKQVISGIHYNFSFKEEFIKLLYKELKVEKDFREFKDDIYLRMARNFQKYHWLLIYLTGASPVFHESYIEEIKEEGEKLGEDSYYIKDDTSLRNSSYGYKNKKDYYVSYNSIEEYASDIKNLVKDKEIQSIKEYYNPIRLKSLGSEDMLESLLHKGIDYLEVRLLDLDPLSIQGVSKETLYLLHLFMIYTLLKENKEITYKDQEEFFKNHDMVALKGRNEEAVIYENGVPVLLKDKGREILSEMDEIVEILFSNNEEFKNVIKRALEKINNPHDTISEKLIKDIKEEGYINFHMRLAKEYLNNFKNKEFNLVGYEDLELSTQILILDAIKRGIEFNIMDRLENFISLSDGEKVEYVKQATKTSKDSYITALIMENKLVTKDILRENNIRVPKGKDYDNIDEAKKDFRLFKDEKIVIKPKSTNFGLGISIFPGEYSREDYDKAVEIAFREDSSILIEEFMTGKEYRFLVIGEEVVGILHREPANVIGNGESTIEELVSEKNKDPLRGKGYKTPLEKIKLGEIEEMFLKNQGLSFKSIPKNGEKIYLRENSNISTGGDSIDFTDKIHPSYKEVALKSAKAVKALICGVDMVIDNIEEEAKEKNHGIIELNFNPAIHIHCFPYKGENRKAGEKILDLLFN | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 90463
Sequence Length: 778
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
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Q6ANW2 | MAFSKNILDSLPPLISKQIFEGFFGFEKENIRVDSRGKLALTPHPRELGEKTSHPYITTDFSESQIEIITPPLPSIAESLGFLETLHDLVSIELKDEYLWPQSAPPILPEREEDIPIAHFGGEFREQEEYRLQLAKIYGRKRQMFSGIHFNISLPERFLELLHEEGKQEQPFAEFREDIYMKTVRNFLRHRWFLICLLGASPVIHKSYRKHCIDMLSPFAKDAYHFPYATSIRNNICGYRNTQDFHLNYSTLTDYRESLQELVEKKVLRDIRENYAPIRIKTTTDPKRINHLEIRLLDLNPFFKTGVNPLHAEIIHIFLIYCLLCPEETSFTSKEQETANRNQEQAATEGLNPGAIICDADGNEQRLDKQLAHCLQEIQQTVSPHLPPEYRAGMEELERLVQNQASRPTDTLLKEIKQEGFTEWHMKQALKFLKKSHDEQFIFHGLRDMELSTQLLLRRAALRGVSFEIMDRQENFVCLEQAGKREYVMQASRTSLDNYISVLSMENKVITKKILDQAGINTPKGRSYSSPSEALADYPYYRGRAIVIKPKSTNFGIGITIIKENNRHDFFAQGIAQAFKHEATVLIENFSSGKEYRFFIVNDQVVGILHRVPANVTGDGTSSVQVLVTEKNKNPLRGRGYRTPLEKIKLEETEEMFLASQGYSFATVPAKDQRIYLRENSNISTGGDSIDFTDKVPQSYKDIAVRAAQALQVKITGLDMMIDSLEEDAAEDNFSIIELNFNPAIHIHCHPYIGKNRHLDDKILDALGFTGAEEAGEKA | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 89336
Sequence Length: 779
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
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Q82ZG8 | MNYRELMQKKNVRPYVLMARFGLEKENQRSTREGLLATTEHPTVFGNRSYHPYIQTDFSETQLELITPVANSGTEMLRFLDAIHDVARRSIPEDEMLWPLSMPPQLPTKDEEIKIAKLDQYDAVLYRRYLAKEYGKRKQMVSGIHFNFEYDQALIQQLYDEQSEVTDCKQFKTKVYMKVARNFLRYRWLITYLFGASPVSEDRYFRVYDDQPQEPVRSIRNSTYGYRNHDNVKVSYASLERYLEDIHRMVENGLLSEEKEFYAPVRLRGGKQMSDLPKTGIRYIELRNLDLNPFSRLGIVEDTVDFLHYFMLYLLWTDEKEEADEWVKTGDIFNEQVALGHPHETIKLIAEGDRIFSEMIDMLDALGIRKGKEVVGKYYQQLRNPQDTVSGKMWTIIQENSNSELGNIFGNQYQSMAFERPYQLAGFREMELSTQIFLFDAIQKGLEIEILDEQEQFLKLQHGEHIEYVKNANMTSKDNYVVPLIMENKTVTKKILSAAGFHVPGGEEFSSFIEAQEAHLRYANKAFVVKPKSTNYGLGITIFKEGASLEDFTEALRIAFKEDTAVLIEEFLPGTEYRFFVLDNDVKAIMLRVPANVTGDGKHTVEELVAAKNSDPLRGTNHRAPLELIQLNDLEKLMLKEQGLTIYSVPEKEQIVYLRENSNVSTGGDSIDMTDVIDDSYKQIAIEAVAALGAKICGIDLIIPDKDVKGTRDSLTYGIIEANFNPAMHMHVYPYAGQGRRLTMDVLKLLYPEVVQ | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 87212
Sequence Length: 756
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
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Q88UW5 | MELDAVGKAIVQYHLVPLVHQANLGLEVTMHRVDAHGHLATTAHPQAFGSAQQNHQLRPGFSASALKFTTPVRRDIPALMAYLKGLNTAARRSLDADERLWPLSSTPVLPDDLTNVPLADVDQVSYQRRRDLARKYELQRLMTTGSHVNMSLNEALFTRLYTETFHQQYHSYVDFRNAIYLKVAQGLVRMNWLIQYLFGASPRLAVTDTTSRPQRSSVQHPDGRYSQVTGDYTSIDRYVAKLTAAVRQQQLLSVNDFDGPVRLRSNGQLAMMARQGVYYLEYRGLDLDPTSPVGVDANAVAFVRLLASYFVMMPALPAKMVSQVNAQADQLTRQVLGENPTTASAQAVPAVQVLDALADFVKTYGLPNEDAVLLKQLKSWVTDPKKTLSAQIAMQADPLAWALERAARYQESSNERPFELAGFTALDLSSQQLAQQALTRGVQVDVVDPHANILRLTKLGRSQLVVNGSGTDLNPQALTTVLTHKAAAKQILAEHGVPVPASQTYHTANQLIADYDRYVQAGGIVLKAADESHKVIVFRIMPERGLFEQVVRQLFEQTSAVMAEEVVVASSYRFLVIDSRVQAIVERIPANIVGDGRSTVKTLLDRKNGRALRGTAFKWPQSALQLGTIERYRLDSYHLTLDSVVSRGTQILLREDATFGNGADVLDATADMHQSYVQAVEKLVADLHLAVAGVDVMIPNLYAELVPEHPEMAVYLGIHAAPYLYPHLFPMFGTAQPVAGQLLDALFKNED | Function: Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 83018
Sequence Length: 751
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
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Q8Y3R3 | MLDSFKEDPNLRKLLFSGHFGLEKENIRVTSDGKLALTPHPAIFGPKEDNPYIKTDFSESQIEMITPVTDSIDSVYEWLENLHNIVSLRSENELLWPSSNPPILPAEEDIPIAEYKTPDSPDRKYREHLAKGYGKKIQLLSGIHYNFSFPEALIDGLYANISLPEESKQDFKNRLYLKVAKYFMKNRWLLIYLTGASPVYLADFSKTKHEESLPDGSSALRDGISLRNSNAGYKNKEALFVDYNSFDAYISSISNYIEAGKIESMREFYNPIRLKNAHTDQTVESLAEHGVEYLEIRSIDLNPLEPNGISKDELDFIHLFLIKGLLSEDRELCANNQQLADENENNIALNGLAQPSIKNCDNEDIPLADAGLLELDKMSDFIKSLRPEDTKLRAIIEKQKERLLHPEKTIAAQVKQQVTKEGYVDFHLNQAKTYMEETEALAYKLIGAEDMELSTQIIWKDAIARGIKVDVLDRAENFLRFQKGDHIEYVKQASKTSKDNYVSVLMMENKVVTKLVLAEHDIRVPFGDSFSDQALALEAFSLFEDKQIVVKPKSTNYGWGISIFKNKFTLEDYQEALNIAFSYDSSVIIEEFIPGDEFRFLVINDKVEAVLKRVPANVTGDGIHTVRELVEEKNTDPLRGTDHLKPLEKIRTGPEETLMLSMQNLSWDSIPKAEEIIYLRENSNVSTGGDSIDYTEEMDDYFKEIAIRATQVLDAKICGVDIIVPRETIDRDKHAIIELNFNPAMHMHCFPYQGEQKKIGDKILDFLFD | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 87728
Sequence Length: 769
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
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Q65RX0 | MNIQQIVKEKGLGLLFRQGTVGIEKESQRVHADGSIVTSEHPKAFGNRSYHPYIQTDFAESQLELITPPNKKIEDTLRWLSALHEVTLRTIDENEYIFPMSMPAGLPPEQEIRVAQLDNAADVAYREHLVASYGKAKQMVSGIHYNFQLDPKLVETLFNAQTDYKSAVDFQNNLYLKMAKNFLRYQWIPLYLLSATPTVEANYFKDGSPLKPNQYVRSLRSSKYGYVNAPDIIVSFDSIEKYVETLEHWVNSGRLIAEKEFYSNVRLRGAKKAREFLHTGIQYLEFRLFDLNPFEAYGINLKDAKFIHHFILLMIWLEETADQDAVELGRARLGEVAFEDPHSETAYRDEGEQIINQLIDMLKAIGAEQSAVEFAEEKLAQFANPGQTLCARLVDAIEQAGGYQQLGGEIAKRNKVQAFERFYALSAFDNMELSTQALMFDAIQKGLNMEILDENDQFLRLQFGDHFEYVKNGNMTSHDSYISPLIMENKVVTKKVLAKAGFNVPQSLEFTSVEQAVASYPLFEGKAVVIKPKSTNFGLGISIFQQGVHDKADFAKAVEIAFREDKEVMVEDYLVGTEYRFFVLGNETLAVLLRVPANVMGDGVHTVAELVAAKNDHPLRGDGSRTPLKKIALGEIEQLQLKEQGLTVDSVPAKDQLVQLRANSNISTGGDSIDMTDEMHPSYKDLAVGITKAMGAAVCGVDLIIPDLKKPAEPNLSSWGVIEANFNPMMMMHIFPYSGKSRRLTLNVLGMLFPELV | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 85101
Sequence Length: 757
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
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Q9LWN0 | MEAPPGPEPMELDAPPPPAAVAAAAATAGISEKVLQKKEEGGGDAVTGHIISTTIGGKNGEPKRTISYMAERVVGTGSFGIVFQAKCLETGETVAIKKVLQDRRYKNRELQLMRAMEHPNVICLKHCFFSTTSRDELFLNLVMEYVPETLYRVLKHYSNANQRMPLIYVKLYIYQLFRGLAYIHTVPGVCHRDVKPQNVLVDPLTHQVKLCDFGSAKVLVPGEPNISYICSRYYRAPELIFGATEYTTSIDIWSAGCVLAELLLGQPLFPGESAVDQLVEIIKVLGTPTREEIRCMNPNYTEFKFPQIKAHPWHKIFHKRMPPEAIDLASRLLQYSPSLRCTALDACAHSFFDELREPNARLPNGRPFPPLFNFKHELASASPELIHRLIPDHIRRQHGLNFAHAGS | Function: Probable serine-threonine kinase that may act as a negative regulator of brassinosteroid (BR) signaling during flower development. May have physiological roles in stress signal-transduction pathways . Phosphorylates LIC in response to BR perception .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 45580
Sequence Length: 407
EC: 2.7.11.1
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Q60EZ2 | MDQPAPAPEPMLLDAQPPAAVACDKKQQEGEAPYAEGNDAVTGHIISTTIGGKNGEPKRTISYMAERVVGTGSFGIVFQAKCLETGETVAIKKVLQDRRYKNRELQLMRAMDHPNVISLKHCFFSTTSRDELFLNLVMEYVPETLYRVLKHYSNANHRMPLIYVKLYMYQLFRGLAYIHTVPGVCHRDVKPQNVLVDPLTHQVKLCDFGSAKTLVPGEPNISYICSRYYRAPELIFGATEYTTSIDIWSAGCVLAELLLGQPLFPGESAVDQLVEIIKVLGTPTREEIRCMNPNYTEFRFPQIKAHPWHKVFHKRMPPEAIDLASRLLQYSPSLRCTALDACAHPFFDELREPNARLPNGRPFPPLFNFKHELANSSQELISRLIPEHVRRQATHNFFNTGS | Function: Serine-threonine kinase that acts as a negative regulator of brassinosteroid (BR) signaling . Phosphorylates DLT and BZR1, two positive regulators that mediates several BR responses. Phosphorylation of DLT and BZR1 inhibits their activities in BR signaling . Phosphorylates OFP8, a positive regulator of BR responses. Phosphorylated OFP8 shuttles from the nucleus to the cytoplasm where it is degraded by the proteasome . Phosphorylates the E3 ubiquitin-protein ligase PUB24, a negative regulator of BR signaling, which targets BZR1 and promotes its degradation via the 26S proteasome . Phosphorylation of PUB24 increases its stability . Phosphorylates the AP2-ERF transcription factor SMOS1, a positive regulator of BR signaling, which cooperatively functions in a transactivating complex with BZR1 to enhance the transcription of BR biosynthetic genes . Phosphorylation of SMOS1 leads to its degradation by an unknown mechanism .
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 45509
Sequence Length: 402
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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P49840 | MSGGGPSGGGPGGSGRARTSSFAEPGGGGGGGGGGPGGSASGPGGTGGGKASVGAMGGGVGASSSGGGPGGSGGGGSGGPGAGTSFPPPGVKLGRDSGKVTTVVATLGQGPERSQEVAYTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDELYLNLVLEYVPETVYRVARHFTKAKLTIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFKSRTPPEAIALCSSLLEYTPSSRLSPLEACAHSFFDELRCLGTQLPNNRPLPPLFNFSAGELSIQPSLNAILIPPHLRSPAGTTTLTPSSQALTETPTSSDWQSTDATPTLTNSS | Function: Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), CTNNB1/beta-catenin, APC and AXIN1 . Requires primed phosphorylation of the majority of its substrates . Contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis . Regulates glycogen metabolism in liver, but not in muscle (By similarity). May also mediate the development of insulin resistance by regulating activation of transcription factors . In Wnt signaling, regulates the level and transcriptional activity of nuclear CTNNB1/beta-catenin . Facilitates amyloid precursor protein (APP) processing and the generation of APP-derived amyloid plaques found in Alzheimer disease . May be involved in the regulation of replication in pancreatic beta-cells (By similarity). Is necessary for the establishment of neuronal polarity and axon outgrowth (By similarity). Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation (By similarity). Acts as a regulator of autophagy by mediating phosphorylation of KAT5/TIP60 under starvation conditions which activates KAT5/TIP60 acetyltransferase activity and promotes acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer . Negatively regulates extrinsic apoptotic signaling pathway via death domain receptors. Promotes the formation of an anti-apoptotic complex, made of DDX3X, BRIC2 and GSK3B, at death receptors, including TNFRSF10B. The anti-apoptotic function is most effective with weak apoptotic signals and can be overcome by stronger stimulation (By similarity). Phosphorylates mTORC2 complex component RICTOR at 'Thr-1695' which facilitates FBXW7-mediated ubiquitination and subsequent degradation of RICTOR .
PTM: Phosphorylated by AKT1 at Ser-21: upon insulin-mediated signaling, the activated PKB/AKT1 protein kinase phosphorylates and deactivates GSK3A, resulting in the dephosphorylation and activation of GYS1. Activated by phosphorylation at Tyr-279.
Catalytic Activity: ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-[tau protein]
Sequence Mass (Da): 50981
Sequence Length: 483
EC: 2.7.11.26
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Q2NL51 | MSGGGPSGGGPGGSGRARTSSFAEPGGGGGGGGGGPGGSASGPGGTGGGKASVGAMGGGVGASSSGGGPSGSGGGGSGGPGAGTSFPPPGVKLGRDSGKVTTVVATVGQGPERSQEVAYTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDELYLNLVLEYVPETVYRVARHFTKAKLITPIIYIKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFKSSKTPPEAIALCSSLLEYTPSSRLSPLEACAHSFFDELRRLGAQLPNDRPLPPLFNFSPGELSIQPSLNAILIPPHLRSPAGPASPLTTSYNPSSQALTEAQTGQDWQPSDATTATLASSS | Function: Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), CTNNB1/beta-catenin, APC and AXIN1 . Requires primed phosphorylation of the majority of its substrates . Contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis . Regulates glycogen metabolism in liver, but not in muscle . May also mediate the development of insulin resistance by regulating activation of transcription factors (By similarity). In Wnt signaling, regulates the level and transcriptional activity of nuclear CTNNB1/beta-catenin . Facilitates amyloid precursor protein (APP) processing and the generation of APP-derived amyloid plaques found in Alzheimer disease (By similarity). May be involved in the regulation of replication in pancreatic beta-cells (By similarity). Is necessary for the establishment of neuronal polarity and axon outgrowth . Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation . Acts as a regulator of autophagy by mediating phosphorylation of KAT5/TIP60 under starvation conditions, activating KAT5/TIP60 acetyltransferase activity and promoting acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer . Negatively regulates extrinsic apoptotic signaling pathway via death domain receptors. Promotes the formation of an anti-apoptotic complex, made of DDX3X, BRIC2 and GSK3B, at death receptors, including TNFRSF10B. The anti-apoptotic function is most effective with weak apoptotic signals and can be overcome by stronger stimulation (By similarity).
PTM: Phosphorylated by AKT1 at Ser-21: upon insulin-mediated signaling, the activated PKB/AKT1 protein kinase phosphorylates and deactivates GSK3A, resulting in the dephosphorylation and activation of GYS1. Activated by phosphorylation at Tyr-279.
Catalytic Activity: ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-[tau protein]
Sequence Mass (Da): 51661
Sequence Length: 490
EC: 2.7.11.26
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P49841 | MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLATILIPPHARIQAAASTPTNATAASDANTGDRGQTNNAASASASNST | Function: Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1 . Requires primed phosphorylation of the majority of its substrates . In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis . May also mediate the development of insulin resistance by regulating activation of transcription factors . Regulates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase . In Wnt signaling, GSK3B forms a multimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes . Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA . Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene regulation, and thereby opposing the action of calcineurin . Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubules . MAPT/TAU is the principal component of neurofibrillary tangles in Alzheimer disease . Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex . Phosphorylates MACF1, inhibiting its binding to microtubules which is critical for its role in bulge stem cell migration and skin wound repair (By similarity). Probably regulates NF-kappa-B (NFKB1) at the transcriptional level and is required for the NF-kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA) (By similarity). Negatively regulates replication in pancreatic beta-cells, resulting in apoptosis, loss of beta-cells and diabetes (By similarity). Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation (By similarity). Phosphorylates MUC1 in breast cancer cells, decreasing the interaction of MUC1 with CTNNB1/beta-catenin . Is necessary for the establishment of neuronal polarity and axon outgrowth . Phosphorylates MARK2, leading to inhibition of its activity (By similarity). Phosphorylates SIK1 at 'Thr-182', leading to sustainment of its activity . Phosphorylates ZC3HAV1 which enhances its antiviral activity . Phosphorylates SNAI1, leading to its BTRC-triggered ubiquitination and proteasomal degradation . Phosphorylates SFPQ at 'Thr-687' upon T-cell activation . Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59' and stabilizes it by protecting it from proteasomal degradation. Regulates the circadian clock via phosphorylation of the major clock components including BMAL1, CLOCK and PER2 . Phosphorylates FBXL2 at 'Thr-404' and primes it for ubiquitination by the SCF(FBXO3) complex and proteasomal degradation (By similarity). Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal degradation . Phosphorylates BMAL1 at 'Ser-17' and 'Ser-21' and primes it for ubiquitination and proteasomal degradation . Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively regulates its activity. Phosphorylates MYCN in neuroblastoma cells which may promote its degradation . Regulates the circadian rhythmicity of hippocampal long-term potentiation and BMAL1 and PER2 expression (By similarity). Acts as a regulator of autophagy by mediating phosphorylation of KAT5/TIP60 under starvation conditions, activating KAT5/TIP60 acetyltransferase activity and promoting acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer . Negatively regulates extrinsic apoptotic signaling pathway via death domain receptors. Promotes the formation of an anti-apoptotic complex, made of DDX3X, BRIC2 and GSK3B, at death receptors, including TNFRSF10B. The anti-apoptotic function is most effective with weak apoptotic signals and can be overcome by stronger stimulation . Phosphorylates E2F1, promoting the interaction between E2F1 and USP11, stabilizing E2F1 and promoting its activity . Phosphorylates mTORC2 complex component RICTOR at 'Thr-1695' which facilitates FBXW7-mediated ubiquitination and subsequent degradation of RICTOR . Phosphorylates FXR1, promoting FXR1 ubiquitination by the SCF(FBXO4) complex and FXR1 degradation by the proteasome (By similarity).
PTM: Phosphorylated by AKT1 and ILK1. Upon insulin-mediated signaling, the activated PKB/AKT1 protein kinase phosphorylates and deactivates GSK3B, resulting in the dephosphorylation and activation of GYS1. Activated by phosphorylation at Tyr-216 . Inactivated by phosphorylation at Ser-9 (Probable). Phosphorylated in a circadian manner in the hippocampus (By similarity).
Catalytic Activity: ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-[tau protein]
Sequence Mass (Da): 46744
Sequence Length: 420
Subcellular Location: Cytoplasm
EC: 2.7.11.26
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Q9WV60 | MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLATILIPPHARIQAAASPPANATAASDTNAGDRGQTNNAASASASNST | Function: Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1 . Requires primed phosphorylation of the majority of its substrates . In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis (By similarity). May also mediate the development of insulin resistance by regulating activation of transcription factors (By similarity). Regulates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase (By similarity). In Wnt signaling, GSK3B forms a multimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes (By similarity). Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA (By similarity). Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene regulation, and thereby opposing the action of calcineurin (By similarity). Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubules (By similarity). MAPT/TAU is the principal component of neurofibrillary tangles in Alzheimer disease (By similarity). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (By similarity). Phosphorylates MACF1, inhibiting its binding to microtubules which is critical for its role in bulge stem cell migration and skin wound repair . Probably regulates NF-kappa-B (NFKB1) at the transcriptional level and is required for the NF-kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA) . Negatively regulates replication in pancreatic beta-cells, resulting in apoptosis, loss of beta-cells and diabetes . Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation . Phosphorylates MUC1 in breast cancer cells, decreasing the interaction of MUC1 with CTNNB1/beta-catenin (By similarity). Is necessary for the establishment of neuronal polarity and axon outgrowth . Phosphorylates MARK2, leading to inhibition of its activity (By similarity). Phosphorylates SIK1 at 'Thr-182', leading to sustainment of its activity (By similarity). Phosphorylates ZC3HAV1 which enhances its antiviral activity (By similarity). Phosphorylates SNAI1, leading to its BTRC-triggered ubiquitination and proteasomal degradation (By similarity). Phosphorylates SFPQ at 'Thr-687' upon T-cell activation (By similarity). Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59' and stabilizes it by protecting it from proteasomal degradation (By similarity). Regulates the circadian clock via phosphorylation of the major clock components including BMAL1, CLOCK and PER2 . Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal degradation (By similarity). Phosphorylates BMAL1 at 'Ser-17' and 'Ser-21' and primes it for ubiquitination and proteasomal degradation . Phosphorylates FBXL2 at 'Thr-404' and primes it for ubiquitination by the SCF(FBXO3) complex and proteasomal degradation . Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively regulates its activity (By similarity). Phosphorylates MYCN in neuroblastoma cells which may promote its degradation (By similarity). Regulates the circadian rhythmicity of hippocampal long-term potentiation and BMAL1 and PER2 expression . Acts as a regulator of autophagy by mediating phosphorylation of KAT5/TIP60 under starvation conditions, activating KAT5/TIP60 acetyltransferase activity and promoting acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer . Negatively regulates extrinsic apoptotic signaling pathway via death domain receptors (By similarity). Promotes the formation of an anti-apoptotic complex, made of DDX3X, BRIC2 and GSK3B, at death receptors, including TNFRSF10B (By similarity). The anti-apoptotic function is most effective with weak apoptotic signals and can be overcome by stronger stimulation (By similarity). Phosphorylates E2F1, promoting the interaction between E2F1 and USP11, stabilizing E2F1 and promoting its activity (By similarity). Phosphorylates FXR1, promoting FXR1 ubiquitination by the SCF(FBXO4) complex and FXR1 degradation by the proteasome .
PTM: Phosphorylated by AKT1 and ILK1. Upon insulin-mediated signaling, the activated PKB/AKT1 protein kinase phosphorylates and deactivates GSK3B, resulting in the dephosphorylation and activation of GYS1. Activated by phosphorylation at Tyr-216. Phosphorylation of Ser-9 in the hippocampus peaks at CT0, whereas in the liver it peaks at CT12. Inactivated by phosphorylation at Ser-9 (By similarity). Phosphorylated in a circadian manner in the hippocampus .
Catalytic Activity: ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-[tau protein]
Sequence Mass (Da): 46710
Sequence Length: 420
Subcellular Location: Cytoplasm
EC: 2.7.11.26
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P09488 | MPMILGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQTMDNHMQLGMICYNPEFEKLKPKYLEELPEKLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDLHRIFEPKCLDAFPNLKDFISRFEGLEKISAYMKSSRFLPRPVFSKMAVWGNK | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2) . Participates in the formation of novel hepoxilin regioisomers .
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 25712
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
Q9TSM5 | MPMTLGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGTHKITQSNAILRYIARKHNLCGETEEEKIRVDILENQAMDVSNQLARVCYSPDFEKLKPEYLEGLPTMMQHFSQFLGKRPWFVGDKITFVDFLAYDVLDLHRIFEPKCLDAFPNLKDFISHFEGLEKISAYMKSSRFLPKPLYTRVAVWGNK | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Participates in the formation of novel hepoxilin regioisomers.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 25577
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
P04905 | MPMILGYWNVRGLTHPIRLLLEYTDSSYEEKRYAMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGSRKITQSNAIMRYLARKHHLCGETEEERIRADIVENQVMDNRMQLIMLCYNPDFEKQKPEFLKTIPEKMKLYSEFLGKRPWFAGDKVTYVDFLAYDILDQYHIFEPKCLDAFPNLKDFLARFEGLKKISAYMKSSRYLSTPIFSKLAQWSNK | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process . Participates in the formation of novel hepoxilin regioisomers (By similarity).
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 25914
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
P21266 | MSCESSMVLGYWDIRGLAHAIRLLLEFTDTSYEEKRYTCGEAPDYDRSQWLDVKFKLDLDFPNLPYLLDGKNKITQSNAILRYIARKHNMCGETEEEKIRVDIIENQVMDFRTQLIRLCYSSDHEKLKPQYLEELPGQLKQFSMFLGKFSWFAGEKLTFVDFLTYDILDQNRIFDPKCLDEFPNLKAFMCRFEALEKIAAYLQSDQFCKMPINNKMAQWGNKPVC | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers.
PTM: The N-terminus is blocked.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 26560
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
Q9BEA9 | MSCESSMVLGYWDIRGLAHAIRLLLEFTDTSYEEKRYTCGEAPDYDRSQWLDVKFKLDLDFPNLPYLMDGKNKITQSNAILRYIARKHNMCGETEEEKIRVDIIENQVMDFRTQLIRLCYSSDHEKLKPQYLEELPGQLKQFSVFLGKFSWFAGEKLTFVDFLTYDILDQNRIFEPKCLDEFPNLKAFMCRFEALEKIAAYIQSDQFFKMPINNKMAQWGNKPVC | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers (By similarity).
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 26604
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
Q8R5I6 | MPMTLGYWDIRGLAHAIRLLLEYTGSSYEEKRYTMGDAPDYDRSQWLSEKFKLGLDFPNLPYLIDGSHKITQSNAILRYIARKHNLCGETEEEKIRVDILENQAMDVSNQLARVCYSPDFEKLKVEYLEQLPGMVKLFSQFLGQRTWFVGEKITFVDFLAYDILDLHLIFEPTCLDAFPNLKDFVARFEVLKRISAYMKTSRFLRTPLYTKVATWGNK | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4. Can also catalyze the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator that possess potent anti-inflammatory and proresolving actions.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 25519
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
P46439 | MPMTLGYWDIRGLAHAIRLLLEYTDSSYVEKKYTLGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILRYIARKHNLCGETEEEKIRVDILENQVMDNHMELVRLCYDPDFEKLKPKYLEELPEKLKLYSEFLGKRPWFAGDKITFVDFLAYDVLDMKRIFEPKCLDAFLNLKDFISRFEGLKKISAYMKSSQFLRGLLFGKSATWNSK | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 25675
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
Q10SX7 | MAMRGDPKQRRASASAPHGGAAHHVADKLRRHSTFLLLLLLLWFALSLYLFLSATPPPPRPAFLPSTSTPRPALRIYVYDLPARFNRHWVAADARCATHLFAAEVALHEALLAYAGRAARPDDATLFFVPVYVSCNFSTDNGFPSLSHARALLADAVDLVRAQMPYWNRSAGADHVFVASHDFGACFHPMEDVAIADGIPEFLKRSILLQTFGVQGTHVCQEADHVVIPPHVPPEVALELPEPEKAQRDIFAFFRGKMEVHPKNISGRFYSKKVRTELLQKYGRNRKFYLKRKRYGNYRSEMARSLFCLCPLGWAPWSPRLVESVLLGCIPVIIADDIRLPFPSVLQWLDISLQVAEKDVASLEMVLDHVVATNLTVIQKNLWDPVKRKALVFNRPMEEGDATWQVLRELEILLDRSQRRHVESWKR | Function: Involved in the synthesis of glucuronoxylan hemicellulose in secondary cell walls.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 48393
Sequence Length: 427
Subcellular Location: Golgi apparatus membrane
EC: 2.4.-.-
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Q10N05 | MGSSTDHGGAGGRGKKGSGSQLWKKALLHSSLCFVMGFFTGFAPSSVSDWTSAAVSAGGVGSSHVVRSLHATGGAAVNRSLLAQAAAGAVDAGPQPLLVVVTTTESTPSAAGQRAAALTRMAHTLRLVPPPLLWVVVEANPDVAATARLLRTTGLMYRHLTYKDNFTVADAAAGKERHHQRNVALGHIEHHRLAGVVLFAGLGDTFDLRFFDQLRQIRTFGAWPVATMSQNERKVVVQGPACSSSSVAGWFSMDLSNATSPVAVGGAGYGAAAARPRELDVHGFAFNSSVLWDPERWGRYPTSEPDKSQDSVKFVQQVVLEDYSKVRGIPSDCSEVMAKLRTVSQQLEATWRSALAIINELLRACASVHGHVRSKLDSLYRSDFPQTEPETLICLIHDHASHYIYGGRFLSGDFC | Function: Involved in the synthesis of glucuronoxylan hemicellulose in secondary cell walls.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 44393
Sequence Length: 415
Subcellular Location: Golgi apparatus membrane
EC: 2.4.-.-
|
Q2QXP0 | MAVTGGGRPAVRQQAARGKQMQRTFNNVKITLICGFITLLVLRGTVGINLLTYGVGGGGGSDAVAAAEEARVVEDIERILREIRSDTDDDDDDEEEEPLGVDASTTTTTNSTTTTATAARRRSSNHTYTLGPKVTRWNAKRRQWLSRNPGFPSRDARGKPRILLVTGSQPAPCDDAAGDHYLLKATKNKIDYCRIHGIEIVHSMAHLDRELAGYWAKLPLLRRLMLSHPEVEWVWWMDSDALFTDMAFELPLARYDTSNLVIHGYPELLFAKRSWIALNTGSFLLRNCQWSLELLDAWAPMGPKGRVRDEAGKVLTASLTGRPAFEADDQSALIHILLTQKERWMEKVYVEDKYFLHGFWAGLVDKYEEMMERHHPGLGDERWPFVTHFVGCKPCGGYGDYPRERCLGGMERAFNFADNQVLRLYGFRHRSLASARVRRVANRTDNPLVNKEAALKMDAKIES | Function: Probable glycosyltransferase that may be involved in the biosynthesis of xyloglucan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 52150
Sequence Length: 463
Subcellular Location: Golgi apparatus membrane
EC: 2.4.-.-
|
Q75L84 | MGTAAVAAAERPKQRRSSHLWKKALLHFSLCFVMGFFTGFAPSSSSSWRAGSGGGGGVQPRHQLAASHVAVNQQVSLVPDAAAAEAAGVGNGAVVDVGDDEGGEGARRMLIVVTTTRGERRRRRGELLRLAHTLRLVRPPVVWVVVEPAADAAATAEVLRGTGVMYRHLAFRPEENFTTADAEAHAQRNAALAHVEKHRLSGVVHFADAAGVYDAHFFDEIRQIEAFGTWPVATMSAGEKKVVVEGPLCSDSKVVGWFSRDFNDGTTRAVTYNTEADLNPAGAAGTRAHTIDVSGFAFNSSILWDPERWGRPTSLPDTSQDSIKFVQEVVLEDRTKLKGIPSDCSQIMVWQYTMPMQVHAQTSTPKTHNRR | Function: Probable beta-1,4-xylosyltransferase involved in xylan biosynthesis in cell walls.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 40177
Sequence Length: 371
Subcellular Location: Golgi apparatus membrane
EC: 2.4.2.-
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Q6AT32 | MVSSRRNTGGIQRDGSLRDWSEFVDPSPSPKLLYSQSYVAMRGLLSSLVSMDFALLSSRLKSAWAAILSQRHTRSPERSKSRGLSCKRLAFHLFVCFMVGIFIGFMPFFSVDVSQKIVSENGRLPFDEGAVDRGMVDGKVKELETIVVEKEVDIIDESEVEESPPVPAMLDDEADFVESAPAIPDINDLDITVRKLLIIVTITTVRPQQAYYLNRLAHVLKTVQSPLLWLVVEWPDQSFQTAEILRSSGVMYRHLICRKNTTSVRKIAVCQRNTAIYHIKKHRLDGIMHFADEERSYMSDVFEEMRKIRRFGAWPVAIHTGIKYRVVLEGPICKGNRVTGWNTIQNIQKKSAVRRFPVGFSGFAFNSTMLWDPERWNRPPMDSVIVHSGGRGGLQESRFIEKLVKHERQIEGLPEDCNRVMVWNFNLEPPLLNVPPGWSLHKNLDAVIPVT | Function: Probable beta-1,4-xylosyltransferase involved in xylan biosynthesis in cell walls.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 51324
Sequence Length: 451
Subcellular Location: Golgi apparatus membrane
EC: 2.4.2.-
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