ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P58142 | MTGEAVSGQDVSNPGKSSWRVTVLGGGAWGTALALAMLRAGHKVRLFARDPQTVAAIGQGQNPRYLPGIAIAPGIEATSDIAAALSGADCVLAVTPAQSLRATLAVAKDNMPDGIPLVLCAKGIERDTGALLSAIVEEILPRNPVAALSGPSFATDVARGLPTAVVVAARDEALAADLAARFSAQNLRCYSSDDLIGVEIGGALKNVFAIAAGAVTGAGLGASAQAAMVTRGFVELRRIGAAFGARPETLMGLSGLGDLLLTCSSAQSRNFAYGLTLGQGKALAGLPLAEGVPTAAIAARIAVERGIDAPIIAAVAAILD... | 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
|
Q9R9L6 | MSGKSKSAPKIVVVGAGAFGTALSAVAAAKDKANVTLLARREEAAAECRRTGRNDAVLPGIPLPPGLVYSSQAAALEDADIVLFAMPSQAHRDAARSYGPAIGARAIVVTCAKGMEQSTGQLLTDVLEEELPGRRIGVLSGPGFAADIASGLPTAMVIAAPDTAIATELAEALSGRTFRLYPSADRTGVQLGGALKNVLAIACGIVEGAGLGDSARAALISRGLAEMSRFIVARGGEADTVRGLSGLGDLVLTATSHQSRNLRFGIALGKDGRAAAGSSELVEGAFAASVAARVAGALGIEMPVTEAVAAIVDGKLDVRS... | 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
|
Q7Y208 | MNSRPSNPTKLVIRSSTLLFCGVVLIHLFAAQIDAQRSTSRWQTLNGDAPLVIARGGFSGLYPDSSIAAYQLATLTSVADVVLWCDLQLTKDGLGICFPDLNLANASTIDRVYPNREKSYSVNGVTTKGWFPNDFSLTELQNFLLIRGILSRTDRFDGNGYLISTIEDVVTTLNREGFWLNVQHDAFYEQQNLSMSSFLLSVSRTVSIDFISSPEVNFFKKITGSFGRNGPTFVFQFLGKEDFEPTTNRTYGSILSNLTFVKTFASGILVPKSYILPLDDEQYLVPHTSLVQDAHKAGLQVYVSGFANDVDIAYNYSSDP... | 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
Subcell... |
Q9SZ11 | MRGLLRASSLLLCGVILIQLLAAQIHAQSKKPKSPWPTLTGDPPLVIARGGFSGLFPDSSYDAYNFAILTSVPDAVLWCDVQLTKDALGICFPDLTMRNSSSIEAVYPTRQKSYPVNGVPTSGWFTIDFSLKDLKDVNLIRGILSRSEKFDGNSNPIMTVQSVSTQMKPSFFWLNVQHDAFYAQHNLSMSSFLVAASKTVLIDFISSPEVNFFKKIAGRFGRNGPSLVFRFLGQDEFEPTTNRTYGSILSNLTFVKTFASGILVPKSYILPLDDQQYLLPHTSLVQDAHKAGLEVFVSGFANDIDIAHDYSFDPVSEYLS... | 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
Subcel... |
F4JEQ1 | MACPRVIFLILITFFILQTAFSSSWQTLSGKPPAVIARGGFSGMFPDSSIQAYQLVNITTSPDVMLWCDLQLTKDGVGICFPNLKLDNGSNVIRIDPHYKERFSVDFTWKELSDVKLAQGVVSRPYIFDDVSSILAIEEVAKLTASGLWLNIQDSAFYAKHNLSMRNSVVSLSRRLKVNFISSPGISFLKSMKNSVKPTVTKLIFRFLKQEHIEPFTNQSYGSLAKNLSYIRTFSSGILVPKSYIWPVDSALYLQPHTSLVTDAHKEGLQVFASEFANDFVIAYNYSYDPTAEYLSFIDNGNFSVDGFLSDFPVTPYRAI... | 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 | MLRFFILFSLFLHSSVAAPKTPAAAAAVPAKKWLTLNGQEPAVVARGGFSGLFPESSISANDLAIGTSSPGFTMLCNLQMTKDGVGLCLSDIRLDNATTISSVFPKAQKTYKVNGQDLKGWFVIDYDADTIFNKVTLVQNIFSRPSIFDGQMSVSAVEDVLGTKPPKFWLSVQYDAFYMEHKLSPAEYLRSLRFRGINVISSPEIGFLKSIGMDAGRAKTKLIFEFKDPEAVEPTTNKKYSEIQQNLAAIKAFASGVLVPKDYIWPIDSAKYLKPATTFVADAHKAGLEVYASGFANDLRTSFNYSYDPSAEYLQFVDNG... | 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 | MSWVRFTKTGVAVVATSAAAVLALDMTNERRFQRQVKDHFRTVHADRLAELNKRAPSALPTRKDILTNLSKGEEFDVLIIGGGATGAGVALDAQTRGLKTALVELDDFSSGTSSRSTKLIHGGVRYLQAAIMKLDLEQYRMVKEALFERHNLLEIAPHLSSPLPIMLPIYKLWQVPYYWSGIKAYDFVSGKRVLKNSFFINKSQALERFPMLRNESLKGALIYYDGQHNDARMNLAIILTAIRHGAACANHVRVEKLNKDETGKVIGAHVRDMVTGGEWDIKAKAVINATGPFTDSIRLMGDPETARPICAPSSGVHITL... | 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:... |
Q54QC1 | MNQLLSKSFKPLVVAGVAVIGISAFSGNRAYDEYRKERESISKKMINDLNENKITMFDYFQECKTLGRDEQLSKLNKLSKVYNKQKLNEQENQEELIDLDLIVIGGGATGTGVALDAQSRGMKVALFEKYDFSSGTSSKSTKLVHGGIRYLESAIMKLKPSELTLVKEALRERSNLLNNAPHLSRQLPIVIPAYSIFDASKFWIGCKLYDFFYPFNDIPKSYLQTSAQTYKEFPFLREGLVSSVVYYDGQHNDSRMNVSLALTAAQQGALTLNYTEVVELIKDDKINNNNKQQQLKGVVIRDRLTGKKYSVPAKCVVNAT... | 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:... |
P43304 | MAFQKAVKGTILVGGGALATVLGLSQFAHYRRKQMNLAYVKAADCISEPVNREPPSREAQLLTLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLQKAIMKLDIEQYRMVKEALHERANLLEIAPHLSAPLPIMLPVYKWWQLPYYWVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYGAATANYMEVVSLLKKTDPQTGKVRVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKMDDKDAAAICQPSAGVHIVMP... | 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: Poly... |
P32191 | MFSVTRRRAAGAAAAMATATGTLYWMTSQGDRPLVHNDPSYMVQFPTAAPPQVSRRDLLDRLAKTHQFDVLIIGGGATGTGCALDAATRGLNVALVEKGDFASGTSSKSTKMIHGGVRYLEKAFWEFSKAQLDLVIEALNERKHLINTAPHLCTVLPILIPIYSTWQVPYIYMGCKFYDFFAGSQNLKKSYLLSKSATVEKAPMLTTDNLKASLVYHDGSFNDSRLNATLAITAVENGATVLNYVEVQKLIKDPTSGKVIGAEARDVETNELVRINAKCVVNATGPYSDAILQMDRNPSGLPDSPLNDNSKIKSTFNQIA... | 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:... |
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
S... |
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... |
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 | MDSSKRHLLLILDGWGLADDPSVSAVEQADTPFVDHLYDEYPHGVLKASGLEVGLPDGQMGNSEVGHTNLGAGRVVYQEILRISKAIEDGSFFENDALVRAARHAKASDQKLHLMGCFSDGGVHSHLEHLYGLLELARREGLAPAQVNVHAFTDGRDTDPHGGVDYVEQFQKKADEIGVGRLASIVGRYYAMDRDERWARTERAYRLLTDGTGAAFDDPVTALKASYDDGVTDEFVEPRRIRADDADAFGDHGTRIEDGDAVVYYNFRSDRARQLTRAFTEADFDGFERERPDDLLFVTMSPYDDEFDLPVAFEKLNLEG... | 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-glyceral... |
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... |
Q58GE8 | MFKLAQRLPKSVSSLGSQLSKNAPNQLAAATTSQLINTPGIRHKSRSSAVPSSLSKSMYDHNEEMKAAMKYMDEIYPEVMGQIEKVPQYEEIKPILVRLREAIDYTVPYGKRFKGVHIVSHFKLLADPKFITPENVKLSGVLGWCAEIIQAYFCMLDDIMDDSDTRRGKPTWYKLPGIGLNAVTDVCLMEMFTFELLKRYFPKHPSYADIHEILRNLLFLTHMGQGYDFTFIDPVTRKINFNDFTEENYTKLCRYKIIFSTFHNTLELTSAMANVYDPKKIKQLDPVLMRIGMMHQSQNDFKDLYRDQGEVLKQAEKSVL... | 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... |
O05572 | MIPAVSLGDPQFTANVHDGIARITELINSELSQADEVMRDTVAHLVDAGGTPFRPLFTVLAAQLGSDPDGWEVTVAGAAIELMHLGTLCHDRVVDESDMSRKTPSDNTRWTNNFAILAGDYRFATASQLASRLDPEAFAVVAEAFAELITGQMRATRGPASHIDTIEHYLRVVHEKTGSLIAASGQLGAALSGAAEEQIRRVARLGRMIGAAFEISRDIIAISGDSATLSGADLGQAVHTLPMLYALREQTPDTSRLRELLAGPIHDDHVAEALTLLRCSPGIGKAKNVVAAYAAQAREELPYLPDRQPRRALATLIDHA... | 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... |
P32784 | MPAPKLTEKFASSKSTQKTTNYSSIEAKSVKTSADQAYIYQEPSATKKILYSIATWLLYNIFHCFFREIRGRGSFKVPQQGPVIFVAAPHANQFVDPVILMGEVKKSVNRRVSFLIAESSLKQPPIGFLASFFMAIGVVRPQDNLKPAEGTIRVDPTDYKRVIGHDTHFLTDCMPKGLIGLPKSMGFGEIQSIESDTSLTLRKEFKMAKPEIKTALLTGTTYKYAAKVDQSCVYHRVFEHLAHNNCIGIFPEGGSHDRTNLLPLKAGVAIMALGCMDKHPDVNVKIVPCGMNYFHPHKFRSRAVVEFGDPIEIPKELVAK... | 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 fatt... |
Q94B38 | MLSSIKPSSSSFSTAISGSVRRSIPTKLKFSPLLIIKNCHNQSFNANVVSHQKPLHISSASNFKREVKVEAYEADRSRPLDINIELPDEQSAQKLKIGIYFATWWALNVVFNIYNKKVLNAFPYPWLTSTLSLACGSLMMLVSWATRIADAPKTDLEFWKTLFPVAVAHTIGHVAATVSMSKVAVSFTHIIKSGEPAFSVLVSRFFMGETFPLPVYLSLLPIIGGCALAAITELNFNITGFMGAMISNLAFVFRNIFSKKGMKGKSVSGMNYYACLSMMSLVILTPFSIAVEGPQMWAAGWQNAVSQVGPNFVWWVVAQS... | 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 s... |
P36148 | MSAPAADHNAAKPIPHVPQASRRYKNSYNGFVYNIHTWLYDVSVFLFNILFTIFFREIKVRGAYNVPEVGVPTILVCAPHANQFIDPALVMSQTRLLKTSAGKSRSRMPCFVTAESSFKKRFISFFGHAMGGIPVPRIQDNLKPVDENLEIYAPDLKNHPEIIKGRSKNPQTTPVNFTKRFSAKSLLGLPDYLSNAQIKEIPDDETIILSSPFRTSKSKVVELLTNGTNFKYAEKIDNTETFQSVFDHLHTKGCVGIFPEGGSHDRPSLLPIKAGVAIMALGAVAADPTMKVAVVPCGLHYFHRNKFRSRAVLEYGEPIV... | 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 ... |
A0A098CZ12 | MGKPDIYNSSANVEKSPYYKAMQHRAPNVLTAVDKKAHGMRRRILSQGLSDSSTRAFGNTIKKHIERLCQKIEGHSDPNTQWSESYDMARWFSYLTFDIMADVVFGQPYNLLGNSEYRYVVDSIEGSNIRTGVLIQAPEAYTWRLDKRLFPASIRHRNTFVKFISSLVQERLTTKPLERDDIISHLLTAKDSETGQGFTKNEVAAESSTLIVAGTDTSSTALAATLFYLTQYPNMYRRAVAEVRSSFAKSQDVKLGRALNECVFTRACIEESMRLSPPAASALWRRVQVGGQTVDGHAIQAGCNIGVCIYAIHHNELYYP... | 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 seri... |
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 (GS... |
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 ... |
A1IIX2 | MNDMSHAPQPAQTKPHVRLVGRVAGVADLFRSSARQTEEARRVPASHIAALRGIGYFDIVKPRAFGGQGGEFAELVEANIELSAACASTGWVAGLLSAHQWLLAMFPEEAQADVWDENPDALLCGSYAPVKMAEAADGGYRLSGKWAFASGCENAQWSLCAAILPPQAKGRPVPAFLLVPASQYAIEDTWHVVGLAGTVSKTLVLDDVFVPKHRVLTFPDATSGHTPGGRFYAQEGLFNMPLLTGIPSCLASTGVGAAKGALAAYVDHVGGRVTRGAVAGGNNRMAEFPTIQLRVAEAAASVDAACEILLRDVARAQALS... | 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): 4... |
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), r... |
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), r... |
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 gasderm... |
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 ... |
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 | MQPFVYTTAPARIVFGTGSSVGVAEEIRRLGLSRALVLSTPHQKGDAEALAARLGPLAAGVFSDAAMHTPVEVTKRAVEAYRAAGADCVVSLGGGSTTGLGKAIALRTDAPQIVIPTTYAGSEVTPILGQTENGVKTTLRGPEILPEVVIYDAELTLGLPVGISMTSGLNAMAHAAEALYARDRNPIASMMAVEGLRAMIEALPGVRMEPQDTKARETALYGAWLCGTVLGAVGMSLHHKLCHTLGGSLDLPHAETHAVLLPYTIAYVEQAVPDQLAPLAALVGGRAGTGLYDFAARLGAPASLAALGVGGEDLDAMAEL... | 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 N... |
Q4WID9 | MKRKAEKQQATAPVSAFAARKARQQQARLLEPEKTAQNEPAVEPPSKRARRSPEEGAARQAANENDRVQTRRSARTKAETLSSAELAEKQPQESAAAARAQTAERTPPPEKGDADTFDAAEEEEEEEKEEDILERENGVGVIAVEDDAEGYESPADDVPQVQNFPLSKTRLNKSNIVSSDERTLCVRIKEKMTLVLLGHYDLWVKRGVISLMGAKLHPSPRLYRVYAPSTHSLPVIKCVAGVDGESEIEVKSCNSGIYRLRHLSPLYQRIWNGKHTAADKLTLKKVSASTKRTFSVLYTSSDDSWNRHLRPLHLEKQWSS... | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 92574
Sequence Length: 841
Subcellular Location: Nucleus
EC: 2.7.1.-
|
Q59U11 | MSAFAALKNNPFGESIFNNTSNGDNHSRDDVEEDEVVQYIANSSDEDDDDDNDDNDNDQGNEDNNLFPLEISAPVDTSISSTPAPILNSRITQSNYTPNESNLKFSDNHVTITLNPSEYIIISGQCNLKIIKGSIKINQCHCLTSEDNKSYNIIALQSQSLPIISHYTTPEMEEDGVTSVSIIQLENSFSGIENISQIEPAFKNLISGQPNVEEPSLFKNYSFDIVLTETNGGYGLDINSYWINELNLLKSNKDDPTPKIIMIIGNKNTGKSTFCKSLINELLLTNPNRPVSYLEIDPGQSEYSTPCALSLSEIVQAQFG... | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 77356
Sequence Length: 686
Subcellular Location: Nucleus
EC: 2.7.1.-
|
Q6FW56 | MAETDLNALAYKDSDSTDTSSSSSSDEEYQAEVKVSNQNEKQVDYDSDTDLNTDNKVSSVDAYKPCVGENLIIRDSNIIILLRAKEKLCLSGLFDLKIEKGGLLYNDIHFNASSKTYHYWHPLSNSIPEIKSSFYAGFEDVDISAFYAAYDISPNNDYETVLKISNHKSKSLIDGEILMPSLKSLWITKEDFLQKNGYTNFSFDIIMPATLQEITTLNISKSWTNCLQKLKFINQNSIHDTRIMVIGGKNSGKSTFLRSLVEKVLYSHDISDKSVSEMLYLDLDPGQPEFSHPDCISMTRLTSNDMNFGQSFGQASPEVL... | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 71688
Sequence Length: 630
Subcellular Location: Nucleus
EC: 2.7.1.-
|
P0CM79 | MSALAARRATAAAASPKPEQPESSIEEVSVSGALTLPSPKRRKTRQTSPKPRSKARYSDDVPTSRQFFQATESLAEQRTGRFSPSAPDSDGGTSSSSVGDSDEDMAQEDEFEDRREVDGERDQRKVSVAANMSSSGPFKSLDLMPVDITSQFNPKDNVNFCRITEGQLASAEMNDGHPGPGVIVSLARNESLTIAGLFLLTPLQNTLSIYSTALSPSMSSFPVYAPTSHPLPVISPASTQAPGKESDKTLLLIRENRCGIDGLRNGAVPGFSNIWLEDNGPWGLRGVHPVVGSFPVPVYPYCTPPSWSHAISSLSSSDVN... | 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 | MSAYAALQKMSGASSILYGINGESDNDESGTIGYLRNSSDEEVEAEEAEVPTTSTMAPTPNIIRTPSIVPKINSFICESNFIPNDDNFIVFHDHIIIGLKANEYILINGQSKMTIQRGAILINTGHYMFAHPNNCIPIIASQSQSLPIISSTQVVDRSGIKDSKTDENMHLFSSNYKSIIKLENLYTGLEKIGTYHPPFKRLFYSHAVIEDEDLTEYERLFKTYSFEIILRDRGCIGISIEKLWLNQIQLLISDIHEDLIPKTIMIIGNKNSGKSTLSKTLLNSLILANQNTVSYLDLDPGQSEFSMPYCLSLTNHSKPI... | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 77674
Sequence Length: 680
Subcellular Location: Nucleus
EC: 2.7.1.-
|
Q5B4D1 | MMKRKADRQTAAAAPVSAFAARKARLQQTQTQVQTVVASEKTTHTDVAAEPPSKRPRRSLQESQAQSTSEEDTKRTSKRSAAKTEKVQRVDSGTITRTRETRMKDSEIEVEDLEKERSSNEESEGEDAVEENAAGVVAVPAAEDGYESPADNTMTVVFPLSKIRLNKNNIVYSDEDTLCVRIQEKLSIVLIGQYDLWVKRGVVSVMGAKLHPSPRVYRVYAPSTHSLPVIKCVTGVNGAAEVEFKSCHSGITRLRDLSPLYQRLWNSGNTPADKLSLKAVGQDARRTFSVLHTSADDPLKRHLRPLHLEKQWSAAIKVLS... | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 89980
Sequence Length: 816
Subcellular Location: Nucleus
EC: 2.7.1.-
|
Q4IR18 | MSSNKKRRIDEKPMSALSALQARRREAAASPVQTTQTGSESDEKSVTTSVNPYQLLRKDSSQSTAPKTPKKNVVKDQYLPRGAESPASRSRGVVIASGNTDTLNPELAGASQKVVREYSSFRLSKQNHRVKTGGVVELNLSNSERFLVLGSFGIRVIQGEVSLAGATLYPSETIEWVHAPHCHAVPMLRTIDETILELHPDRNARGIRQLGRLSPLFRKIWNESPETNSSKTSKESTFEIIYTSEDAPKKCIIQKLVSPPEWNKKLSSLVATSRKKPSLSTLICGPKSAGKSTFSRLFLNGLLTDRSQKQGARSVVILDL... | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 79096
Sequence Length: 720
Subcellular Location: Nucleus
EC: 2.7.1.-
|
Q6CQ06 | MSEDILTYTANTDSDDSDVEQREIEKKYKTSSETPVVQLYDGDDYDNDDIRETNGNDFPNEEDESNQLYSPVVDMNFFTLSDECTEVIICLEKNQHLLICGQFNLQIIKGGITYNNVHYNSGYKNWEFWHPACNAISPIVSSFYAGWESKLFLNREYQHFTTQIESYDCVLKISNGCNITELSSLLPELRDMWGPLNISLLPGIARKQLTFNIISKISDSVRILDISTEWSTVIDEMRIFHANSSQDMRVMVIGGKNSGKSTLMRLLVQKFLHSNNDLSYEAIHYLDIDPGQPEYSPPESISWNKVDPKSMSLGQHLCQG... | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 72566
Sequence Length: 631
Subcellular Location: Nucleus
EC: 2.7.1.-
|
Q9UU96 | MVKRQRIESSNVPLSAFAVRQLTLSKAARKKDNSSGKKRSVSEEESQDKYEDEMKTEGEFPSYKHTLVQVVVPGVDHRTKLHSESSKNDSEITPDINRSKVNPQEYSEFSVASPQTISPSLPLNLDDETVSENVPHSPQSSNDAIPVIKITEENSFRVKDTLYVGLHKDQKLAMVGTFIFRSVRGKFQLFGATYSSACMSWFPLNAPLAFATPVFSAIDNALPAMQISEYEEDSLNLRSFAVPSYSPKEHEYELEPKDILPNFETVIAFRENENGLSKIARVLPFAKRLFSFKNLLQDASSISNNFEITPESWCSFSNQL... | 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 | MTKRKSALSALKPTKKQVISSEDSDPEVVVVTNPPLDSPDAEESFISITEEDEAVRQLSTFDFSAKNTKVVRDETRGRSRVFHGMKFKETIVLRGAYVVTVWSGVIHINGALVNINSPVDIPVFAPASHALPQIEAAAGAPETRESGDEDVMEALHQLEGSSVIVEIAAMPRRSENPLITVSNFGKMSSGNIVPFVRQLWHCSEDDGSNYSRIYNTASVVTKSQAAVIPGIYDEWAEVCDDIRRLKHSSTMVVGSQNTGKSTFCKYLSAFMTTKKTGTSVAFVDLDPSNCEFTAPGQVSVTVIGAGHLSPYSILGPSFTH... | 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 | MVIDSKQDLPQYTKDSGSESDSDSSNNFIVESPSIPSSKSATVVLNSEEYEDDEGDDLNGLDAELIDNITYEGDEDETMFVGLKEKQKLHLSGVFRLQVVKGGIVYNNVHYNASREILTFWHPLSQSIPTIDFSHFAGWQDTFFMPRNNRFKIRDEEFKSFPCVLRVFNSNHTGLLEAGHLYRDVNYLWKPKEPYFPLNERTTYHLLHESDRIQSLSVPGYWSTPLEKLYLSHKNAAYDTRIMVIGGKNSGKSTFLRLLLEKFTQDIRDSTTSQEELVYLDLDPGQPEYSLPDSISLNKILSSPISLGQHLCQGSNFQTL... | 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 produc... |
Q47878 | MSDIKQMIGKTFMEIADAIETGSFAGKVKVGITTLGSEHGVENLVKGAELAAKDAAGFDIVLIGPKVETSLEVVEVATEEEAHKKMEELLDSGYIHSCVTVHYNFPIGVSTVGRVVTPGMGKEMFIATTTGTSAAQRVEAMVRNALYGIITAKSMGIENPTVGILNLDGARAVERALKELAGNGYPITFAESLRADGGSVMRGNDLLGGAADVMVTDSLTGNIMMKVFSSYTTGGSYEGLGYGYGPGIGDGYNRTILILSRASGVPVAANAIKYAAKLAQNNVKAIAAAEFKAAKAAGLESILAGLSKDTKKASTEEEVK... | 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. ... |
Q9R4G7 | MRLEIGNIFIKDIQFGEQTKVENGVLYVNKDEMIKKLSVIEHIKSVDLDIARPGESVRITPVKDVIEPRVKVEGPGGIFPGVISKVETDGSGRTHVLKGAAVVTTGKVVGFQEGIVDMSGVGAEYTPFSKTLNLVVIAEPEDGIEQHRHEEVLRMVGLNAGVYIGEAGRSVTPDEVKVYETDTIFEGAAKYPNLPKVGYVYMLQTQGLLHDTYVYGVDAKKIVPTILYPTEVMDGAILSGNCVSSCDKNPTYVHCNNPMVEELYAMHGKEINFVGVIITNENVYLADKERSSDWTAKLCKFLGLDGAIVSQEGFGNPDTD... | 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 P... |
O86186 | MKKLKVVHYINNFFAGVGGEEKANIPPEMREGAVGPGMALAAALGDEAEVVATVICGDSYYGENMDSARKEILEMIKDAQPDAFVAGPAFNAGRYGVACGSIAKAVEEDLGIPSVTGMYVENPGVDMYRKDIQIIETGNSAADLRNSMPKLAKLVMKKAKGELVGPPEVEGYHMMGIRTNFFHEKRGSERAIDMLVNKLNGEKFETEYPMPVFDRVPPNPAVKDMSKVKVAIVTSGGIVPHDNPDRIESSSATRYGIYDITGMDSMSADDFTSIHGGYDRAFVVKDPNLVVPLDVMRDLEREGVIGELANYFVSTTGTGT... | 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... |
O69406 | MKLELGNFYVEEIVFGEKTSFKDGVLTINKQEALDYVMEDENITHAELHIVKPGDMVRLCPVKEAIEPRIKLDGRTYFPGVTDEELTRCGEGRTHALKGCSVLVVGKHWGGFQDGLIDMGGEGAKYTYYSTLKNIVLVGDTNEDFEKNEQQKKNKALRWAGHKLAEYIGKTVKDMEPQEVETYELEPVTQRSEEVTKLPGVVFVMQPQSQMEELGYNDMVYGWDMNRMVPTYMHPNEVLDGAIISGSFMPCSSKWSTYDFQNFPALKRLYAEHGKTVNFLGVIMSNLNVALQQKQRSALFVAQMAKSLGAQGAIVAEEGY... | 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 P... |
Q12068 | MSVFVSGANGFIAQHIVDLLLKEDYKVIGSARSQEKAENLTEAFGNNPKFSMEVVPDISKLDAFDHVFQKHGKDIKIVLHTASPFCFDITDSERDLLIPAVNGVKGILHSIKKYAADSVERVVLTSSYAAVFDMAKENDKSLTFNEESWNPATWESCQSDPVNAYCGSKKFAEKAAWEFLEENRDSVKFELTAVNPVYVFGPQMFDKDVKKHLNTSCELVNSLMHLSPEDKIPELFGGYIDVRDVAKAHLVAFQKRETIGQRLIVSEARFTMQDVLDILNEDFPVLKGNIPVGKPGSGATHNTLGATLDNKKSKKLLGFK... | 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 regulat... |
P19493 | MRIICRQIVLLFSGFWGLAMGAFPSSVQIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVENFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDFNTPMVTKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKI... | 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-gluta... |
Q61627 | MEALTLWLLPWICQCVTVRADSIIHIGAIFEENAAKDDRVFQLAVSDLSLNDDILQSEKITYSIKVIEANNPFQAVQEACDLMTQGILALVTSTGCASANALQSLTDAMHIPHLFVQRNPGGSPRTACHLNPSPDGEAYTLASRPPVRLNDVMLRLVTELRWQKFVMFYDSEYDIRGLQSFLDQASRLGLDVSLQKVDKNISHVFTSLFTTMKTEELNRYRDTLRRAILLLSPQGAHSFINEAVETNLASKDSHWVFVNEEISDPEILDLVHSALGRMTVVRQIFPSAKDNQKCMRNNHRISSLLCDPQEGYLQMLQISN... | 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 (... |
Q68Y21 | MKVFPAVLFLITFWSLEWEPVLPDSIIHIGAIFDESAKKDDEVFRMAVADLNLNNEILETEKITVSVEFVDGNNPFQAVQEACELMNRGILALVSSIGCMSAGSLQSLADAMHIPHLFIQRAPAGTPRSSCPPTTRAQPDDYTLFVRPPVYLNDVIFQVVMEYTWQKFIIFYDTDYDIRGIENFLDQTSQQGMDVSLQKVESNINMMITGMFRTMRVEELHRYRDTLRRAVLFMSPATAKAFITEVVETNLVAFDCQWIIINEEISDMDVQELVMKSIGRLTLVRQTFPLPQNTSQRCVRNNHRINTSLCDPKDPKAQML... | 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... |
O43424 | MEVFPFLLVLSVWWSRTWDSANADSIIHIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQSLADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLHDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDKVSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEINDVDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSTLCDPKDPFAQNM... | 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 lo... |
Q61625 | MEVFPLLLFLSFCWSRTWDLATADSIIHIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQSLADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNEVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDKVSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFISEVVETNLVAFDCHWIIINEEINDVDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSSLCDPKDPFAQNM... | 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 lo... |
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 r... |
B1VTI7 | MSSSPSPSPSSSSSSSASSSASSSPSSSSKLTWLDIRSVGEARAAIVQEALHHRVEALVADDPAHLADLPPTVAKVLLVVGKQIPEEFGEATVVVVDPSKHGVTPAELALKHPEIEFGRFVEIIDAPTLEDACESSRTEKWSVLLFRDPTKIPLEIVIAAAARASGSMVTIAQDLEEAEILFGVLEHGSDGVMMAPKTVGDAAELKRIAEAGIPNLNLTELRVVETSHIGMGERACVDTTTHFGEDEGILVGSHSKGMILCVSETHPLPYMPTRPFRVNAGAIHSYTLGRDERTNYLSELKTGSKLTAVDIKGNTRLVTV... | 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
... |
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
Sequen... |
O95267 | MGTLGKAREAPRKPSHGCRAASKARLEAKPANSPFPSHPSLAHITQFRMMVSLGHLAKGASLDDLIDSCIQSFDADGNLCRSNQLLQVMLTMHRIVISSAELLQKVITLYKDALAKNSPGLCLKICYFVRYWITEFWVMFKMDASLTDTMEEFQELVKAKGEELHCRLIDTTQINARDWSRKLTQRIKSNTSKKRKVSLLFDHLEPEELSEHLTYLEFKSFRRISFSDYQNYLVNSCVKENPTMERSIALCNGISQWVQLMVLSRPTPQLRAEVFIKFIQVAQKLHQLQNFNTLMAVIGGLCHSSISRLKETSSHVPHEI... | 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 antige... |
Q6NTL4 | MGTVGKKKDRPAHGCSTIPKLALELKQIIHSTTHPKVPAVTPLRVMMPLGKLSKGASLDELIQMCIQAFDLDGNMGQNNELLQIMLTMHGFLIPSTELLIKLRTLYQDAMQNRSFSFCLRICYFIRYWITELWVMFKMDAKLTQTMEEFQELVRSHGEELHWRLIDTAQINSRDWSRKLTQRIQSNCSKKRKVSLLFDHLEPQELAEHLTYLEFKAFRRISFSDYQNYIVNGCVKDNPTMERSIALCNGISQWVQLMVLSRPTPQLRAEVLTKFIHVAQKLHQLQNFNTLMAVIGGLCHSSISRLKDTSSHVSHDVTKVL... | 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... |
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
|
B7GIK0 | MNFTKSEQLYQEALEHIVGGVNSPSRSYKAVGGGAPVVMERAQGAYFWDVDGNKYIDYLAAYGPIITGHAHPHITKAIQHAAENGVLYGTPTPYEITFAKMLKEAIPSLEKVRFVNSGTEAVMTTIRVARAYTGRDKIVKFAGCYHGHSDLVLVAAGSGPSTLGTPDSAGVPKSIAQEVITVPFNDVDAFKQAMDRWGNEVAAVLVEPIVGNFGIVEPKPGFLQAINDIAHAVGALVIYDEVITAFRFMYGGAQNLLGIEPDLTALGKIIGGGLPIGAYGGRKDIMEQVAPLGPAYQAGTMAGNPASILAGIACLEVLQQ... | 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
|
P42799 | MSATLTGSGTALGFSCSSKISKRVSSSPASNRCCIKMSVSVDEKKKSFSLQKSEEAFNAAKNLMPGGVNSPVRAFKSVGGQPVLIDSVKGSKMWDIDGNEYIDYVGSWGPAIIGHADDEVLAALAETMKKGTSFGAPCLLENVLAEMVISAVPSIEMVRFVNSGTEACMGVLRLARAFTNKEKFIKFEGCYHGHANAFLVKAGSGVATLGLPDSPGVPKAATSDTLTAPYNDLEAVEKLFAAHKGEISAVILEPVVGNSGFIPPTPEFINGLRQLTKDNGVLLIFDEVMTGFRLAYGGAQEYFGITPDLTTLGKIIGGGL... | 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 M... |
Q3B1A1 | MPTHTRSAELFEKAKKFIPGGVNSPVRAFKSVGGNPIFMAKGQGAYMTDVDGNTYLDYVGSWGPFILGSMHPRITAALEHTLTKIGTSFGTPIEMEIEIAELLTKIVPSIEMVRMVNSGTEATMSAVRLARGCTGRDKIIKFEGCYHGHGDSFLIKAGSGALTLGAPDSPGVTKGTAEDTLNAKYNDIKSVELLVAENKGNIAAIIIEPVAGNTGVIPAKKEFLQALRDLCDREGIVLIFDEVMCGFRVALGGAQELYGITPDLTTMGKIIGGGLPVGAFGGKRSLMENVAPLGGVYQAGTLSGNPLALTAGIETLKILM... | 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
|
A1BJG8 | MLQHTKSAELFEKAKQFIPGGVNSPVRAFKSVGGTPIYMAKGRGAYLTDVDGNSYLDYVGSWGPFILGSMHPRITAALEYTLKNIGTSFGTPIEMEIEIAELLCKIVPSLEMVRMVNSGTEATMSAVRLARGYTGRDKIIKFEGCYHGHGDSFLIKAGSGALTLGAPDSPGVTKGTALDTLNATYNDIESVKLLVEENKNNIAAIIIEPVAGNTGVIPAKPGFLADLRNLCDQNGIVLIFDEVMCGFRVALGGAQSLYGVTPDLTTMGKIIGGGLPVGAFGGKRKIMERVAPLGDVYQAGTLSGNPLALTAGLETLKILM... | 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
|
Q9JRW9 | MLNCSNQKHTVTFEEACQVFPGGVNSPVRACRSVGVTPPIVSSAQGDIFLDTHGREFIDFCGGWGALIHGHSHPKIVKAIQKTALKGTSYGLTSEEEILFATMLLSSLKLKEHKIRFVSSGTEATMTAVRLARGITNRSIIIKFIGGYHGHADTLLGGISTTEETIDNLTSLIHTPSPHSLLISLPYNNSQILHHVMEALGPQVAGIIFEPICANMGIVLPKAEFLDDIIELCKRFGSLSIMDEVVTGFRVAFQGAKDIFNLSPDITIYGKILGGGLPAAALVGHRSILDHLMPEGTIFQAGTMSGNFLAMATGHAAIQL... | 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
|
A6Q2X6 | MLSKSEAAYKEALRYIPGGVDSPVRAFKSVGGVPPFIDRGEGAFLYDIDGNRYIDYVQSWGPLIFGHADKETLEAVCEQAQKGLSFGTPTLLETELAREIVELFDNIDKIRFVSSGTEAVMSAIRLARGYTGRDDIVKFEGCYHGHSDSLLVSAGSGAATFGNPSSPGVPADFTKHTLLARYNDIESVKRCFQASDNIACVIIEPIAGNMGLVPAEEEFLQDLRKLCDEHGALLIFDEVMSGFRASLKGAQGFTSVVPDMVTFGKVIGGGMPVGAFGARAEIMAHLSPEGPVYQAGTLSGNPVAMVAGLSVIRRLKNDPS... | 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
|
Q5YP79 | MSASPRATHASAAASARLFDRAAQVIPGGVNSPVRAFRSVGGTPRFIASADGYTLTDADGNEYVDLVCSWGPMILGHAHPAVVDAVRRAATGGLSFGAPTEAEVELAEHIVARVAPVDRVRLVNSGTEATMSAVRLARGFTGRTKIIKFAGCYHGHVDALLADAGSGVATLGLPTSPGVTGAQAADTIVLPYNDLDAVAAAFEANPGEIACVITEAAAGNMGAVAPLPGFNAGLRELTENHGALLIMDEVMTGFRVSRSGWYGREGVAGDLYTFGKVMSGGLPAAAFGGRAEVMNQLAPLGPVYQAGTLSGNPVAVAAGL... | 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
|
B2T6C2 | MSRNETLFERAQRTIPGGVNSPVRAFRSVGGTPRFIERAQGPYFWDADGQRYIDYIGSWGPMILGHVHPEVLEAVQRVLGNGFSFGAPTESEVEIAEEICKLVPSIEQVRMVSSGTEATMSALRLARGFTNRSRIVKFEGCYHGHADSLLVKAGSGLLTFGNPTSAGVPADIAKHTTVLEYNNVAELEEAFKAFGNEIASVIVEPVAGNMNLVRATPEFLQALRRLCTEHGSVLIFDEVMCGFRVALGGAQEVYGITPDLTCLGKVIGGGMPAAAFGGRRDIMAHLAPLGGVYQAGTLSGNPIAVAAGLKTLQLIQAPGF... | 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
|
Q6MAC7 | MISRPISQQIYSNLNRVIPGGVNSPVRACANMGQIPMIIDHAYRDTLVDVDGKTYVDYCGSWGALIHGHAHPSILEAVQQRMKKGTSFGITTSIEGELAQEVIKLIDSVEKIRFVSSGTEATMSAVRLARGYTNKEFIVKFNGNYHGHADFFLVQAGSGVLEVSPSASSAGIPADIVKQTLCLPYNDIEACRQIFHHSDYRHKIAAIILEPIAGNMGVIPASQEFMQFLRKETLAMGALLIFDEVMTGFRVALKGAQDIYPVEPDLTCFGKIIGGGFPAAAFGGREEIMNLLAPLGSVYQAGTLSGNPIAMEAGLQSLRL... | 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
|
Q9KUG5 | MSKFAERLQTVANKPEVFQKFSRGLERESLRYTPEGALTQTPHPKALGAALTHRWITTDFAESLLEFITPVSHEVDTLLAQMSDIHHFAQTKLGDEKLWPLSMPCYVGSEEGIVLAQYGSSNTGKMKTLYREGLKRRYGSLMQIISGVHFNFSFPESFWDALFGEQEESARQASKSAAYFGVIRNYYRFGWLIPYLFGASPALCSSFLQGRKTDLPFESIGKTLYLPYATSLRLSDLGYTNSAQSVLQIGFNSIEQYLQGLNEAIRTPSAEFAKLGVKVEGEYRQLNSNVLQIENELYAPIRPKRVTQSGERPSQALARA... | 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
|
Q8D2V5 | MIPKVSKIIPWIKDNKKFLKKTYKGIERESLRIDIDGNISKKPHPIIFGSPLTHNWITTDFSESLLELITPVSNSKKYTINFLNDLHIFIIKNLINENLWPMSMPCKINNDSSIIIAQYGNSKLGRTKTIYRNGLKNRYGAKMQIISGVHYNFSFHKDFWKKYNNFYKIQDKFSSIGYFNLIRNYYRFGWIIPYFFGASPIAHSSFFKGLNTDLIFKKNKFGDIYLPFSTSLRLSEIGYINKVQKKIKLKFNNIEEYVDIVKKAMKTPYLNYKKIELKNNEKNLQINVNLLQKENELYSHVRPKRSLNKNKYKLEDLIYK... | 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
|
P32477 | MGLLALGTPLQWFESRTYNEHIRDEGIEQLLYIFQAAGKRDNDPLFWGDELEYMVVDFDDKERNSMLDVCHDKILTELNMEDSSLCEANDVSFHPEYGRYMLEATPASPYLNYVGSYVEVNMQKRRAIAEYKLSEYARQDSKNNLHVGSRSVPLTLTVFPRMGCPDFINIKDPWNHKNAASRSLFLPDEVINRHVRFPNLTASIRTRRGEKVCMNVPMYKDIATPETDDSIYDRDWFLPEDKEAKLASKPGFIYMDSMGFGMGCSCLQVTFQAPNINKARYLYDALVNFAPIMLAFSAAAPAFKGWLADQDVRWNVISGA... | 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
Sequenc... |
Q8ZBU2 | MIPDVSHALTWLEAHPKALKGIRRGIERETLRVTADGHLASTGHPESLGAALTHQWITTDFAEALLEFITPVDGDIDHLLTFLRDIHRYTARKLGDERMWPLSMPCFIEAEQDIELAKYGSSNIGRFKTLYREGLKNRYGALMQTISGVHYNFSLPLEFWQAWAGVTDEQSGKEEISAGYFRLIRNYYRFGWVIPYLFGASPAICSSFLQGRETALPFERNGKGMCYLPYATSLRLSDLGYTNKSQSNLGITFNDLHTYVDALKRAIQTPSEEYVALGLKDGDRHLQLNTNVLQIENELYAPIRPKRVTRAGESPSDALL... | 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
|
Q8XK30 | MVNLDKGLLKIIKDESLEDYFIKANFGLEKENVRVTESGNLALTPHPKAFGDREKNAYIKTDFSESQLEMVTPVCNTLEEVYSFICNLNKVVSLEIMKNGEFLWPQSNPPILPREEEIPIAKLSNREDELYRENLSYKYGKKKQVISGIHYNFSFKEEFIKLLYKELKVEKDFREFKDDIYLRMARNFQKYHWLLIYLTGASPVFHESYIEEIKEEGEKLGEDSYYIKDDTSLRNSSYGYKNKKDYYVSYNSIEEYASDIKNLVKDKEIQSIKEYYNPIRLKSLGSEDMLESLLHKGIDYLEVRLLDLDPLSIQGVSKET... | 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: ... |
Q6ANW2 | MAFSKNILDSLPPLISKQIFEGFFGFEKENIRVDSRGKLALTPHPRELGEKTSHPYITTDFSESQIEIITPPLPSIAESLGFLETLHDLVSIELKDEYLWPQSAPPILPEREEDIPIAHFGGEFREQEEYRLQLAKIYGRKRQMFSGIHFNISLPERFLELLHEEGKQEQPFAEFREDIYMKTVRNFLRHRWFLICLLGASPVIHKSYRKHCIDMLSPFAKDAYHFPYATSIRNNICGYRNTQDFHLNYSTLTDYRESLQELVEKKVLRDIRENYAPIRIKTTTDPKRINHLEIRLLDLNPFFKTGVNPLHAEIIHIFLI... | 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: ... |
Q82ZG8 | MNYRELMQKKNVRPYVLMARFGLEKENQRSTREGLLATTEHPTVFGNRSYHPYIQTDFSETQLELITPVANSGTEMLRFLDAIHDVARRSIPEDEMLWPLSMPPQLPTKDEEIKIAKLDQYDAVLYRRYLAKEYGKRKQMVSGIHFNFEYDQALIQQLYDEQSEVTDCKQFKTKVYMKVARNFLRYRWLITYLFGASPVSEDRYFRVYDDQPQEPVRSIRNSTYGYRNHDNVKVSYASLERYLEDIHRMVENGLLSEEKEFYAPVRLRGGKQMSDLPKTGIRYIELRNLDLNPFSRLGIVEDTVDFLHYFMLYLLWTDEK... | 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: ... |
Q88UW5 | MELDAVGKAIVQYHLVPLVHQANLGLEVTMHRVDAHGHLATTAHPQAFGSAQQNHQLRPGFSASALKFTTPVRRDIPALMAYLKGLNTAARRSLDADERLWPLSSTPVLPDDLTNVPLADVDQVSYQRRRDLARKYELQRLMTTGSHVNMSLNEALFTRLYTETFHQQYHSYVDFRNAIYLKVAQGLVRMNWLIQYLFGASPRLAVTDTTSRPQRSSVQHPDGRYSQVTGDYTSIDRYVAKLTAAVRQQQLLSVNDFDGPVRLRSNGQLAMMARQGVYYLEYRGLDLDPTSPVGVDANAVAFVRLLASYFVMMPALPAKM... | 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 fr... |
Q8Y3R3 | MLDSFKEDPNLRKLLFSGHFGLEKENIRVTSDGKLALTPHPAIFGPKEDNPYIKTDFSESQIEMITPVTDSIDSVYEWLENLHNIVSLRSENELLWPSSNPPILPAEEDIPIAEYKTPDSPDRKYREHLAKGYGKKIQLLSGIHYNFSFPEALIDGLYANISLPEESKQDFKNRLYLKVAKYFMKNRWLLIYLTGASPVYLADFSKTKHEESLPDGSSALRDGISLRNSNAGYKNKEALFVDYNSFDAYISSISNYIEAGKIESMREFYNPIRLKNAHTDQTVESLAEHGVEYLEIRSIDLNPLEPNGISKDELDFIHLF... | 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: ... |
Q65RX0 | MNIQQIVKEKGLGLLFRQGTVGIEKESQRVHADGSIVTSEHPKAFGNRSYHPYIQTDFAESQLELITPPNKKIEDTLRWLSALHEVTLRTIDENEYIFPMSMPAGLPPEQEIRVAQLDNAADVAYREHLVASYGKAKQMVSGIHYNFQLDPKLVETLFNAQTDYKSAVDFQNNLYLKMAKNFLRYQWIPLYLLSATPTVEANYFKDGSPLKPNQYVRSLRSSKYGYVNAPDIIVSFDSIEKYVETLEHWVNSGRLIAEKEFYSNVRLRGAKKAREFLHTGIQYLEFRLFDLNPFEAYGINLKDAKFIHHFILLMIWLEET... | 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: ... |
Q9LWN0 | MEAPPGPEPMELDAPPPPAAVAAAAATAGISEKVLQKKEEGGGDAVTGHIISTTIGGKNGEPKRTISYMAERVVGTGSFGIVFQAKCLETGETVAIKKVLQDRRYKNRELQLMRAMEHPNVICLKHCFFSTTSRDELFLNLVMEYVPETLYRVLKHYSNANQRMPLIYVKLYIYQLFRGLAYIHTVPGVCHRDVKPQNVLVDPLTHQVKLCDFGSAKVLVPGEPNISYICSRYYRAPELIFGATEYTTSIDIWSAGCVLAELLLGQPLFPGESAVDQLVEIIKVLGTPTREEIRCMNPNYTEFKFPQIKAHPWHKIFHKR... | 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(+) + ... |
Q60EZ2 | MDQPAPAPEPMLLDAQPPAAVACDKKQQEGEAPYAEGNDAVTGHIISTTIGGKNGEPKRTISYMAERVVGTGSFGIVFQAKCLETGETVAIKKVLQDRRYKNRELQLMRAMDHPNVISLKHCFFSTTSRDELFLNLVMEYVPETLYRVLKHYSNANHRMPLIYVKLYMYQLFRGLAYIHTVPGVCHRDVKPQNVLVDPLTHQVKLCDFGSAKTLVPGEPNISYICSRYYRAPELIFGATEYTTSIDIWSAGCVLAELLLGQPLFPGESAVDQLVEIIKVLGTPTREEIRCMNPNYTEFRFPQIKAHPWHKVFHKRMPPEA... | 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 res... |
P49840 | MSGGGPSGGGPGGSGRARTSSFAEPGGGGGGGGGGPGGSASGPGGTGGGKASVGAMGGGVGASSSGGGPGGSGGGGSGGPGAGTSFPPPGVKLGRDSGKVTTVVATLGQGPERSQEVAYTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDELYLNLVLEYVPETVYRVARHFTKAKLTIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIF... | 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 pri... |
Q2NL51 | MSGGGPSGGGPGGSGRARTSSFAEPGGGGGGGGGGPGGSASGPGGTGGGKASVGAMGGGVGASSSGGGPSGSGGGGSGGPGAGTSFPPPGVKLGRDSGKVTTVVATVGQGPERSQEVAYTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDELYLNLVLEYVPETVYRVARHFTKAKLITPIIYIKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIF... | 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 pri... |
P49841 | MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRL... | 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/CR... |
Q9WV60 | MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRL... | 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/CR... |
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: gluta... |
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: glutath... |
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 a... |
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 a... |
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-subs... |
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-docos... |
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 | MAMRGDPKQRRASASAPHGGAAHHVADKLRRHSTFLLLLLLLWFALSLYLFLSATPPPPRPAFLPSTSTPRPALRIYVYDLPARFNRHWVAADARCATHLFAAEVALHEALLAYAGRAARPDDATLFFVPVYVSCNFSTDNGFPSLSHARALLADAVDLVRAQMPYWNRSAGADHVFVASHDFGACFHPMEDVAIADGIPEFLKRSILLQTFGVQGTHVCQEADHVVIPPHVPPEVALELPEPEKAQRDIFAFFRGKMEVHPKNISGRFYSKKVRTELLQKYGRNRKFYLKRKRYGNYRSEMARSLFCLCPLGWAPWSPR... | 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.-.-
|
Q10N05 | MGSSTDHGGAGGRGKKGSGSQLWKKALLHSSLCFVMGFFTGFAPSSVSDWTSAAVSAGGVGSSHVVRSLHATGGAAVNRSLLAQAAAGAVDAGPQPLLVVVTTTESTPSAAGQRAAALTRMAHTLRLVPPPLLWVVVEANPDVAATARLLRTTGLMYRHLTYKDNFTVADAAAGKERHHQRNVALGHIEHHRLAGVVLFAGLGDTFDLRFFDQLRQIRTFGAWPVATMSQNERKVVVQGPACSSSSVAGWFSMDLSNATSPVAVGGAGYGAAAARPRELDVHGFAFNSSVLWDPERWGRYPTSEPDKSQDSVKFVQQVVL... | 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 | MAVTGGGRPAVRQQAARGKQMQRTFNNVKITLICGFITLLVLRGTVGINLLTYGVGGGGGSDAVAAAEEARVVEDIERILREIRSDTDDDDDDEEEEPLGVDASTTTTTNSTTTTATAARRRSSNHTYTLGPKVTRWNAKRRQWLSRNPGFPSRDARGKPRILLVTGSQPAPCDDAAGDHYLLKATKNKIDYCRIHGIEIVHSMAHLDRELAGYWAKLPLLRRLMLSHPEVEWVWWMDSDALFTDMAFELPLARYDTSNLVIHGYPELLFAKRSWIALNTGSFLLRNCQWSLELLDAWAPMGPKGRVRDEAGKVLTASLT... | 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 | MGTAAVAAAERPKQRRSSHLWKKALLHFSLCFVMGFFTGFAPSSSSSWRAGSGGGGGVQPRHQLAASHVAVNQQVSLVPDAAAAEAAGVGNGAVVDVGDDEGGEGARRMLIVVTTTRGERRRRRGELLRLAHTLRLVRPPVVWVVVEPAADAAATAEVLRGTGVMYRHLAFRPEENFTTADAEAHAQRNAALAHVEKHRLSGVVHFADAAGVYDAHFFDEIRQIEAFGTWPVATMSAGEKKVVVEGPLCSDSKVVGWFSRDFNDGTTRAVTYNTEADLNPAGAAGTRAHTIDVSGFAFNSSILWDPERWGRPTSLPDTSQ... | 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.-
|
Q6AT32 | MVSSRRNTGGIQRDGSLRDWSEFVDPSPSPKLLYSQSYVAMRGLLSSLVSMDFALLSSRLKSAWAAILSQRHTRSPERSKSRGLSCKRLAFHLFVCFMVGIFIGFMPFFSVDVSQKIVSENGRLPFDEGAVDRGMVDGKVKELETIVVEKEVDIIDESEVEESPPVPAMLDDEADFVESAPAIPDINDLDITVRKLLIIVTITTVRPQQAYYLNRLAHVLKTVQSPLLWLVVEWPDQSFQTAEILRSSGVMYRHLICRKNTTSVRKIAVCQRNTAIYHIKKHRLDGIMHFADEERSYMSDVFEEMRKIRRFGAWPVAIHT... | 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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