ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8XPC4 | MNPVAFSIGSFEVRWYGIIIALGILIAMTLVSINAKKKNLNFDVILDLFLWCFPFAIIGARAYYVLFELENYHSFWDMINIRQGGLAIHGGIIGAFLTAFIYCKVKKVDFLAYADIVAPAFILAQGIGRWGNFFNQEAHGGQVTSEFISKFPEFIQRGMYINGAYYHPTFLYESIWDIFVAILLMIILYNITDRYKGVVISAYISLYSLGRFFIEGLRTDSLYFMNIRVAQLVSLLGIIIGIVAIIIIVSRGKKKRKGIFIN | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q9S2U8 | MELAFIPSPSRGVLHLGPVPLRGYAFCIIIGVFVAVWLGNKRWVARGGRPGTVADIAVWAVPFGLIGGRLYHVITDYQLYFSEGRDWVDAFKIWEGGLGIWGAIAFGAVGAWIGARRRGVPMPAYADAVAPGIALAQAIGRWGNWFNQELYGKATDLPWAVEITSTADGRVPGTYHPTFLYESLWCIGVALLVIWADRRFKLGHGRAFALYVAAYCAGRFWIEYMRVDDAHHILGLRLNNWTALFVFLLAVLYIVLSARKRPGREAVVEPGAETAAGDSGSAADKDVKGTKDAEDAEGAEDGAEKTDASGATEAPEDTSG... | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q74NQ3 | MNLLSIQPLNRIAIQFGPLTVYWYGIIIGIGILLGLILATREGKKLQVPSNTFTDLVLYALPISILSARIYYVLFEWAYYKNHLNEIFAIWNGGIAIHGGLIGAIVTTIVFTKKRNISFWKLADIAAPSLILGQAIGRWGNFMNQEAHGGPVSRTFLESLRLPDIIINQMYINGSYYHPTFLYESIWNIIGFVTLLILRKGSLKRGEIFLSYLIWYSIGRFFVEGLRTDSLMLTSSLRMAQVMSISLIIISLLLMIYRRRKGLATTRYNELNNNALE | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q8XHH1 | MRIVLGEIFGLKIYSYGFMIGLGIICATLLFLKRGTQRGYNEDKLFNATILTVISGILGGKILYIITEWKTVMQDPSLIFRDFGNGFVIYGAIIGGALGIALCSLKNKWNVLELADLVVPGLALAQGFGRIGCLLAGCCYGAETTSSIGIIFPADSLAPAGVPLYPTQIFSSIFDFALGLFLLWYGNKNKEKGKTMSMYMIIYSIGRFFVEFLRNDPRGSVGLLSTSQFISIFILIGGILLYNINKLKGRKETGEK | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q9FBW3 | MDLAYLPSPSTGVLHLGPIPLRAYAFCIILGVFAAVWLGNRRWVARGGKQGVIADVTLWAVPFGLVGGRLYHVFTSPDAYFGERGEPVRALYVWEGGLGIWGAIALGAVGAWIGCRRHRIPLPAFADAVAPGIVLAQAIGRWGNWFNQELYGRPTTLPWGLEIDRAHRPAGTLDIATYHPTFLYESLWNIGVAALILWAAKRFPLGHGRTFALYVAAYTVGRFGTEYLRIDEAHTFLGLRLNNWTSVLVFLGAVACLVVSAHRHPGIENVARLQGAGADGRTDDPRPADASVGLASGPPGNSTPRRATESWNVRNRS | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
P57033 | MQNHVISLASAAERRAHITDTFGVRGIPFQFFDALMPSERLEQAMAELVPGLSAHPYLSGVEKACFMSHAVLWKQALDEGLPYIAVFEDDVLLGEGAEKFLAEDAWLQERFDPDSAFIVRLETMFMHVLTSPSGVADYCGRAFPLLESEHWGTAGYIISRKAMWFFLDRFAALPSEGLHPVDWMMFGNPDDRERMPVCQLNPALCAQELHYAKFHDQNSALGSLIEHDRCLNSKQQRRDSPANTFKHRLIRALTKISREREKRRQRREQLIGKIIVPFQ | Function: Adds the second galactose to the lacto-N-tetraose chain in lipooligosaccharide (LOS).
Sequence Mass (Da): 31904
Sequence Length: 279
Pathway: Glycan metabolism; lacto-N-neotetraose biosynthesis.
EC: 2.-.-.-
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Q51116 | MQNHVISLASAAERRAHIADTFGRHGIPFQFFDALMPSERLEQAMAELVPGLSAHPYLSGVEKACFMSHAVLWKQALDEGLPYITVFEDDVLLGEGAEKFLAEDAWLQERFDPDTAFIVRLETMFMHVLTSPSGVADYCGRAFPLLESEHWGTAGYIISRKAMRFFLDRFAALPPEGLHPVDLMMFSDFFDREGMPVCQLNPALCAQELHYAKFHDQNSALGSLIEHDRLLNRKQQRRDSPANTFKHRLIRALTKISREREKRRQRREQFIVPFQ | Function: Adds the second galactose to the lacto-N-tetraose chain in lipooligosaccharide (LOS).
Sequence Mass (Da): 31578
Sequence Length: 275
Pathway: Glycan metabolism; lacto-N-neotetraose biosynthesis.
EC: 2.-.-.-
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A1TMB0 | MLMYPHIDPIALQIGPLAIHWYGLTYLAAFGLFMFLGTRRLRHEPYASLTGAQAWTRKDVEDILFLGVLGVVVGGRLGYCLFYKPGYYLSHPLEIFYIWQGGMSFHGGLLGVIASMVWFARSRHRPWLQVADFVAPCVPTGLAAGRVGNFINGELWGRFCDPSLPWGMVFPQSGSMLPRHPSQVYQFLMEGLLLFVLLWLYARRERRQGEVAAAFLVGYGCFRFIAEYFREPDAFLGILSLGMSMGQWLCVPMIVAGVLLWVWARRQPAR | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q6FER4 | MLTYPNIDPVALSLGPLKVHWYGLMYLLAFLCAWGLASYRAKQRDSWTSEMVSDLVFYGALGVVLGGRVGYVLFYEFDKFLANPIWLFQVWTGGMSFHGGFIGVMLAMILWCRKYQKTWFETLDFIAPCVPTGLMFGRIGNFIGAELYGREVQDPNYPFGMIFPTDPFHLVRHPSQIYQAICEGLLLFILLWWFSSKPRPRMAVSALFLMGYGVARFVVEFFREPDADQGFILFGWMTKGQILTVPMLLIGLWMIWYAYQRKVYDWGPLKTHK | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q6A8N5 | MRHRRRPGGRSTAGGTPVSQLSIPSPSIEAFHLGPLTIHIYALCILAGIVVAYISGGRRYQARGGKQEQFEELCALAVIAGIIGGRLYHVITDHQLYFGPGRTWYHCFFIWQGGLGIWGAISLGGLAIWLYCRRKGIRFASVADSLAPGILAAQAIGRLGNWFNQELFGRPTSLPWGLEIDLSHRPAGYLQYATFHPTFLYELVWSLVGAVFLLWVDRRWTLDHGRLFTLYVAIYTFGRFWVERLRIDPAHHVGQWRLNDVTALVVFTGAVVILIVLQRRYGKGDEHSSCPAHKTR | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q3Z7W0 | MFEINVDPVAFSIGSLVVKWYGIMMALGVIALVSWIFWRIKRGADISYDTVLTAAIIAIPSGIIFSKLLHVIDAWEYYSLNPGAILSGEGLTIFGAIIGATIGLWIYSRYSHFNLGYLLDVAVPGILLGQAIGRVGCLLNGCCYGEYGGSGCSVIYTNPASAAPYGVEVVPTQAYEIIFLLCLFAFSLFIAKKLRPDGQLFLLYISLYAAWRVAIGFVRVNDDFALGLEQAQVVGLILIALAVPFFIYRQRKQKEADKNT | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q9RW62 | MPRRGPFLALFAGCVSRGASRSPPGHTLTRRPMDPVFLQIGNFTIAWYGVLMMLGIAAGYWLGLKLARERGLNADLFERMILWMLFWGFVGARLVFVLTSWHIFEGIPFPRVLLDIVNLRNGGISIHGGLIGGVLTLIYFARRYRLNFYQYADLAVPGVAFGIIGGRLGNIMNGTDTVGRVTGWPIGYHWPASARAFHEGMCRPNPNPDMDLSKYCHEVGGQIMMTAPVHFTQLYGVIIGIILAVASYFWLKSRVPGWAFWQFWLWYSILRAGWEETFRLNPLTIKTYLNQGLDAPGIGLWTDTQIFSVPLILVSLWMLW... | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q72G45 | MLTFPRIDPVAITLGPLQFRWYGLMYLFGFLSGWWLGRRRAAQPGSRWTGEMVDDMVTYVILGVVLGGRIGYILFYDLAYYLGNPTQIFSIWNGGMSFHGGLLGVVFAMWLLGRRNGLGFMDVSDFVAPLIPPGLFFGRIGNFINGELWGKHTTLPWGMVFPDGGPFPRHPSQLYECALEGVILFLALWVFSSRKRPTGHVSGLFALLYGVFRFTVEFVREPDVQLGYLAFGWLTMGQVLCLPLIMLGLWLLRPGGDKGTKAA | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
B8DQF5 | MLAYPRIDPVAVSIGPLQFRWYGLMYLFGFISGWWLGRRRAAQPGSGWHPQQVDDMVTWAIFGVVLGGRLGYILFYDLAYYASQPAAIFQIWHGGMSFHGGLLGVLFAVWLYARRAEREFLSVVDFVAPLIPPGLFFGRIGNFINGELWGAPTTLPWAMVFPDGGPFPRHPSQLYEAVLEGVVLFAAVWWFSGRKRPVGAVSGLFGVLYAIFRFAVEFVREPDPQLGYLAFGWLTMGQVLCLPLFGVGMWLLLRNRGAAEGPAAR | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
A1SS95 | MSVSNFVLPKIDPVAVSIGPVDIHWYGLMYLLGFTFALWMANRQCDKSNGIWTREQASDLLFYGFMGVILGGRIGYVLFYQFPLFLDSPLYLFKIWEGGMSFHGGVLGVTTAIIFYAKKNKRSILSVGDFIVPLLPVGLGAGRIGNFINSELWGRVTDSPFGIIFQNAGPLPRHPSQLYEFALEGVVLFIILILYIRKARPAGSVAGLFLLAYGVFRFIVEFAREPDAHLGLLSLGLSMGQLLSLPMIFAGMAFIAYAYRAKAQAPSQADNVKPPKAKTNKAKKKHG | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q98HW8 | MNEYFLLPLASLPFPNINPILIQIGPLAVHWYGVGYIVGILFAWWYAKRLAANPKLWPDGILPMKLEDLDDFIVWAAIGVVLGGRTGYVLFYDLPRYIAHPLDIFAVWQGGMSFHGGLLGVILAMTLFSIKRGIRTWSLFDVVAAGVPVGLGLVRVANFINSELWGRPTDVPWAIEFPNGGPFTRHPSQLYEALLEGLVLFVVLRILTHSRLKLKTPRFVGGAFICGYGLSRIFVEFFREPDQQLGYLLGTNWLTMGMILSTPMVLAGIWAMATAKPVKQAQPQAT | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
A5V5N0 | MQQAVIANAAQAIHWADLGLNPIALDLGFLQIHWYSLAYISGILLGWYYLTRLIAQPGAPMARRHADDLVFYATLGILIGGRLAYVFFYQPDILLHPLDVLKLWQGGMSFHGGALGVAAGIFYMARRNGLSWLRIHDYVACCAPFGLFFGRIANFVNGELWGRPTDVSWAMIFPGAPDGLPRHPSQLYEAGLEGIVLGLVLSFFFWRTDARNQPGKLVGIFLLGYGLSRFVVEYFREPDAQLGTLSWGLTMGQTLTVPMLIGGLYLIATASKRTPINAD | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q7UMF7 | MEVARTVRIPHAFDGLTLSRQATMRRTLFLIPHEFAGWPIFGIGWALLFLLIAVLAYVGWESRRGGLGASTAIRQIAGFAVMAAVILVVVVPRTELVNTLGDPVGVAVRGYGMFLMLAAIASVGLAAWRAERAGLGADSILQLAPWTFIGGLLGARVFYVTQYYEDFLRPTWGETLMAMAALNQGGLVVYGGFIGGFIASLIALKRHQTPIWRIGDVIIPCVFVGLLFGRLGCLMNGCCYGGACEAGPLAVQFPAGSQVHAEQLLSGELLGIEGHPVVSDEEPPAGQSQMVVDSVRPDSLANQAGVKKGETLTIALDPSY... | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
B6ITJ7 | MSGIPFPAIDPVAVELGPIVIRWYALAYLAGFLFGWWYCTRLARAIPGRPTPDDLSEFLTWAIVGVLLGGRLGFVLFYNLDYYIQHPLQALAIWSGGMSFHGGLTGIVAAILLYGWRHGFSPFALGDLVAVAGPVGLFLGRIANFVNGELWGRPAPDLPWAVIFPDPRAGGVPRHPSQLYEAALEGLVLFAVLAWLASKPAVRERTGTLSGTFLVGYGIARILGEVFREPDVQIGYLAFGVTMGQILSVPMVLIGLWILVRAPFGPVRTPAAAAAGR | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q0SHZ8 | MTSTVDVLAYIPSPPQGVWYVGPVALRAYALFIIVGIVVAIVWGDRRWVARGGEKGTVLDIAIWAVPFGLIGGRLYHVMTDWPTYFGEGGDPVDALKVWQGGLGIWGAVALGGVGAWIGCRRRGIPLPALGDAVAPAILLAQAIGRLGNYFNQELYGRETEVPWGLEIFERRNDVGQVSPQLIDGVSTGEVAFVVHPTFLYEALWNVLIVLLLVWVDRRFRIGHGRLFALYVAGYCAGRFWIELMRSDHASLIAGVRVNSFTSALVFVAALVYFFAATKGREDPAELRPADGGPVGGGGEPVDGEIAQKEPEKNVEDAGK... | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
P60973 | MPFFAVAFPVFDPVAVAIGPFAIRWYALAYIAGIVIGWLYARMLLQRQRLWGGPSPISLEAFDDFILWVTIGIILGGRTGYVLFYNLDFFIRHPAEIFELWKGGMSFHGGFMGCVAAVVLFGWKRKVPILSLGDITCAVGPIGLFLGRIANFINGELWGRPADASVPWAMVFPNAGPLPRHPSQLYEAGLEGIGLFVILALMIRAGALKRPGLIIGAFLTFYGLARITGEFFREPDPQLGFLWGDMTMGMLLSIPMVIVGILVMITTWRRGRGAPAAATPSSEAAS | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q2RWQ0 | MLFALPFPAIDPVLVEIGPFAIRWYALAYIVGLLGGWWYTRFLSRRSRPPVMSDADVDDLLVWATLGTILGGRLGYVVFYNAAHFLANPLEIPMLWHGGMSFHGGLVGVITATVLFCRSRRLSVARVGDLVALVAPLGLFFGRLANFINGELFGRPAPDVPWAMVFPHGGPLPRHPSQLYEATLEGLVLFCLLGLLWRFTALSRKPGQIIGLFLIGYGLSRITAEFFREPDAQIGFLALGVTMGQILSLPMILAGIVVFVVARRAKPLAVPGGR | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
P02948 | MSKFYKIWLVFDPRRVFVAQGVFLFLLAVLIHLILLSTPAFNWLTVATAKHGYVAAAQ | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 6594
Sequence Length: 58
Subcellular Location: Cell inner membrane
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P80588 | SAPAQWKLWLVMDPRTVMIGTAAWLGVLALLIHFLLLGTERFNWIDTGLKEQKATAAAQAAITPAPVTAAAK | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 7727
Sequence Length: 72
Subcellular Location: Cell inner membrane
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P0DJO0 | MWRIWRLFDPMRAMVAQAVFLLGLAVLIHLMLLGTNKYNWLDGAKKAPAATAVAPVPAEVTSLAQAK | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
PTM: The N-terminus is blocked.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 7348
Sequence Length: 67
Subcellular Location: Cell inner membrane
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Q3J144 | MTNGKIWLVVKPTVGVPLFLSAAVIASVVIHAAVLTTTTWLPAYYQGSAAVAAE | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 5599
Sequence Length: 54
Subcellular Location: Cell inner membrane
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P80101 | MWRMWKILDYRRTVVLAHVGMAVLALLIHFILLSTESFNWLEGNPYG | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 5563
Sequence Length: 47
Subcellular Location: Cell inner membrane
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P80103 | MWKLWKFVDFRMTAVGFHIFFALIAFAVHFACISSERFNWLEGAPAAEYYMDENPGIWKRTSYDG | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 7688
Sequence Length: 65
Subcellular Location: Cell inner membrane
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P95655 | MNNAKMWLVVKPTVGIPLFLVACAIASFLVHLMLVLTTGWMGDYYSGSFEAASLVSNATTLLS | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 6766
Sequence Length: 63
Subcellular Location: Cell inner membrane
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P77799 | MNQGKVWRVVKPTVGVPVYLGAVAVTALILHGGLLAKTDWFGAYWNGGKKAAAAAAAVAPAPVAAPQAPAQ | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 7135
Sequence Length: 71
Subcellular Location: Cell membrane
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P80107 | MNQARIWLVVKPSVGLPLLLGVVLLIALLVHGAILTNTSWYPTYFEGNW | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 5479
Sequence Length: 49
Subcellular Location: Cell inner membrane
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X4Y2L4 | MKEIAVTIDDKNVIASVSESFHGVAFDASLFSPKGLWSFVDITSPKLFKLLEGLSPGYFRVGGTFANWLFFDLDENNKWKDYWAFKDKTPETATITRRWLFRKQNNLKKETFDDLVKLTKGSKMRLLFDLNAEVRTGYEIGKKMTSTWDSSEAEKLFKYCVSKGYGDNIDWELGNEPDHTSAHNLTEKQVGEDFKALHKVLEKYPTLNKGSLVGPDVGWMGVSYVKGLADGAGDHVTAFTLHQYYFDGNTSDVSTYLDATYFKKLQQLFDKVKDVLKNSPHKDKPLWLGETSSGYNSGTKDVSDRYVSGFLTLDKLGLSA... | Function: Hyaluronidase that mediates hydrolysis of (1->3)-linkages between beta-D-glucuronate and N-acetyl-D-glucosamine residues in hyaluronate. Very specific to hyaluronate: not able to hydrolyze chitin, heparin or chondroitin sulfate.
Catalytic Activity: Random hydrolysis of (1->3)-linkages between beta-D-glucurona... |
Q6R0H1 | MDTNTSGEELLAKARKPYTITKQRERWTEDEHERFLEALRLYGRAWQRIEEHIGTKTAVQIRSHAQKFFTKLEKEAEVKGIPVCQALDIEIPPPRPKRKPNTPYPRKPGNNGTSSSQVSSAKDAKLVSSASSSQLNQAFLDLEKMPFSEKTSTGKENQDENCSGVSTVNKYPLPTKQVSGDIETSKTSTVDNAVQDVPKKNKDKDGNDGTTVHSMQNYPWHFHADIVNGNIAKCPQNHPSGMVSQDFMFHPMREETHGHANLQATTASATTTASHQAFPACHSQDDYRSFLQISSTFSNLIMSTLLQNPAAHAAATFAAS... | Function: Transcription factor involved in the circadian clock. Binds to the promoter region of APRR1/TOC1 and TCP21/CHE to repress their transcription. Represses both CCA1 and itself. May recognize the promoter of JMJ14 to regulates its expression during the night in a circadian manner .
PTM: Phosphorylated by CK2.
Se... |
P0C7R2 | MVFSVATSSVTNPKLHHHHHLSDFNRNRVSTSLKIMNSKNHTNPRKCECFDLYDQLIPYKKAWSWQKSILNEKKALIDKNQECSDSLIILQHPSVYTMGTGSSENYLNFDIKNAPFDVYRTERGGEVTYHGPGQLVMYPIINLRNHKMDLHWYLRKLEEVVIRVLSSAFAINASRLDGFTGVWVGNKKMAAIGIRVSKWMTYHGLALNVTTDLTPFNSIVPCGIRNRGVGSVKGLIEDGEHYNKLEDLQLLDIAHESLLKEFSEVFQLQMEKQTVFKLEC | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity) . Together with LIP1P is essential for... |
P20013 | MAFKSLLSFVSVIGALQGANAALTRRVACPDGVNTATNAACCQLFAVREDLQQNLFHGGLCTAEAHESLRLTFHDAIAISPALEAQGIFGGGGADGSIAIFPEIETNFHPNIGLDEIIELQKPFIARHNISVADFIQFAGAIGASNCAGAPQLAAFVGRKDATQPAPDGLVPEPFHTPDQIFDRLADASQGEFDPILTVWLLTAHTVAAANDVDPTKSGLPFDSTPELWDTQFFLETQLRGTSFPGSGGNQGEVESPLAGEMRLQSDHTIARDSRTACEWQSFVDNQPKAQQMFQFVFHDLSIFGQDINTLVDCTEVVPI... | Cofactor: Binds 2 calcium ions per subunit.
Function: Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin.
Catalytic Activity: 1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + glycolaldehyde + guaiacol + H2O
Sequence Ma... |
O34398 | MAFTMQPVLTSSPPIGAEWRYEVKYDGYRCILRIHSSGVTLTSRNGVELSSTFPEITQFAKTAFQHLEKELPLTLDGEIVCLVNPCRADFEHLQVRGRLKRPDKIQESANARPCCFLAFDLLERSGEDVTLLSYLDRKKSLRELISAAKLPASPDPYAKETIQSIPCYDHFDQLWEMVIKYDGEGIVAKKTNSKWLEKKRSSDWLKYKNFKQAYVCITGFNPNNGFLTVSVLKNGIMTPIASVSHGMRDEEKSAIREIMEQHGHQTPSGEFTLEPSICAAVQYLTILQGTLREVSFIGFEFQMDWTECTYAQVIRHSKPV... | Cofactor: Binds 3 Mn(2+); 2 Mn(2+) for polymerase/primase activity and 1 for ligase activity.
Function: With Ku forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity (Probable). Probably involved in DNA repair during spore germination.
Catalytic Activity: ATP + (d... |
A0R3R7 | MARHPWGMERYERVRLTNPDKVLYPATGTTKAEVFDYYLSIAQVMVPHIAGRPVTRKRWPNGVAEEAFFEKQLASSAPSWLERGSITHKSGTTTYPIINTREGLAWVAQQASLEVHVPQWRFEDGDQGPATRIVFDLDPGEGVTMTQLCEIAHEVRALMTDLDLETYPLTSGSKGLHLYVPLAEPISSRGASVLARRVAQQLEQAMPKLVTATMTKSLRAGKVFLDWSQNNAAKTTIAPYSLRGRDHPTVAAPRTWDEIADPELRHLRFDEVLDRLDEYGDLLAPLDADAPIADKLTTYRSMRDASKTPEPVPKEIPKTG... | Cofactor: Binds 4 Mn(2+); 2 Mn(2+) for polymerase/primase activity, 1 each for 3-phosphoesterase and ligase.
Function: With Ku forms a non-homologous end joining (NHEJ) repair enzyme which repairs blunt-end and 5'-overhang DNA double strand breaks (DSB) with about 50% fidelity, and DSB with non-complementary 3' ends. P... |
P9WNV3 | MGSASEQRVTLTNADKVLYPATGTTKSDIFDYYAGVAEVMLGHIAGRPATRKRWPNGVDQPAFFEKQLALSAPPWLSRATVAHRSGTTTYPIIDSATGLAWIAQQAALEVHVPQWRFVAEPGSGELNPGPATRLVFDLDPGEGVMMAQLAEVARAVRDLLADIGLVTFPVTSGSKGLHLYTPLDEPVSSRGATVLAKRVAQRLEQAMPALVTSTMTKSLRAGKVFVDWSQNSGSKTTIAPYSLRGRTHPTVAAPRTWAELDDPALRQLSYDEVLTRIARDGDLLERLDADAPVADRLTRYRRMRDASKTPEPIPTAKPVT... | Cofactor: Binds 4 Mn(2+); 2 Mn(2+) for polymerase/primase activity, 1 each for 3-phosphoesterase and ligase.
Function: With Ku forms a non-homologous end joining (NHEJ) repair enzyme which repairs DNA double-strand breaks (DSB) with reduced fidelity. Recognizes, processes and reseals DSBs, including repairs on incompat... |
Q9I1X7 | MPSSKPLAEYARKRDFRQTPEPSGRKPRKDSTGLLRYCVQKHDASRLHYDFRLELDGTLKSWAVPKGPCLDPAVKRLAVQVEDHPLDYADFEGSIPQGHYGAGDVIVWDRGAWTPLDDPREGLEKGHLSFALDGEKLSGRWHLIRTNLRGKQSQWFLVKAKDGEARSLDRFDVLKERPDSVLSERTLLPRHGEAATPAARPARRGKSGGKTPMPEWIAPELASLVEQPPRGEWAYELKLDGYRLMSRIEDGHVRLLTRNGHDWTERLPHLEKALAGLGLQRSWLDGELVVLDEEGRPDFQALQNAFEEGRGENILYVLFD... | Cofactor: Binds 4 Mn(2+); 2 Mn(2+) for polymerase/primase activity, 1 each for 3-phosphoesterase and ligase.
Function: With Ku probably forms a non-homologous end joining (NHEJ) repair enzyme, which repairs dsDNA breaks (DSB) with reduced fidelity. Acts as a DNA ligase on singly nicked dsDNA, fills dsDNA gaps (3- or 4-... |
Q01198 | MKDFQDQVAFITGGASGAGFGQAKVFGQAGAKIVVADVRAEAVEKAVAELEGLGITAHGIVLDIMDREAYARAADEVEAVFGQAPTLLSNTAGVNSFGPIEKTTYDDFDWIIGVNLNGVINGMVTFVPRMIASGRPGHIVTVSSLGGFMGSALAGPYSAAKAASINLMEGYRQGLEKYGIGVSVCTPANIKSNIAEASRLRPAKYGTSGYVENEESIASLHSIHQHGLEPEKLAEAIKKGVEDNALYIIPYPEVREGLEKHFQAIIDSVAPMESDPEGARQRVEALMAWGRDRTRVFAEGDKKGA | Function: Catalyzes the C alpha dehydrogenation of arylglycerol-beta-aryl ether (C alpha alcohol type) (compound IV).
Sequence Mass (Da): 32344
Sequence Length: 305
Pathway: Secondary metabolite metabolism; lignin degradation.
EC: 1.-.-.-
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P27457 | MARNNTITLYDLQLESGCTISPYVWRTKYALKHKGFDIDIVPGGFTGILERTGGRSERVPVIVDDGEWVLDSWVIAEYLDEKYPDRPMLFEGPTQKNLMKFLDNWLWSTAVGPWFRCYILDYHDLSLPQDRDYVRWSREQWFLGGQRLEDVQAGREDRLPLVPPTLEPFRRILAETKWLGGDQPNFADYSALAVFLWTASVARTPPLTEDDPLRDWLDRGFDLFDGLGRHPGMNPLFGLKLREGDPEPFVRQTGPAGAGGQALNKGPQTTKMPPRVAEKAD | Function: Able to degrade various dimeric lignin compounds. Catalyzes the unique and reductive cleavage of arylglycerol-beta-aryl ether.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32070
Sequence Length: 281
Subcellular Location: Cell inner membrane
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Q93PS7 | MSQFEKTPGWLDWYANPSKPQFKLPAGAVDAHCHVFGPGNEFPFAPERKYTPCDASKAQLYALRDHLGFARNVVVQATCHGADNRAMVDACKSSGGKARGVATVKRSISDAELQQLHDAGVRGVRFNFVKRLVDFTPKDELMEIAGRIAKLGWHVVIYFEAVDLPELWDFFTALPTTVVVDHMGRPDVTKGVDSEEFALFLKFMREHQNVWSKVSCPERLSVTGPKALNGEQNAYRDVVPFARRVVEEFPDRVLWGTDWPHPNLKDHMPDDGLLVDFIPHIAPTAELQQKLLVDNPMRLYWPEEV | Function: Involved in the degradation of aromatic compounds via the protocatechuate 4,5-cleavage pathway . Catalyzes the hydrolysis of 2-pyrone-4,6-dicarboxylate (PDC) to oxalomesaconate (OMA) . Also catalyzes the reverse reaction .
Catalytic Activity: 2-oxo-2H-pyran-4,6-dicarboxylate + H2O = (1E)-4-oxobut-1-ene-1,2,4-... |
O87170 | MTNDERILSWNETPSKPRYTPPPGAIDAHCHVFGPMAQFPFSPKAKYLPRDAGPDMLFALRDHLGFARNVIVQASCHGTDNAATLDAIARAQGKARGIAVVDPAIDEAELAALHEGGMRGIRFNFLKRLVDDAPKDKFLEVAGRLPAGWHVVIYFEADILEELRPFMDAIPVPIVIDHMGRPDVRQGPDGADMKAFRRLLDSREDIWFKATCPDRLDPAGPPWDDFARSVAPLVADYADRVIWGTDWPHPNMQDAIPDDGLVVDMIPRIAPTPELQHKMLVTNPMRLYWSEEM | Function: Contributes to the degradation of lignin at the level of the protocatechuate 4,5-cleavage pathway . Catalyzes the hydrolysis of 2-pyrone-4,6-dicarboxylate (PDC) to (4E)-oxalomesaconate (OMA) . The keto form of OMA can tautomerize into the enol form, 4-carboxy-2-hydroxymuconate (CHM), under certain pH conditio... |
G2IQQ5 | MMMIIDCHGHYTVLPKAHDEWREQQKAAFKAGQPAPPYPEISDDEIRETIEANQLRLIKERGADMTIFSPRASAMAPHVGDQSVAVPWAQACNNLIARVVDLFPETFAGVCMLPQSPEADMTSSIAELERCVNELGFIGCNLNPDPGGGHFKHPPLTDRFWYPFYEKMVELDVPAMIHVSGSCNPAMHATGAYYLAADTIAFMQLLQGNLFADFPTLRFIIPHGGGAVPYHWGRFRGLADMLKQPSLDTLLMNNVFFDTCVYHQPGINLLADVIDNKNILFGSEMVGAVRGIDPTTGHYFDDTKRYIDALDISDQERHAI... | Cofactor: Binds 1 zinc ion per subunit. The metal center contained within the active site of LigJ is not used to activate the water molecule but is utilized to activate the substrate via polarization of the carbonyl oxygen.
Function: Contributes to the degradation of lignin at the level of the protocatechuate 4,5-cleav... |
G2IQQ8 | MRGAAMGVVVQNIERAPLEVIDGLAACGVATVHEAQGRTGLLASYMRPIYRGARVAGSALTISAPPGDNWMVHVAIEQLKAGDILLLAPTSPCEDGYFGDLLATSAQARGCRGLVIDAGVRDVRDLTEMNFPVWSKAIYAQGTVKNTLGSVNVPVVCANALVNPGDVIVADDDGVCVVPLANAEKVLEAARAREANEGDKREKMANGVLGLDLYKMRERLEKEGLKYV | Function: Contributes to the degradation of lignin, being involved in the final step of the protocatechuate 4,5-cleavage pathway. Catalyzes the conversion of 4-carboxy-4-hydroxy-2-oxoadipate (CHA, also named 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate) to pyruvate and oxaloacetate but also the decarboxylation of oxaloac... |
G2IQS7 | MSAPTNLEQVLAAGGNTVEMLRNSQIGAYVYPVVAPEFSNWRTEQWAWRNSAVLFDQTHHMVDLYIRGKDALKLLSDTMINSPKGWEPNKAKQYVPVTPYGHVIGDGIIFYLAEEEFVYVGRAPAANWLMYHAQTGGYNVDIVHDDRSPSRPMGKPVQRISWRFQIQGPKAWDVIEKLHGGTLEKLKFFNMAEMNIAGMKIRTLRHGMAGAPGLEIWGPYETQEKARNAILEAGKEFGLIPVGSRAYPSNTLESGWIPSPLPAIYTGDKLKAYREWLPANSYEASGAIGGSFVSSNIEDYYVNPYEIGYGPFVKFDHDFI... | Function: Involved in the catabolism of vanillate and syringate. Catalyzes the transfer of a methyl moiety from vanillate or 3-O-methylgallate (3MGA) to tetrahydrofolate, forming protocatechuate (PCA) or gallate, respectively, and methyl-tetrahydrofolate. Has similar activities with both substrates . Cannot use syringa... |
Q50L44 | MLAGEASMRSPILACWQPILLLMLGSILSGSATGCPPRCECSAQERAVLCHRKRFMVVPEGIPTETRQLDLGKNRIKTLNQDEFANYPHLEELELNENIISAIEPGAFNNLFNLRTLGLRSNRLKLIPLGVFTGLSNLTKLDISENKIVILLDYMFQDLYNLKSLEVGDNDLVYISHRAFSGLNSLEQLTLEKCNLTSIPTEALSHLHGLIVLRLRHLNINAIRDYSFKRLYRLKVLEISHWPYLDTMTSNCLYGLNLTSLSITHCNLTSIPYVSVRHLVYLRFLNLSYNPIVTIEGSMLHDLLRLQEIQLVGGQLTTVE... | Function: Functional component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. Is also an important negative regulator of oligodentrocyte differentiation and axonal myelination (By similarity).
PTM: N-glycosylate... |
Q96FE5 | MQVSKRMLAGGVRSMPSPLLACWQPILLLVLGSVLSGSATGCPPRCECSAQDRAVLCHRKRFVAVPEGIPTETRLLDLGKNRIKTLNQDEFASFPHLEELELNENIVSAVEPGAFNNLFNLRTLGLRSNRLKLIPLGVFTGLSNLTKLDISENKIVILLDYMFQDLYNLKSLEVGDNDLVYISHRAFSGLNSLEQLTLEKCNLTSIPTEALSHLHGLIVLRLRHLNINAIRDYSFKRLYRLKVLEISHWPYLDTMTPNCLYGLNLTSLSITHCNLTAVPYLAVRHLVYLRFLNLSYNPISTIEGSMLHELLRLQEIQLVG... | Function: Functional component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors . Is also an important negative regulator of oligodentrocyte differentiation and axonal myelination . Acts in conjunction with RTN4 an... |
Q6FIK6 | MSTPYTPAPQIFNLFKVLAVSLALIAAVEYFKYGTRINYEWFHCTPVMERVGGPDSSVLKIWARGGPSCDKRGEYKTILKRISRDYEPNDEHLSFCIKENMSVDPVHYPIHEDKGEPGYIAYVGYDSDKRTVDELCEGTTVFHF | Function: Component of the ceramide synthase complex required for synthesis of ceramides.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 16478
Sequence Length: 144
Subcellular Location: Endoplasmic reticulum membrane
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O46107 | MRCSLRMQLLLLLGLCVFISRIQGQLIGGEEDEEDEEEEEEEEESVEDETPEDRLQRKNIKQDSTLSVDKLIAKYGYESEVHHVTTEDGYILTMHRIRKQGAPPFLLQHGLVDSSAGFVVMGPNVSLAYLLADHNYDVWLGNARGNRYSRNHTTLDPDESKFWDFSWHEIGMYDLPAMIDHVLKVTGFPKLHYAGHSQGCTSFFVMCSMRPAYNDKVVSMQALAPAVYAKETEDHPYIRAISLYFNSLVGSSIREMFNGEFRFLCRMTEETERLCIEAVFGIVGRNWNEFNRKMFPVILGHYPAGVAAKQVKHFIQIIKS... | Function: Could be a digestive enzyme.
Sequence Mass (Da): 50661
Sequence Length: 439
Subcellular Location: Secreted
EC: 3.1.1.-
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P17573 | MVSKTFFLAAALNVVGTLAQAPTAVLNGNEVISGVLEGKVDTFKGIPFADPPVGDLRFKHPQPFTGSYQGLKANDFSSACMQLDPGNAISLLDKVVGLGKIIPDNLRGPLYDMAQGSVSMNEDCLYLNVFRPAGTKPDAKLPVMVWIYGGAFVFGSSASYPGNGYVKESVEMGQPVVFVSINYRTGPYGFLGGDAITAEGNTNAGLHDQRKGLEWVSDNIANFGGDPDKVMIFGESAGAMSVAHQLVAYGGDNTYNGKQLFHSAILQSGGPLPYFDSTSVGPESAYSRFAQYAGCDASAGDNETLACLRSKSSDVLHSAQ... | Function: Hydrolyzes all ester bonds in triglyceride and displays a high affinity for triolein. For unsaturated substrates having long fatty acyl chains (C18:2 cis-9, cis-12 and C18:3 cis-9, cis-12, cis-15) GCL I shows higher specific activity than GCL II, whereas GCL II shows higher specific activity against saturated... |
Q6CXA2 | MATQQNKNRVYILLQYVLAALVLIAAVEYFKYKTRISYEWFHCTVQSEELFDHPEGSPLKLWAIGGPSCDKRGELKTIMKRITMDFDPNVEPVKFCIVEDTKVKSIHYPIEDGNKGDPGYISFVGYERDSDVVEQACASYAATVFNL | Function: Component of the ceramide synthase complex required for synthesis of ceramides.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 16768
Sequence Length: 147
Subcellular Location: Endoplasmic reticulum membrane
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P40601 | MKRSFIFAPGMLALSISAISNAHAYNNLYVFGDSLSDGGNNGRYTVDGINGTESKLYNDFIAQQLGIELVNSKKGGTNYAAGGATAVADLNNKHNTQDQVMGYLASHSNRADHNGMYVHWIGGNDVDAALRNPADAQKIITESAMAASSQVHALLNAGAGLVIVPTVPDVGMTPKIMEFVLSKGGATSKDLAKIHAVVNGYPTIDKDTRLQVIHGVFKQIGSDVSGGDAKKAEETTKQLIDGYNELSSNASKLVDNYNQLEDMALSQENGNIVRVDVNALLHEVIANPLRYGFLNTIGYACAQGVNAGSCRSKDTGFDAS... | Catalytic Activity: a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+)
Sequence Mass (Da): 70717
Sequence Length: 645
Subcellular Location: Secreted
EC: 3.1.1.3
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P65288 | MKSQNKYSIRKFSVGASSILIATLLFLSGGQAQAAEKQVNMGNSQEDTVTAQSIGDQQTRENANYQRENGVDEQQHTENLTKNLHNDKTISEENHRKTDDLNKDQLKDDKNSSLNNKNIQRDTTKNNNANPSDVNQGLEQAINDGKQSKVASQQQSKEVDNSQDSNANNNLPSQSLTKEAPSLNKSDQTSQREIVNETEIEKVQPQQNNQANDKITNHNFNNEQEVKPQKDEKTLSVSDLKNNQKSPVEPTKDNDKKNGLNLLKSSAVATLPNKGTKELTAKAKDDQTNKVAKQGQYKNQDPIVLVHGFNGFTDDINPSV... | Catalytic Activity: a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+)
Sequence Mass (Da): 76531
Sequence Length: 680
Subcellular Location: Secreted
EC: 3.1.1.3
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Q9S2A5 | MRRFRLVGFLSSLVLAAGAALTGAATAQAAQPAAADGYVALGDSYSSGVGAGSYISSSGDCKRSTKAHPYLWAAAHSPSTFDFTACSGARTGDVLSGQLGPLSSGTGLVSISIGGNDAGFADTMTTCVLQSESSCLSRIATAEAYVDSTLPGKLDGVYSAISDKAPNAHVVVIGYPRFYKLGTTCIGLSETKRTAINKASDHLNTVLAQRAAAHGFTFGDVRTTFTGHELCSGSPWLHSVNWLNIGESYHPTAAGQSGGYLPVLNGAA | Function: Catalyzes the hydrolysis of fatty acid esters with a preference for mid-length acyl chain (C10-C16). Is able to hydrolyze the triacylglycerol triolein and mixed triacylglycerols from a wide range of natural oils; better activity is obtained with corn-, wheat germ- and olive oil that have higher content of lin... |
B9MQ24 | MSYLKKPDWLKIRVKADQKIDDVIEILKMFSLHTVCEEAQCPNIYECFSKKTATFLIMGDVCTRNCTFCDVKKGKPVKLNSDEPKMVANAVGALGLKYVVITSVTRDDLPDGGASHFAECIRSIKGKRPYTKIEVLIPDFKGSFESVSKVVEASPDVVAHNIETIERLYPCVRPLASYKRSLDVLRMVKEIDKNIFTKSGIMVGLGETKDEVKKALEDLRNAECDFVTIGQYLSPSKNHHPVVEFVHPDVFEEYKEFAISIGFKFVMSGPLVRSSYMAENTKDIIENVRKI | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
Q8F3V7 | MNPLKKKPRTHSLQNAPEKPDWLKVKLAFPDPKNNPVAIVRNSLEEKKLNTVCESASCPNLNHCWSRKTATYMLGGDICTRRCSYCDVASGKPFPLDPEEPKRIAESSIALDLRHVVITSVNRDDLEDGGAAHFAKTVKEIRKGLPDCKIELLIPDLKVKQEALEIIFECNPDIFNHNLETVKRLFPEVAPQKRYERSLDVLKIASARGFLTKSGLILGMGETLEEVKECMQDLASVGVSLLTLGQYLQPTSTHLPVKEYVVPQVFKDLRIYGKSIGFKGVFSGPLVRSSYHADEQISWNP | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
A1U380 | MSESAKPRITSGSKFRNEHGFSAIKDGVKRSSSNTEGKSLERKPKWLRARMPGGERYDAVRRNVTEHRLSTVCQESHCPNIGECWTNGTATIMVMGSVCTRACKFCAVDTGNPKGWLDPEEPENTAKSVELMGLRYIVLTSVDRDDLPDGGAAHYAACVSAIKQRTPEVAVEALTPDFDAVMSDVEKVVDSGLDVFAQNVETVKRLTSRVRDPRAGYEKTLSVLAHAKKHRPDVLTKTSLMLGLGETEEEILETMDDLRAIGVDILTLGQYLRPTPNHLPVERYVTPEEFNRYRDIGLEKGFMEVPSGPMVRSSYRADRV... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
Q0W150 | MPDPTSPKPDWLKVRLPRTDKYGAVKDVIKKYNLNTVCSSAMCPNAFECWDGGCLTFMVLGNTCTRACRFCTVTHGPAGEPLDSNEPQRLAAAAKELDLSYVVITSVDRDDLPDYGAGHYAACIRAVKEQLPGARVEAIIPDFTGRLDLLEQVVDARPDVISHNIETVERLSPSVRDRRAGYYRSLDVLRDVKRVNPHMLTKSSLLLGMGEEDIEIKEALHDLQEARVDIVTLGQYLRPSIRQWPVHRYVAPGEFSELAEYGRSLGFKYVAAGPFVRTSYRAGEQYVSVIADSRMA | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
P0CT91 | MRLAPQKPLLLSTVLHLLLSIWMLGFASLAGATVQEPLAASDTPKPVSAALFSSIERLSRLVDITYCVGNTGVWKPFACASRCNEFPTLTLERTWRTGILMSDSCGLIAVDHGTPRHDAGEGKDDPLAEKAIIVAFRGTYSLTNTIIDLSTIPQEYVPYPSPDDGGNEPPREPSHRCDNCTVHSGFLASWRHARKVVLPELKVLRQKYPEYPIRLVGHSLGGAVAMLAALEMRVSLGWRDTVVTTFGEPRVGNRQLCDYLNAVFELNLGDEMDPAEREYRRVTHADDPVPLLPPAEWGYSSHGGEFFISKKDLPPSVEDV... | Function: Lipolytic enzyme that possesses both lipase and acetylxylan esterase activity. Active towards p-nitrophenol esters of various carbon chain length with preference for medium-chain fatty acids (C-8). Also highly active on the acetylated compounds xylose tetra-acetate and oat spelt xylan.
PTM: Glycosylated.
Cata... |
A9FD62 | MAQFSPKPEWLKVRAPGGDTYHHLKETFRKLDLHTVCEEARCPNVGECWREGTATVMLLGDVCTRGCRFCAVTTGDPRGAVDVREPEHVARAIARLSLQYVVMTMVNRDDLLDGGAEHVARTVSRLHALRPDLLIETLVGDFQGHMSAVDMVVDAGPDVFAHNVEVVRRITRVIRDVRSSYDQSLAVLRRAKERQRRLAADAAEAGAPAPRRLTKSSIMVGIGETDDEVLEALRDLREAGVDIVTIGQYLRPSSKHAPVQRFVEPETFAAFERAALEMGFLYAASAPLVRSSYKAAEVFVRSLMDRGGAALPASPGAAAV... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
Q4JWD9 | MGTTGTNDGATTPPANTSTPAVDIDVRDLGTVDYEDTWHLQANLAAQRAEEKIPDTILLLQHPPTYTAGKRTQDSDRPTNGLPVVDVDRGGRITWHGPGQLVAYPIIKLADPVDVVDYVRRLEQALIQTCEDLGLHGTGRVEGRSGVWLPAGVINGELKPARKIAAIGIRVTRGVTMHGVALNCDNTMEYYDHIVPCGLADAGVTTLTEELGRDVSVSDAYSSLAHNLVDALNGDLPVHS | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q83C64 | MNDVIIRQLAHLIPYQPLWEAMQTFTARRQSQTTDEIWFLEHEPVFTQGLAGKPEHVLNSGNIPLIRTDRGGQVTYHGPGQLMMYLLLDLNRLGLSTRTFVRTIENTVAESLQEWGIPAQGKETAPGVYVDDKKICSIGLRVRKGFSYHGLALNVAMDLTPFSCINPCGFKGLTMTQIQDYVNPIEMDAVKRTIIPLFLKNFGYNQPAIMVETSLEFLIDDHLRSFSEKLGERETVTNSRQN | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q6A9W7 | MQQDPPTSQPHTPQIVDGVKPRGWVDHPAGLHFEYLGIADSRPTRTEYNECWAHQREVHAEVSAHQRPNTVIYVEHDPVYTAGRRTRKEAYPFDGTPVVPVDRGGEITWHGPGQLVGYPIVFLQRGIGVVDYVRRVEEAVIRLVSQYGLRAGRVPGRTGVWFPSDGMGPERKVCAIGIRVSRQTAMHGFALNIDPDTAGFDNIIPCGISDADVTSMARELRRLHGPDAEVPSLLEVAGNLEPILTEMMSFQPYEMSPDIPRREHPAFLHPMP | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
O19898 | MMLIIRYGLLNFETSWVHQKTMVFIQIRKRQKKKLSIYLKHPQVYTLGHRANKEYISFCSNNTLVNLHRVDRGGEVTYHDYGQVIIYNITHLQKINRNVNIYIANLEQLGKRILLLYKTKSTKKEKFPGIWIQQKKIVALGIKIIQRTTFHGLSINFSCSKRNYELILACGIKDGISVNFNEIHKKNSQNQFYWKYKIVLLIVDILAFNNIISF | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity).
Catalytic Activity: L-lysyl-[protein]... |
Q11XW2 | MHKNTNKSVLVEDLGLIDYQQAWDYQTQLFNSTIEKKLALRDLPEDEQVAPGNFLIFCEHPHVYTLGKSGKREHLLISEAQLQHAQAAYYEINRGGDITYHGPGQLVGYPIFDLDNFFTDIHKYLRYIEEAIILTLADFNIVAGRIDGLTGVWIESDNPLKARKICAMGVKASRWVTMHGFALNVQPDLTYFKNIVPCGIDDKAVTSIEQELNTTVSMQAVKDYLLKHLTALFELHIENTTHTT | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q9RWA5 | MPKSALMSSSFQTSVSPRPLPVSCASRTAARKLSLYCSEGRTRCGMGQGKGWRWPGHRPPGLPSPTNRVGQSVPKWRPQPHKAAGGGRTIRDVKEAAFDVLDLGLLPYPQAWARQKQELARVAVGGRPTLLLVEHPAVLTLGRKAQEGENIVVTREYLAAQGIDVFAVERGGDVTYHGPGQLVAYAIFPVGRRVRDFLRLLENAVVTALGTLGLPDARPNPGYAGVYVDPREINGKTYDQKICSIGVAIKQNVALHGIGLNVCTNLDHFDLIVPCGLTDTQMTSVQREYDLRGLGSVSMEQAKKALTDAFALTFADYDWS... | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
A9BPT8 | MSAPAAELAQTLDLRLLGRTDYEATVQAMQAFTSGRDAGTRDELWICEHAPHFTQGLAGKSDHLLNPGDIPVVATNRGGQVTYHGPGQVVAYPLLDLQRLGYFVKEYVFRIEDAVIRTLEHFGITGHRVEGAPGIYVRLDDPRSHAMLAQRPQLRVPGSPAPQPDFSGLGKIAALGIKVSRHCTYHGVALNAAMDLEPYERINPCGYAGLQTVDLSTIGVQTTWDEAARVLGRQLQRRLAP | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
B8J3G1 | MLGFDLGRTGYEDAFTLQKQVQAMVQSGGDDILLLLEHPPTVSIGKNSGAENVPPHLQDMWNGHVDIVHSTRGGNVTCHFPGQLVAYPVISLKKRSGGIRAYVHDLEEAAIRMLARFGVTAARRQGFPGVWTGERKIASLGIAVSRYVTMHGMALNVAEDLSLFNIISPCGLEGVAATSIARETAGPVPDMPAVKTAFLEEFYHIFQPAGDHAQPLPTLRTTQDLMTLLQDAQRTEK | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q6ARJ9 | MSFLVDLGATSYIACYATQQAVVARRCSGDLDRDCFLLTEHPPVYTLGKRGGEQHLHISKEMLAQKGIDVVSIERGGEITYHGPGQLVLYPILHLRKRKMRVTEYVGLLEETMIRLAADFGVRVVRNTRNAGVWTEDGRSKIGSIGIAIRHGVSFHGFAFNLNTDLEPFSWINPCGLTGVTATSLAREAGTDFDPAEVKKRLLSIVADLFGEFTVVDSLHSVK | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q88DM4 | MMSACLGFRELGLQPYEPVLEAMRRFTEQRSPDSQDEIWLVEHPAVFTQGQAGKAEHLLVPGDIPVVQTDRGGQVTYHGPGQLVAYLLLDVRRLGFGVRELVSRIELALIDLLASYAVQASAKPDAPGVYVDGAKIASLGLRIRNGRSFHGLALNVDMDLAPFRRINPCGYAGLAMTQLRDLAGPIELDEVRTRLRGQLVKHLDYAEQTTLTGGID | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q87VW6 | MANALGFRDLGLIDYETAWHAMQRFTDGRGREAGDEVWLVQHPPVFTQGQSGKAEHLLLPGNIPVVQVDRGGQVTYHGPGQLVAYLMLDVRRLGFGVRDLVTRIENTLIALLADYGVTAAAKADAPGVYVDGAKIASLGLRIRNGCSFHGLALNVDMDLEPFRRINPCGYAGLAMTQLSDQAGQIEFSEVSVRLRAQLVKHLDYAEQATLTGGINQYD | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q4FS63 | MPNTMQALNTQPLNDTLITKSITAADYVPTLDAMLSRTLARIALKKEQGLRTPDELWIVDHNDVYTLGQAGKEEHILQRTNTPIIKTDRGGQVTWHGHGQLVMYWLFDLDSVGWSVRNMVSHAEQAIEDVVNDCLKSPASTDTIHISARARRDAPGVYIYADTAAEIDSAHRSTDEIKVDNTIMIGKIASLGFKIKHGFSYHGVAINLNCDLSAFNAINPCGYAGMQMLRLADFVNMNQATTPQPNNPTLTDDAKTITYEQFTQKLIDNIAQRHAGVIPLRELAPK | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q8ZUR4 | MKILWIGRTQYAEAWRLMKSLHCAVAQGLTGDIALVTEHEPVVTVGKHGRLNNVIKWDVPVYLVERGGDATYHGPGQAVVYPIVALRWPLKRYIDAIEDAVIKTLGTYGILAGKKQGHRGVWVGDRKIASIGIAVENNVAYHGVAINVTIDPREFARINPCGLPASTMISMKELGVVAEVRDVGIETAKKLALELGLTPELISKPPEVPQVAEELKPVRVAINA | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
A3MW04 | MRGLDLGLLDYVSAWRMMKILHREVASGGDDAFILVEHPHVITVGKHGRTNNVVKWELFVYVVERGGDATYHGPGQLVAYPVVKLRWPLSRYLWMLEEAVIRSLRPLGVEAGRVEKHRGVWVGGKKVASIGIAVEGGVAYHGVAVNVSTDLSYFYHINPCGLHPSAITSLNQLGVEISLEEYKGLFVEAFEEVFEAKVVWVDPAPYLAAAAQLRASPTLLSAPIEAST | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q1MG80 | MAMLRTDLEFSMLPQLGTRPVRWRFADGLVPYEEAVETMEREVALIADGGDELVWLVEHPPLYTAGTSANARDLVQPNRFPVFATGRGGEYTYHGPGQRVAYVMLDLKRRRQDVRAFVAALEDVVIRTLDMMNVRGERREDRVGVWVRRPEKPLLADGTMAEDKIAALGIRLRKWVTFHGLSLNVDPDLDHFGGIVPCGISAYGVTSLVDLGLPVMMADVDIRLRTAFEAVFGETTGEI | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
P71668 | MPSLDNTADEKPAIDPILLKVLDAVPFRLSIDDGIEAVRQRLRDLPRQPVHPELRVVDLAIDGPAGPIGTRIYWPPTCPDQAEAPVVLYFHGGGFVMGDLDTHDGTCRQHAVGADAIVVSVDYRLAPEHPYPAAIEDAWAATRWVAEHGRQVGADLGRIAVAGDSAGGTIAAVIAQRARDMGGPPIVFQLLWYPSTLWDQSLPSLAENADAPILDVKAIAAFSRWYAGEIDLHNPPAPMAPGRAENLADLPPAYIAVAGYDPLRDDGIRYGELLAAAGVPVEVHNAQTLVHGYVGYAGVVPAATEATNRGLVALRVVLHG | Function: Esterase that can hydrolyze short-chain esters with the carbon chain containing 2 to 12 carbon atoms. In vitro, pNP-butyrate is the preferred substrate.
Catalytic Activity: a fatty acid ester + H2O = a fatty acid + an aliphatic alcohol + H(+)
Sequence Mass (Da): 34053
Sequence Length: 320
EC: 3.1.1.-
|
O07732 | MAQAPHIHRTRYAKCGDMDIAYQVLGDGPTDLLVLPGPFVPIDSIDDEPSLYRFHRRLASFSRVIRLDHRGVGLSSRLAAITTLGPKFWAQDAIAVMDAVGCEQATIFAPSFHAMNGLVLAADYPERVRSLIVVNGSARPLWAPDYPVGAQVRRADPFLTVALEPDAVERGFDVLSIVAPTVAGDDVFRAWWDLAGNRAGPPSIARAVSKVIAEADVRDVLGHIEAPTLILHRVGSTYIPVGHGRYLAEHIAGSRLVELPGTDTLYWVGDTGPMLDEIEEFITGVRGGADAERMLATIMFTDIVGSTQHAAALGDDRWRD... | Cofactor: Cannot use Mg(2+) as a cofactor.
Function: May play a role in cell wall modulation . The N-terminal domain exhibits lipolytic activity . In vitro, hydrolyzes various p-nitrophenyl (pNP) esters . pNP-decanoate (C10) is the best substrate, followed by pNP-octonate (C8), pNP-laurate (C12) and pNP-butyrate (C4) .... |
Q94252 | MRESISDLMTVMIPLLIILLLSNYSKSVDLEFYLDTPELIKSWGYSVEIYNTTTKDGFILELHRIPYGREVPTSSDVNNSRPVIFLQHGFLCSSFDWVANSPHQSAGFVFADAGFDVWLGNFRGNTYSRKHVSLNPDKDPKFWDWSWDQISEYDLPAMIGKALEISGQESLYYTGFSLGTLTMFAKLSTDPKFSRKIKKYFALAPIGSIKHAHGVFLFLGRHFGKDYEEYVKKHGSDELFGSSLLFKKIVKYTCGLFDTLEEFCSDITLLFIGTANENWNQTRIPVYLAHTPAGSSSNVMAHLDQMFSYGGVPTFDMGEE... | Function: Lysosomal lipase that regulates the metabolism of long-chain fatty acids, primarily in response to nutrient availability . The production of these lipid signaling mediators regulates various processes, including lipolysis, autophagy, mitochondrial beta-oxidation, which in turn control lifespan and adaptation ... |
O61866 | MWRFAVFLAAFFVQDVVGSHGDPELHMTTPQIIERWGYPAMIYTVATDDGYILEMHRIPFGKTNVTWPNGKRPVVFMQHGLLCASSDWVVNLPDQSAGFLFADAGFDVWLGNMRGNTYSMKHKDLKPSHSAFWDWSWDEMATYDLNAMINHVLEVTGQDSVYYMGHSQGTLTMFSHLSKDDGSFAKKIKKFFALAPIGSVKHIKGFLSFFANYFSLEFDGWFDIFGAGEFLPNNWAMKLAAKDICGGLKVEADLCDNVLFLIAGPESDQWNQTRVPVYATHDPAGTSTQNIVHWMQMVHHGGVPAYDWGTKTNKKKYGQA... | Function: Lipase involved in lipid homeostasis . Regulates mitochondrial lipid composition, in particular cardiolipins and coenzyme Q-9 levels, in response to nutrient availability . Does not affect global triglyceride levels in response to nutrient availability . However, in coelomocytes, specifically promotes triglyc... |
Q8IEG9 | MKRIFRLVRRCHYSTEKRTNGPLVLVSNNQNIHFNLSLENFLLNNYNDLLKYLNINTIEKFNEPILFLWRNNRSIIIGKNQNIWSECNLKNIKEDGVLVARRFTGGGAVYHDLGNVCFTFLNNNINTSSNFLIILNTLKNHFNIEAKTQGRNDITVNDQKCSGSAFKKIKDVFLHHGTILINLEKNILNKYLTPDKIKYIKHGVSSVNARTINLSEINNNITCENLCIALIKEFTKFYEQNYKENINNIKNLENNINNSNFQNKEQININNTNENNLINNTNIIPNDITVHYIDQNNNITKNPEFLKYYNLLKDWDWCYG... | Function: Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes . In the mitochondrion, functions as a redox switch between two lipoylation routes . Senses the oxidation state of lipoate and... |
Q8Y489 | MNIENTLLKQDVWRFIDNTTINPAFDAIQSFATDDTLCRSVGARMAPSTVRGWVHEKTVSLGIQDSKLPDIDKGIAFLQKQGYRVVVRNSGGLAVVLDSGVLNLSMVLPDAERGIAIERGYETMFTLIKDMFVDCNEVIEAKEIEDSYCPGSYDLSIQGKKFAGISQRRMAKGVAVQIYLAIDGDQTTRSELIRDFYTISGKAKQTKYTFPDVNPNVMGSLSDLMKNDISLNGTLVRLFNSLRHYAGDLVSGTLTSEELDLFPAYYERLIARNDKVLT | Function: Catalyzes the amidotransfer (transamidation) of the lipoyl moiety from lipoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes. Takes part in a pathway for scavenging of lipoic acid derived from eukaryotic host cells. Cannot use lipoyl-tripeptide (DK(L)A), lipoamide (LD), or free lipoa... |
Q81JR5 | MSNSRSILSQPEWRIVDQSSLGPTFHALQSFAMDDTLCTSIGKGESAATMRSWVHHNTIVLGIQDSRLPHLEEGISFLKENNFNVIVRNSGGLAVVLDEGVLNVSLLFQETEKGIDIDLGYDTMWHLIQEMLKDYDVTIEAKEIVGSYCPGSYDLSIRDQKFAGISQRRIRGGVAVQIYLCATGSGSERAALVRDFYNLAIQGEETRFTYPEIVPSTMASLSELLDETITVQDLMMRLLKTLQQFAPKLTPSQLTIDEIPLYETNLQRIIDRNNKALGLEK | Function: Catalyzes the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes.
Catalytic Activity: L-lysyl-[lipoyl-carrier protein] + N(6)-octanoyl-L-lysyl-[glycine-cleavage complex H protein] = L-lysyl-[glycine-cleavage complex H pr... |
P39648 | MANQPIDLLMQPKWRVIDQSSLGPLFDAKQSFAMDDTLCMSVGKGVSPATARSWVHHDTIVLGIQDTRLPFLQDGISLLESEGYRVIVRNSGGLAVVLDDGVLNISLIFEDEKKGIDIDKGYEAMVELMRRMLRPYNAKIEAYEIEGSYCPGSYDLSINGKKFAGISQRRVRGGVAVQIYLCADKSGSERADLIRRFYQAALKDKQNDKKGVYPEIRPETMASLSELLQKDISVQDLMFALLTELKALSTHLYSAGLSIDEEMEFEKNLVRMAERNAKVFG | Function: Catalyzes the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes.
Catalytic Activity: L-lysyl-[lipoyl-carrier protein] + N(6)-octanoyl-L-lysyl-[glycine-cleavage complex H protein] = L-lysyl-[glycine-cleavage complex H pr... |
A7Z9Y5 | MGKQPIDLLMQPSWRIIDQSSLGPYFDAKQSFAMDDTLCASVGKGESPATARSWVHHRTIVLGIQDTRLPFLEDGVKLLEDEGYRVIVRNSGGLAVVLDEGVLNISLIFEDEKKGIDIDRGYEAMTELVRRMLRPHHAEIEAYEIKGSYCPGSYDLSIGGRKFAGISQRRLRGGTAVQIYLCADKSGSERADLIRRFYQAALKDKSNDTKGVYPDIRPETMASLSELLRTDITVQDLMLALLTELKELSGRLYAAGLSPEEEMVFEKNLTRMLERNEKVFGTQESLD | Function: Catalyzes the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes.
Catalytic Activity: L-lysyl-[lipoyl-carrier protein] + N(6)-octanoyl-L-lysyl-[glycine-cleavage complex H protein] = L-lysyl-[glycine-cleavage complex H pr... |
C0ZF00 | MSFSVNQPFRWMDSGTYQDSPLEPLIRDEALAASMQSESAAPVIHLWVYDQALYLGRRDAKLPHLQQALHQFGQDGFGCVLRSSGGACVPLDAGVLNMACLLPNTSISIDSFFSFVAQLLDVGLRDYGKLEFGEVTGSYCAGEYDFSIHGKKIGGMAQRRTRHGSILQLCINVDDRPRGEWMEHFYRLAGLDEMQSHKPIPSIDASTVGSIASLTGKLATMDDVKARLLETIRSEWAVSPTPFYVQNELVTESRHHLSQRLHLFSYTAKELAAPDWHLPE | Function: Catalyzes the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes.
Catalytic Activity: L-lysyl-[lipoyl-carrier protein] + N(6)-octanoyl-L-lysyl-[glycine-cleavage complex H protein] = L-lysyl-[glycine-cleavage complex H pr... |
P11153 | MNIDRKILNKALAKEKVANCQKDYTDIESKFARRTPENTVEDTCHLIPGVTESVANCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLRRAQHHYPESADYTKLVGEDVARFINWMEDEFKYSVDNVHLLGYSLGAHAAGVAGSRTNTKVSRITGLDPAGPNFEYAEATSRLSPDDAQFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGSFQPGCNIQDALRVISQKGFGDMDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNVGYEINKVRAKRSSKMYL... | Function: Key enzyme in triglyceride metabolism (By similarity). Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (By similarity). Although it has ... |
A0CH87 | MVLTARQRDELNQAIHQYLLISYQQSAQVFKTEAVVKDGQIEADLLEKKWNSIVRLSKRVITLEQQVEQLNEQLAQAQAGKIQFNKSDDEQRLTPFEKFKLEGHRAGVNCVAFHPQYQILGSASDDGSIKLWDYESGHFEKTLKGHTSNVNCLAFDPTGKYICSASSDLSIKLWELKNHTCVKTLIGHEHSVSTVQFSDHGDFILSASRDKSIKLWEVQTGFCKKTFSEHQEWVRCAVFSNDEKQMASCSQDQMIYIWVIDSGQILHQLSGHEHVVEQVKYVPEHGAKQILTQQQQQNIQTINLLVSVSRDKEIKIWNTI... | Function: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes.
Sequence Mass (Da): 46168
Sequence Length: 403
Domain... |
B6GZD3 | MPSSLTPQQAAELNKSIIAYLSAHGLAETLAAFRKESDFPDNMFDATAAKQYENLLERKWTSNSTLMKKLLALESHNKALRNELNSTRPSFLNRNADVNDWLPQHPIRSLESHRDSINCIAFHPKYSLIASGSGDLTIRIWDWEDSTLERTLKGHTMAVCDVDYGDTSSGILLASCSSDFTIKLWDTTDDYKNVKTLRGHDHIVSAVRFIPSGNLLASASRDMKVILWNVINGYRVKTIEDHTGWVRDISPSFDGQFLLSTGDDMTVRLWEISASQPICKFTATGHENRILCCAVAPATSFRYLASFLESRGSTIAAEIT... | Function: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for nuclear migration during vegetative growth as well as development. Required for retrograde early endosome ... |
Q803D2 | MVLSQRQRDELNRAIADYLRSNGYEEAYSTFKKEAELDVNDELDKKFAGLLEKKWTSVIRLQKKVMELESKLNEAKEEITLGGPVGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSLMVSASEDATIKVWDYEAGDFERTLKGHTDSVQDISFDQTGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTMKMWEVATGYCVKTFTGHREWVRMVRPNQDGTLLASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESAHPTISEATGSENKKSGKPGPFLLSGSRDKTI... | Function: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in the PAF inactivation. Regulates the PAF-AH (I) activity in a catal... |
Q17N69 | MYVRRLRRERSNQAIADYLGSNGYTDALEAFRKEADMPNEIERKYGGLLEKKWTSVIRLQKKVMELEAKLSEAEKEAIEGAPTKAKRTPTDWIPRPPEKFALAGHRATVTRVVFHPVFSMMASASEDATIKIWDFETGEYERTLKGHTDSVQDLAFDSHGKLLASCSSDLSIKLWDFQQTFECVKTMHGHDHNVSSVSFVPAGDYLLSASRDKTIKMWEVATGYCVKTFTGHREWVRMVRVNVDGSLMASCSNDHSVRVWQTNSKECKAELREHENTVECIAWAPESAAAAINEAAGADNKKGAHQGPFLASGSRDKTIR... | Function: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes.
Sequence Mass (Da): 46183
Sequence Length: 409
Domain... |
B9I666 | MIEQSLSKPSFSLSIPIPQPPKSKSSFLCSYSKIRCESVDYPSSSKIDAKHPQISSINSNGGGKMGSYTGRDPNVKKPEWLRQKAPQGERYDEVKESLSRLKLNTVCQEAQCPNIGECWNGGGDGIATATIMVLGDTCTRGCRFCAVKTSRNPPPPDPMEPLNTALAIASWGVDYIVITSVDRDDLPDGGSGHFAQTVRAMKELKPEIMVECLTSDFRGDLKAVDTLVHSGLDVFAHNVETVKRLQRIVRDPRAGYEQSLSVLKHAKISKKGMITKTSIMLGLGESDNEVKEAMADLRAIGVDILTFGQYLQPTPLHLTV... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
B9N2B0 | MIEQSLSKPSFSLSIPIPKAPKSKSSFFCSYSKIRCESVDYPSLTKIDAKHPQNSTTINNGSSSSASVDLKNNEKGPYPYPGGGKMGPYTGRDLNEKKPEWLRQRAPQGERFEEVKESISRLNLNTVCQEAQCPNIGECWNGGGDGIATATIMVLGDTCTRGCRFCAVKTSRTPPPPDPMEPLNTALAIASWGVDYIVITSVDRDDLSDGGSGHFAQTVRAMKELKPEIMVECLTSDFRGDLKAVDTLVHSGLDVFAHNVETVKRLQRIVRDPRAGYEQSLSVLKHAKVSKKGMITKTSIMLGLGETDDEVKEAMTDLRA... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
Q8LEE8 | MMHHCSITKPTFSISISTQKLHHHSSKFLNLGFRIRCESGDVSSPLRTKAVSLSSEMEDSSSLKKSLMELEGKKSEPYPGGMPKMGPFTGRDPNVKKPAWLRQKAPQGERFQEVKESLSRLNLNTVCEEAQCPNIGECWNGGGDGVATATIMVLGDTCTRGCRFCAVKTSRNPPPPDPMEPENTAKAIASWGVDYIVITSVDRDDIPDGGSGHFAQTVKAMKRHKPDIMIECLTSDFRGDLEAVDTLVHSGLDVFAHNVETVKRLQRLVRDPRAGYEQSMSVLKHAKISKPGMITKTSIMLGLGETDEELKEAMADLRAI... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
A8I2V9 | MRSLATLHQSPASCSRSAPVAPCPARRANSSRRVARQGPRARASSPVVETESEDVDITPQIDAFEELVRLAVEKDPSLATLAEQHLRSKSKSAAPVSPFAAPSPGSPSASSMLGPSLGALPNQNKPAWLRQRAPQGEIYSGLKDQLRGLKLATVCEEAQCPNIGECWNGELATATIMLLGDTCTRGCRFCAVNTARTPPPPDPNEPVNTATAVASWGVGYVVLTSVDRDDMPDGGSEHFAATVRTLKQLRPGILVECLTPDFKGDLDAVRHLARSGLDVYAHNVETVERLQKRVRDPRAGYMQTLDVLRAAKECGVYTKS... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
A4RW69 | MCGPTATTVANAGTGGETIKGLPPGLKKPPWLRQRAPSGERFDYLSESLTGLKLNTVCEEAMCPNVGECWNGDTGTATVMLLGDTCTRGCRFCAVNTSQTPPPPDENEPENTAHAIAEWGVGYIVLTSVDRDDIPDGGSEHFARTVRTLKTIKSSVLVEALTPDFQGDMNAVAHLARSGLDVFAHNVETVERLQKRVRDPRANYEQSLAVLRHAKASKEGLVTKTSIMLGLGEEDEEIKQCMRACKEAGVDIFTLGQYLQPTPQHLPVKEFVTPEKFDFWKAYGEEVIGFRYVASGPLVRSSYKAGEFFIESMLRKDALD... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
B9RX57 | MEQTLFNPSISMPKSFYHKHITISSRIQCQLSTNSPSSNTKTTTVTVPSKKTMGPYTGRDPNVKKPEWLRQRAPQGERFQEVKHSLSSLKLNTVCEEAQCPNIGECWNGGGDGIATATIMLLGDTCTRGCRFCAVKTSRNPSPPDPLEPQNTALAIASWGVDYIVLTSVDRDDLPDGGSGHFSETVQAMKKLKPEIMVECLTSDFRGDLEAVETLVHSGLDVFAHNIETVKRLQRIVRDPRAGYEQSLSVLKHAKHSKEGMITKSSIMLGLGETDDELKEAMADLRAIDVDILTLGQYLQPTPLHLTVKEYVTPEKFAFW... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
Q96376 | MQLITNFSSSSSELQFLVDKVKRESLSSSSSNTQNLFLSTSPYDTAWLALIPHPHHHHHHGRPMFEKCLQWILHNQTPQGFWAAAGDNISDTDDDVTLDCLLSTLACLVALKRWQLAPDMIHKGLEFVNRNTERLVMKQKPSDVPRWFTIMFPAMLELAGASSLRVDFSENLNRILVELSQNRDDILTREEVDEKKQYSPLLLFLEALPAQSYDNDVLKQIIDKNLSNDGSLLQSPSATARAYMITGNTRCLSYLHSLTNSCSNGGVPSFYPVDDDLHDLVMVNQLTRSGLTEHLIPEIDHLLLKVQKNYKYKKASPKSL... | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Involved in the biosynthesis of the acyclic monoterpene S-linalool, a major component of the strong sweet scent of the C.breweri flowers.
Catalytic Activity: (2E)-geranyl diphosphate + H2O = (S)-linalool + diphosphate
Sequence Mass (Da): 99790
Sequence Leng... |
N6Z5E2 | MESTRMLRQPIQLLQGHKGPVTASRHRRNAVVYALLCLLALLPVATGQSAAWQAAGLGLFMPGAGFLALGGAWALLFPLTVFVFWLAVIAWFWSGMVVAPLTLWLGTAALAGWLAGEAIWPPAVYLAPAAAAATFLFFQYRGAKRRAKDREHFKFRQSFFAESLAEVHQRAATEPEPGERELTPDQLQGVRYLLELALQPVGQYKGYTIIDQFQPAALRYQLNHIGFALGMVQGHYTPNFQGYLGQAQRNVIDTYRERKVWGYWVYESMWGHFNFSDFDPARKDNIMLTGWYGMHVGQYMLNAGDTRYSQPGSLSFRLND... | Function: Involved in linalool degradation. Catalyzes the reversible isomerization of linalool to geraniol. Does not show stereospecificity towards linalool isomers and acts equally well on both (R) and (S)-linalool. Cannot use the monoterpenoids citronellol and nerol as substrates.
Catalytic Activity: linalool = (2E)-... |
Q10156 | MHSLKRRRNHAPDWQDFYKNGVPQEVIVIEDSASPRLTPNLPPPFSVHQLQSFVPPQPPSSSSPSTTGTVAVPINGANAVYPSTNSVSLPQSYDPWLDANGVVPLPHDVASHPSYMVQSPTSYHACSNNQSPFPHSHHPPLHNPLPVSCQPVLRPPPVPQVPSHWYPVSLPSPNLPHQPISKPPVIPNLPKLQVHPNRLPHPIHNHPYSSPTSYPPPLCPATYCPSNPPQLAPATAIAPSSQSSQHKSVNYSVTPSSINNHTAVPLSPTLAVWLPMTQPTFQPPSANVYQPASNANQVITPVSISDYRPPKKRKRAAWPP... | Function: Protein kinase that may act as a negative regulator of filamentous growth and flocculation. Appears to have a role in normal cell wall and septum formation and in cell separation. May have antagonistic function in the regulation of beta-glucan distribution between the sites for cell wall and septum assembly.
... |
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