ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P61035 | MPGFNAVPRRDYVMAALSGVLLALSFPKPGFSILAWVALVPLLLACGRKAPAVAFRLGFTAGLVAYAGILYWINIAVVTYGRLHWSVSIVIFLMLAGYLALYPAATAYVVRRGEDRGISALLAFPVVWVGLEYIRSFLLTGFPWASLGYSQYRTLPLIQIADLTGVYGLSFLIALSNVVLYRIIRGFAARERAPYPVKSAAILVLLLVATLAYGFNRLHRPEAGAPFSVALIQGNIDQSVKWDPAFQEATVAVYERLSRKACSTGPADLVVWPESAVPFYLQNEEKYASRIRNLTRELRSCTVVGSPAFERDGETIRYLNSAFLLSPWGDVVGRSDKIHLVPFGEYVPMAKFLPFVNKIVAGIGDFSPGARIASLETGKGAIGVLVCFEGIFPELARGYVRAGSRVLVNITNDAWYKRSSAPYQHLSMTVFRAVENRVPLVRAANTGITAIIDSKGHILRMTNLFEVWRPRFSWTRK | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52609
Sequence Length: 477
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
Q7NJV1 | MSGIALRRRREQAQRRRSIAGVLAAVGGGTALGLAAPPTGWGVLVWVALVPLLVYLRAEHRPRAFWLGTLAGMVYYAILLRWLLGFHPLTWLGIEWWPSLAIALGAWLFVSASQAWVIGLWASLVVRTRLSGLRRVLFAVGLWVGLHWLWGQGETAFPWGTLAQSLAGDLWAVQTVALGGAQLLVGLAVAVNALVAESWSTRRVGYAGLAALLAASVYLYGWWQLAQPLPAGEPLRMGVIQGNIAQARKWTPDGRRETVETYVRGYEELAAAGAQLVLTPETAFPFIWSRPTNPAAPLVPEIQSRRVPVLLSAFERRTDGQVATTLFALDGDARTISTFNKIHLVPFGEQIPLKALIGPLVRKLSPVQQEVFAGSLGQRLQTPVGLVAAGICFDSAFADGFRAQVAAGARLLVQSTNDAWYGPAMAPQHHALDALRAVETGRYLVRASNNGTSAVVDPLGRTTRITGWNVYAAFVEPVRLLEGMTLYALWGDWFVPLSAALALLGLIAGRSPAGRRGRRNF | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56431
Sequence Length: 521
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
Q7VM56 | MNLVNPSILVACILSFCLGAIGCLAFSPFDIWLIAYLSAAGLIWAATLVERKTAMLATFAWSIGYFGVGVQWVNVSMTQFGGVPVIVSYLAVLLLASYLGLYNLLFSYLARRFGLISPFVLASLFTFTEYLRGVVFTGFPWLQFGYTQIDSPFAQLAPIFGVEGLTFLVILLSSYLVDIVKNPTRKIATFTKIAVIIGFSLASNLLQFVQIDQQKPPVKVALIQANIEQQLKWDPAHFENTLRTYQQLINSSLAENEVIILPESAIPALESKINPLLNQLQKMAAAKNTEIIIGTLYENEQQQLFNSALVLGNQTKPYQLHQSLRYNKHHLVPFGEYVPFGSLLDWMREVFILPVNLAKGPFIQPALFTNKGKFNMAICYEVIFGHQLQQNQLAQQADYLITITNDAWFGDSIGPWQHLQMARMRALELGKPLLRAANTGITAVVGFDGKVIKKLPQFETNTLTAEIATTKGHTLFGQFGHWLIYSLSFICVAFGLFRRQKHKKH | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56529
Sequence Length: 505
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
P44626 | MKNLNRILLSIKFMNKYFTYLIAIISGLLGVFAFSPFDYWPLAYVSLLGLLYVAKNPKKSTALLSTFLWAMGFFCFGVSWLNVSIHQFGGASLGVSYFLVGLLAAYLALYPMLFTYLVHHFKVQSAVIFAVIWTLTEFLRGWIFTGFPWLQFGYTQIDSPFYGIAPIFGVTGLTFFTVWASAVIFNLVSSLFKTKNLKLVLANALLLIIVGGLSAYSSRIHFVKSVEDKAISVTLAQGNIEQNLKWDPNYFYSTLAIYQKLITENLGKTDLIILPESALPTLENAITPFFEGLERAAKETKTEIMVGTVFQDTKSGKLLNSIMTAGNPDFPYQPNTQNRYNKHHLVPFGEYVPLESILRPLNSVFNLPMSAFQSGEAVQPSLIAKKRAFSPAICYEIIFGEQVRQNLKQDTDYLLTLSNDAWFGDSIGPWQHLQMARMRALELGKPLIRATNTGISVFVDAQGKVLAQAPQFIETTLTYKIAPAEGKTPYSVLGNMPLYALSLLFLLLHSMMAFIRRKMNIL | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58553
Sequence Length: 522
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
Q7VFP7 | MLPFYAQWVLESYDKAISPLLVSLLGLFSIASVLFVPKNRRFGVGFFIGMLWFYWISLGLRYFDMSFLIPLVVIACGIFMGFVFYIGLWCECLIVRFAFLLLLSYLTPFGFDWIVPESVFAYSYIGVDKLSFALSILALWILFKYKTWWKLGGVICLVFALDFGLKDSKIQNLPPLKIKLAQSAVSQDFDYRMREAKSIFSEHISDIQKAINEEYDVIILPESAFYVPLDSQYFPYFDSLLEMSHKIVIIVGALREEIHTDGRASYFNSTYKFDKGKVSFYDKVHLVPFGETLPSFLLPLVNTFFQGIGGFSAGKDFGYFDIAEIKFKNAICYEGSNRGFYADYPQYVIVTSNNAWFVPSIEPILQKNLMKYYARLYGSVIFHATNLSPAAIITPFVSSR | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45856
Sequence Length: 400
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
O24982 | MRLLLFNQNAFLLACMFVSSVYVNAVLDAYAIENPYISITLTSLLAPLSMLAFLKTPRNSAFALGFFVGALLFYWCALSFRYSDFTYLLPLIIVLIALVYGVLFYLLLYFENPYFRLLSFLGSSFIHPFGFDWLVPDSFFSYSVFRVDKLSLGLVFLACIFLSTKPLKKYRIIGVLLLLGALDFNGFKTSDLKKVGNIELVSTKTPQDLKFDSSYLNDIENNILKEIKLAQSKQKTLIVFPETAYPIALENSPFKAKLEDLSDNIAILIGTLRTQGYNLYNSSFLFSKESVQIADKVILAPFGETMPLPEFLQKPLEKLFFGESTYLYRNAPHFSDFTLDDFTFRPLICYEGTSKPAYSNSPSKIFIVMSNNAWFSPSIEPTLQRTLLKYYARRYDKIILHSANFSTSYILSPSLLGDILFRKRS | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48474
Sequence Length: 425
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
Q608N5 | MKAMLLALTGGILLPFAFAPFGYALVAPLSLALLFRVWLNASPSKAALYGYLFGLGQFGIGVSWVFVSMYEYGGSDVFSAAGLTALFVAYLALFPALAGWLGVKAGGGSILVRTLLVFPAAWVVTEWLRGWLFSGFPWLQIGYSQTDTGLRSIAPVFGVFGVGWLLAVLAGLLLSAWLLDRRGRRFALLGAAVVLVGSTQFAKVQWTHPAGDPIRVTLLQGNVPQDQKWRPEAKTTTVQMYVDMTRQHWDSRLIIWPETAVPAFYQQVAESFLAPLEAEARQHGVDVLVGVPYYEAQGNRYYNALVTLGAKPGRYFKRHLVPFGEFLPLRPVLAFVLDILQIPLADFTAGAHRQTLLQAAGYPLIASICYEDIFGQESLTGLPEGAYLVNVTNDAWFGDSFAPHQHWQKARMRALETGRYMLRATNTGVTGIIDAGGRPVAVAPMFEREALTGMMQPMAGATPYALWGDWPAIGLCAGIVGICFARRRRNASSHQGRQAEPGRN | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55064
Sequence Length: 504
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
A0QZ13 | MIPAVTDDDPLEDPLDDDVAPGLDDAEPEPEPRDEHDEPSRPATGSRIGGWVARRGSRFGKGVLDRCAPLSAAIGGGLALWLSFPPIGWWFTAFPGLALLGWVLTRTATTKAGGFGYGVLFGLAFYVPLLPWISGLVGAVPWLALAFAESLFCGLFGLGAVVVVRLPGWPLWFATLWVAAEWAKSTFPFGGFPWGASSYGQTNGPLLALARIGGAPLVSFAVALIGFSLTLLTAQIVWWWRHGHKPGVPAPAVMLPGVAIAASLLVTALVWPQVRQSGTGAGDDTAVTVAAVQGNVPRLGLEFNAQRRAVLDNHVKETLRLADDVKAGRAAQPMFVIWPENSSDIDPLLNADASAQITTAAEAIDAPILVGGVVRADGYTPDNPVANNTVIVWEPTDGPGERHDKQIVQPFGEYLPWRGFFKHLSSYADRAGYFVPGTGTGVVHAAGVPIGITTCWEVIFDRAARESVLNGAQVLAVPSNNATFDEAMSAQQLAFGKLRAVEHDRYVVVAGTTGISAVIAPDGHEISRTEWFQPAYLDNQIRLKTDLTPATKWGPIVQAVLVIAGVAVLLIAILHNGRFAPRMLRRRSATTVKR | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Can transfer a number of fatty acids (C16 and C19, palmitic and probably tuberculostearic acids respectively are shown) . Enhances the polyprenol monophosphomannose (PPM) synthase activity of Ppm1 (AC A0QZ12) without itself having PPM synthase catalytic activity .
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63346
Sequence Length: 594
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell membrane
EC: 2.3.1.269
|
Q9K0A2 | MVSKLDKYWQHPALYWPLLILFAAATPFTFAPYYHFWLMPLIFGAFVRLIELRPRFAVSSAYLFGLTAYTTQFYWIHTALHDVSGLPDLYAVPLTFLLPAYLALYPALCFWLWKKFTLPRGIKIGLVLPILWTLTEFARERFLTGFGWGAIGYSQITPDSPLAGFAPLGGIHMVTLATAFLGVWLVLASNNTARSGKRLLPIILIAALLAAGYTARQTDFTRPDGSRSTVALLQGNIDQTLKWREDQVIPTIQKYYEQVGKTTADIVILPETAIPVMRQNLPENILAKFAEQAQNNGSALAVGISQYTSDGNGYENAVINLTGYQENNQDGIPYYAKNHLVPFGEYKPLPFLTTPLYKMMDMPLSDFRKGGGKQSALLMKNQKIAFNICYEDGFGDELIAAAKDATLLANASNMAWYGKSNAMYQHLQQSQARAMELGRYMVRATNTGATAIISPKGNIIAQAQPDTETVLEGHIKGYVGETPYMKTGSSWWLMGILALAALILFIFRNKEH | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57062
Sequence Length: 512
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
Q820C9 | MNGYFRLIAAFALGVATVSGFAPFYLYPIPVVTLALLALLWRRSRTPGQAALTGFTFGMGLFGAGVTWLYVSLHDFGHMEPALAVLALIILCAYLALFPALTGWITAFRHFRASWAWPGMVAALWALAEWLRGTLFTGFPWLTVGYSQAPASPLAGFAPVIGVYGLSLLLMLSAAWLACWLENRQSHRFWLGLGSVWLIGFGLQQIHWTQPEGEPVTVSLLQGNIPQNMKWQPEHLAATMQIYAELVQESPSRLIVTPEISFPLFYEQAPQDYLALLAEHARSRQGDLLIGMAERSSSDNGYYNTMFSFGTSPEQSYRKYHLVPFGEYIPLKPVFGWIIDVLHIPLSDFSRGGLDQQPLDLAGQQVAVNICYEDVFGEEIIMQLPQASLLVNVSNDAWFGRSIGPRQHLQISQMRALETGRYMLRATNTGVTAIIDERGRVLEQLDMFTTAGLHSTAQGFGGATPYVRFGNSLVFALIGLLLLAGSLAAFSGRRKTL | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54905
Sequence Length: 497
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
Q8YYI9 | MGLTVAPFAAWFLAWIALAPLWIFVVSSKRKNYPPSSLLLLGLTWGIGYHGVALFWITGIHPMDWLGVPWWPSLAITIFCWSFISFYGGLFGAIWAACLTHISEQKSWLRILIGTAMWCVLESLWSAGPLWWSSLAYTQSPHNLAILHLGQISGPNLVTAAIVSVNGIVAEAWLNRKQGLLGRYLAIATGLLITLHLIGFGLYTAPIAKSSDTALKVGIVQGNIPNKIKLLPQGLSRAITGYTDGYLTLVNQGVEAVLTPEGALPFFQRNLPTTPLVSAVREKGVVAWIGAFGDRGRSYTNSLFTVNSQGEITSRYDKSKLVPLGEYIPFEGIIGGLVQRLSPLDEHQVHGSPNQIFDTPFGRAIVGICYESAFPEVFRSQAAAGGQFILSSSNDAHYSAAMPFQHHAQDIMRAIETDRWSARATNTGYSAFVDPHGRTLWISGYNTYETHAETIYRRQTQNLYVRWGDWFTPLLVGLSFLGWSLNIFWRNDANANSKLR | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55263
Sequence Length: 500
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
Q7U5S4 | MGDLRSQPLLRAVLGGLLAGLAPGVAGPLSMLPALALLWSLVERPRDAALWGLFGVLLSHRWLLGLHPLTWMGLPAWLSLPVAVAIWLSCGVAAALLLLLWSLLARLCRRRDGTWRFGAVLLLALVWGAAELLLEGSPLFWIGVGGSVLPLDRPLAGLGRWLGSGGLATLQLLWGWGLWQLWRRRGRRCAWWLISLLLAHAMGALSLSPPPALAALRLGAWQPAIPTREKFSPERQRRFQSALSSALQQAQSLKVEALVAPEGTLPFRWQADEDPLPVPLISGGFRWVRGQQRSSVLLARPDRAGVEPLVDKHRLVPLGEWLPPLPAGLTRGLSAVGGLQPGDASRFVNVWPSPFAVAICYEISDGRALAKATAQGAEWLLTIANLDPYPQLLQRQFLALAQLRAIETGRDVLSVANTGPTALVSADGTVQRLLEPQTDAVAAAELQRRQQLTGYSRLVWAWSSR | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50507
Sequence Length: 465
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
Q7VAT8 | MLALSRSKYFAFLTGTVGGLLAGVGLSQGGVVFIWISTACLWASMAFPSAVFLWGLFAILLSYRWLLYLHPLTWIGVPIAFSLPIAILIWFSCGLLGGLLVALWSLIGQIPFFQRRLNSSTKDQLLYVIALSLIWGLVEVGLAKSPFFWFGLGDSLLPYDRWLAGLARWFGSGGLAALQLILGWWVWKIIFAFKKGSPWLGLFALGVCSLLLAHCIGWILLADNEFTSSKRIALWQTNIPTRQKFTLRELKRLPISLQDALEEADNLGADWMVAPEGTLSAGQNLLAPSPLPLLSGGFRRVKNKQMSSLLVFNEGSTSYSSAIDKHRLVPLGEWLPSLPGVNWNGLSFVGGVDPGDASRFFDWDGGPLAVAICYELSDGNNLAKAIFDGAEWILAIANLDPYPISLQRQFLALAQLRSIESARNLISVANTGPTSMILSSGKIKSIIEPFNEGVGVIDINVSQKISGYVRWGEIPLISSLLIVLCFIARLKGKA | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54005
Sequence Length: 494
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
Q7V8K1 | MGNDRSLALVQGAVGGVLAGIGIAHGGLLWMAPALALLWSACRFPVAASLWGFVAVLLSHRWLLALHPLTWVGVPAPLSVPVAASIWLFCGAAAAVLVGLWAWLGTSIAHLATREAGIRAQLSHALLMASIWGLAEVLLAGSPLFWIGVGGSLLPGDRALAGLARWFGAGGLATLQLLIGWWLWRTALAWRRGVGWRRSLLVGLLCLLLAHGFGWSLLRSSDATAPISVAAWQPAIPTRSKFSEEQQRRLPEALQNALDRADDLDAAWLVAPEGLLPPDAVLLRPAPLPLLSGGFRWLRGQQRSALLVVDRGERQASAFIDKHRLVPLGEWLPALPGGVFRGLSAVGGLQPGAASRLLQWPGPTAAVAICYELSNGAALAQAVADGAQWLLAVANLDPYPLALQRQFIALAQLRSIETARDLLSVANTGPSALVLATGKQQQLLAPFTEGVGLADLHFHQGISGYTRWREAPLIGLMLFAVVGLGLSRVRSWLISLMLC | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52990
Sequence Length: 499
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
Q7V0G7 | MINTQNKKFNKYFVPCLGGIFGGIATSTHFWLLFMPLSLFILWSRSDKKLANFLWGFFFILVSHSWLYELHPLTWLGFSWISSLIISISILFGCSIIGGILVYLWGLLVKKILQKKEISNMNSLRLTIKVLLLSFAWGIGEFILSQTPLFWIGLGEGIVPGDLYLAGLARWIGASGLCVVQLTIGFWIYLIYEKWKRKYHFKKTFLFGLLILVILHFLGGLTNPIERNNDYPVALWQTNMPTREKTNFKNQFINDKLISAQKIALSNDAKLLITPEGTLNNNFNLNFKSKIRMLAGGFRNSKNGLRSSLLGYQIGDKTYSSFIDKHRLVPLGEKIPGFLNIFSRGLSAVGGIQPGSDSRFFKWKFTQPLAIAICYEITDGFKIRNAVKSGAELIISAANLDPYPRKLHYQFLSLARVRSIENKKDNIIISNTGPSGLISEEGKIIKLFDPNTEQNDVVNPNFSIEKTFYTTYGERPLFLLCLFLIGLNLYFGKFTN | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56347
Sequence Length: 496
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
A4VPC2 | MSLLKNLLAPCLALLLAGCAALGPHESVEGPGNTAAWKEHRSHVATLDGWQISGKIGIRAPQESGSGTLFWLQRQDYFDIRLSGPLGRGATRLTGRPDAVSLEVAGQGRFEAESPEALVEAQLGWQLPVSHLLWWVRGLPAPDSRSRLSIDSESRLARLEQDGWQVEYLAYAEHNGFVLPERIRLQGHDLQITLVIKDWQPRQLGR | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22797
Sequence Length: 206
Subcellular Location: Cell outer membrane
|
Q3SLR7 | MRRLAVIASLAWALGGCATVAPPPQAAIPVPLADAWTLQGRLGVQTERESLSGQIRWQHGGGVDQVLLTSPLGQGVARIVRDPEGVSLELPGQPVRRATDVDTLTRDALGYELPVAGLAWWIQARPDPLREAAVALGDDGRPARIVQDGWTIDYLQYGADARPRKLVVSRAGLEIRLVADSWQSAP | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 19963
Sequence Length: 186
Subcellular Location: Cell outer membrane
|
C4LBL3 | MKLLQHLTLIFCLLILTACSSRQQQPDNTNWRQQREKLESVTHWTISGKLAIITPEKKGSVRIRWQQNGDDYHLNLTSLLGTRVMEMRKTGEQIVIIDDKGQEYRGTDAEYLVYRLTGWQMPVYKLPMWIKGLPGDTDYQINPNGQVTQIKTAQWQMQYQTYQPVDGWMMPENITFKGQQTELRLVINEWKLAK | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22788
Sequence Length: 194
Subcellular Location: Cell outer membrane
|
P57070 | MNALVRRLLPGLASLLLLAGCATAPLQPVNVQWQSHQVTLEQIQHYQLTGKLGYIAPDQRQSFNFQWQKSPQKLSLRLSNFLGQTVLNLQVDEQGARVETYDDQIYRDQDAQSLIRNLTGLDIPVEQLEDWILGLPTQATHYELNEQNTLATLTKLASTEEWHVEYQRYQAIEWQHQPIPLPDKLKLQQNKTSIQLVISQWTLLP | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23619
Sequence Length: 205
Subcellular Location: Cell outer membrane
|
Q87RN6 | MTLRSFLIFFLSSLILAGCSSVPESVTSVEWQAHEQRLETIHDFQATGKLGYIGPDQRQSLNFFWKHSTALSQLRLTTVLGQTALKLTITPQGATVETYDDQVLSARNANQLIYRLTGLMMPVDHMPDWLLGLPTDADTFQLSPANTLQTLDKQIGLNDWKIAYERYGDVEWHEQTLPLPNKLKLTTSDVKINLVITKWNITQ | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23004
Sequence Length: 203
Subcellular Location: Cell outer membrane
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Q1GFI8 | MSEVTLKIEGLRKTYLAGTPGEVAVLRGVDLTLHAGEVVALVAPSGAGKSTLLQIAGLLDVADAGRVEIAGQDMAGARDRKRTRVRRQDVGFVYQFHHLLPEFSALENIVLPQLANGISQRDAEARGAELLALVGLETRAAHRPAALSGGEQQRVAFCRALANRPRLLLADEPTGNLDPATSDQVFEVLMQLVSETGLSALIATHNLELAARMDRVLHLEDGVLVER | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24334
Sequence Length: 227
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q5PGR6 | MNKILLQCDNLCKRYQEGTVQTDVLHDVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFSGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEIDARAREMLHAVGLEHRATHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFELLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLMGAE | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25479
Sequence Length: 233
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q2S3A3 | MHRGAATQGLVFTTPLSPFILPFAVDTPLLQVDALLKQYDTGGDEPLTVLRDLDLAVQEGEILAIVGESGTGKSTLLHLLGALDRPTDGTVRFAGTDLFAKSDEELAAFRNRSIGFVFQFHHLLPEFTALENVAMPALIQHRSLADVTPRAHELLALLGLDDRADHRPRTLSGGEKQRVAIARALMNEPALVLMDEPTGNLDARTAEPLHREIERLSREMDHTFVLASHDPSLAEVAGRVLRLEHGTLHPLAAADEMAPEAGPSDDGHAGG | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29264
Sequence Length: 271
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q8EEV5 | MQDVLLQVQAVSKSYHDGDVTTQVLSDVDLQVFKGEQLAIVGTSGSGKSTLLHIMGTLDKPSSGKVLLAGEDLYQVSSARQAQIRNQDLGFIYQFHHLLPEFTALENVAMPAFIQGRDRTLAQADAKVLLERVGLGHRMSHIPAELSGGERQRVAIARALINKPKLVLADEPTGNLDAKSGEAVYELIRELANQLGTAFVVVTHDPKLAARMDRQLTMKNGYLQVPESAQ | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25066
Sequence Length: 230
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q2LVM2 | MIQVRNLKKTFIKDGNRIEVLRGLDLKIEDGTSLAILGVSGAGKTTFVHILGTLDHPTSGEVLFNGLDVFNWPEKKLASFRNRTIGFVFQFHNLLPEFSSLENTMMPALISGMPRRNALERAETLLHDVGLGDRMTHKPSELSGGEQQRVAVARALVMEPEILLADEPTGNLDTETGRKIEDILLELNRQKGITLIVVTHNQSLAGRMSRSIGLRDGEIVTCA | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24609
Sequence Length: 223
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q11QT1 | MLDTEPVDMIPLITPEEEAEMDKEEFPSVLPILPVRNIVLFPGVVLPITVGRQKSIRLVKKFYKGDRTIGVVAQENQKSEEPSFQDIFKVGTVAKILRMFVLPDGNTTIIIQGKRRFKIEEQVQDEPFMQAKVSMLKDIHPDMSKKEVKALLQSVKESATKILKMNPEIPQDAQIAINNIESENFLTHFLSSNINAELKDKQKLLEFDDAVERATWLLQLMDKDIQMLEIKREIHTKVHTDIDQQQRDYFLRQQIKVLQDELGDFSSEQEFERLKEKALTKKWSDKVRAHFDKEMSKLQRVNPMAPDYPVTFNYLELLVDLPWGENSTDNFDLVRAKEILDEDHFGLTKVKQRILEYLAVLKLKNNMKAPILCLYGPPGVGKTSLGKSIAKALDRKYIRMSLGGVHDESEIRGHRKTYIGAMPGKIIQGIKRSETSNPVFILDEIDKISKDFRGDPSSALLEVLDPEQNSSFMDNFLEVEYDLSKVLFIATSNALDTIQPALRDRMEIIEINGYTLEEKIQIAKKYLIPKQKEEHGLKAKDISFTDAAIVKIIEDYTRESGVRNLERKIGAVVRNIAVAIAMETAYTKKIQPAQVREILGSEDFEKDTYQQDDLAGIVTGLAWTPYGGEILTIESIISKGKGKLTLSGQLGDVMKESASAALSLLRANVDAIGIDHRVFDHFDLHVHVPAGATPKDGPSAGIALYTSLASTFTQRKIKPALAMTGEITLRGKVLPVGGIKEKILAAKRAGIKEIILSKKNKKDIEEIHPPDIADLKFHFVETADEVLAIALLKQKIKKPFNLEVPEEPKKKDK | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 91748
Sequence Length: 813
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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Q9RXG4 | MPDSTALPTTIPVCPVRGSVIYPTMVQHIDASRAISINAIEAAMSGEKVILIVSQRDKDVDDPKGEDLYDVGTACNVLRVRKNPDGTLQMLVSAVARVQVSAYQLGDYLTADIEPLDAGKSGGVELQALSRELKDKFETVASGGRINAESVQTINSKDDIGEMADHIAFNLDFKLEDKQAILEAANVTERLKKLLTLLDTEQEVQAVQAKIRAQVKEEIDKNQREYYLREQMKVIQKELQGGDEEEGDEAEAFRAKIDALGLNPEVKKEIDREVNRLARMHPDAAEASVIRTYLTWVTELPWNERSDDRLDVEEAAQVLDEDHYGLEKVKDRVLEFLAVRRLRKERAERGEISAEEVNKGPILVFTGPPGVGKTSIAQSIAKSLGRKYVRIALGGARDESDIRGHRRTYIGAMPGRIIQGIRTAGTKNPVILLDEVDKLGSSYQGDPSSALLEVLDPSQNQHFTDHYLGVPFDLSEVMFIATANYPEQIPAALMDRMEVIEFNSYIEQEKLEIAKRYLLPRQLLQNGLKPNQISFSDAALEKLISHYTREAGVRNLEREIGTVARKVARNIATGKTKRAKVTDKELEKYLGQPRHTPETENMEDMVGVSTGMFYTPVGGDILFVETSIMTGKGGGLLLTGQLGDVMKESARAALTYAKSNAERFHIDREKLDNSEIHVHVPAGAIPKEGPSAGGAMATSLISALTGIPARHDVAMTGEMTLTGRYLPIGGLKEKVLGARRAGIKHIILPKANERDINDIPLHLRSSMRFHPCETVDQVLDVALVGGLKALETPRTDSQVTPPADSGSKGRKTGRRSPEARA | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 90363
Sequence Length: 821
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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B8F9K1 | MAHTDTDDLVGLLDADDQNLDIPATLPMLPVRDVVVFTHMIIPLFVGRDKSVRAVDAAMAKDRFLFLATQMDGAVENPESDQIFKHGTAARILRVLKLPDGRVKVLVQGLAKAKIVRYTKKSDMFRVRIELLHEEDLGDLDMETEALMRNVKESCEKILGLRGELTPDVTMVLDGIDHPGRLADLVASNLNLKIEEAQSIFETIDPVQRLLAVNGFVSREVELSAMQARIQSSVRDEISKSQKDYFLREQMRAINRELGEMDEKTQEIKEYQDKIRKAKMPKEAKEEAERQLKRLEQMHPEAGEAPTVRTYLDWLVEVPWKKATKDTLDIKKAKEILEEDHYGLEKVKDRILEYLAVRKLNPKMKGPILCFVGPPGVGKTSLGKSIARAMGRKFYRLSLGGIRDEAEIRGHRRTYIGALPGRIIQGLKHCKSNNPVFMMDEIDKIGADFRGDPSSALLEALDPEQNFAFSDHYLNVPFDLSSVMFITTANMTDTIPSALLDRMEVINLAGYTENEKVLIAQQYLVPRQVKENGLKPEDITISGNALLKMATEYTSESGLRNLEREIGTLCRKVSRKIAEGKKGPYQITASSLVKYLGLEKFLPEMDQEEPQIGLATGLAWTHWGGEALYIETTLMRGKGELVLTGQLGEVMQESARAALSYARTNEDELEIDPDLFDNFDIHIHVPAGAIPKDGPSAGIAMTTALVSALTERPVANDIAMTGEVTIRGRVLPIGGLREKSLGALRAGIKTIIIPEKNKKELSEVPQQVRRKLKYITVSHVNEVLEKALLPAEKKKAPPKKKPPKKAAKPKAKKTQPKAKTTEAADK | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 92194
Sequence Length: 826
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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A8ZX50 | MAQPKIPEYKANGTTDKLPETVPIMPLSDGVLFPKMIIPVVITQNEYMTLIDEVMSGNRLVALITPKSGERKSDYGPGDLSPIGTLALILKMAKPDESRIHLMLQGISRIRTKNFIKTDPYLEAAFAQITENEKKDKETEGLMSNISNVYQELVRISPAIPNELGAMAVTIDEPGSLADMVASTINSSTEEKQNILETLDVKLRLKKVTRQLNHQLEILKLGDKIQSQIKEDMDKQQKEFYLRKQLKAIREELGEKEEGNVEAEEYRTKIEEGNLPEEAYKAATRELERFSRMHPSSSEYTVSSTYLDWLTTLPWDKQTEDHLDIKKARAILDKDHFGLEKPKKRILEYLAVRKLNPDSKGPILCFLGPPGTGKTSLGRSIARALGREFIRISLGGVRDEAEIRGHRRTYVGALPGRIIQEIRKAGTNNPVFMLDEIDKVGADFKGDPSSALLEVLDPEQNFSFADHYLDVSFDLSRVMFVATANVIDTIPPALRDRMEVIGLRGYTLEEKVKIARQYLIPRQRKENGLAAKHISFSQSAIRHIISDYTREAGLRNAEREIASVCRGVAAKIAEGKKVSGAIKPEDLYEYLGPVRFTSETGENALTPGVVMGLAWTPVGGEILFIEATSMKGKRGLTLTGQLGDVMKESATAALSFIRAHARDYDIDEDFFDKYDFHIHVPSGAIPKDGPSAGVTMLTALVSLLTGRKVKKGLAMTGEITLRGKVMPVGGIKEKVIAAHRAGIKEVILPRPNKKDLEEIPAKVKSAMKFHFAEKMGDVLELALNGNGATKKKKKTPAKSKKSTKPAAKKTAARKSRK | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 90649
Sequence Length: 817
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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A4J7L6 | MNSEIKSLPLLPLRGILVFPYMVIHLDVGREKSIQAIEEAMVQDRMIFLATQREAQTDEPTVDDIYNIGTVAEVKQLLKLPGGTIRVLVEGIARAKIEKYEHQDPYFRVEVQQYSEEFEKGAEVEALMRSLVYQFEQYVKLSKRIPPETVVSVVNLEEPGRLADIIASHLALKIEDKQNVLESVEIVDRLEKLCGIVAKELEIVELERKINIRVRKQMEKTQKEYYLREQMKAIQKELGEKDERVAECEEFREKISKAKFPKEAEEKALKEVERLEKMPPMAAEAAVVRNYLDWMLSLPWSKSTKDRIDINAAEEVLEADHYGLKDPKERITEYLAIRKLAKKMKGPILCLVGPPGVGKTSLGRSVARALDRKFVRISLGGVRDEAEIRGHRRTYVGAMPGRVIQGMRTAGSKNPVFLLDEIDKMASDFRGDPSSALLEVLDPEQNSTFSDHYIETPFDLSNVMFITTANNMYSIPRPLLDRMEVIQISGYTEEEKLQIAKRHLMPKQIKDHGLTEEMIQISENTILKVIREYTRESGVRNLERKIASICRKTAKKIVAGQAEKVKVTTQNLEQFLGIPRYRYGVAEQNDEVGTVTGMAWTEVGGDTLVIEVTTYKGTGRMTLTGKLGDVMKESAQAGYSFIRSRAQELGIDQEMFEKWDLHIHIPEGAIPKDGPSAGITMATAMASVLTGRKVRHDIAMTGEITLRGRVLPVGGIKEKVMAAHRAGIKLIILPNDNKKDLEDIPVNIKKQLEFKLVDHIDQVLAIALLEKEVVDTTTVLEPEAAVMDNPHFSAVDSQEVQQQGGTQLPS | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 91333
Sequence Length: 810
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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Q72CE6 | MTDTGREGLQNREEGFELPLMSLREVVMFPRSIVPLFVGREASIKAIESAISDYGKKIFLVAQREPELEKPGPEDLFEVGTVSKILQLLRLPDGTIKVLFEGLYRARWDGTADAIIGADDAYPRVRVTRIEQESSEDDDEALVRATHEALDEYGKINKKLAQETLVAISALSDAARLADAIMPHLKVDYRRKQELLEVESGAERLEKVYELLQGEIAVASLEKRIKSRVKNQMERNQREYYLNEQIKAIHKEMGREDDPQAEVNELEARLAEKSMPEEAREKALREMKKLRQMPPSSAEYTVVRNYVDWILDLPWNTLKETEIDIDNARSILDADHYGLEKPKERILEYLAVQKLVNRLKGPILCLVGPPGVGKTSLAKSVAKATGREFVRLSLGGVRDEAEIRGHRRTYVGALPGKIIQSLKRVKHNNPLFCLDEIDKMSTDFRGDPSSALLEVLDPEQNSTFNDHYLDMDYDLSQVFFITTANSLHSIPLPLQDRMEIIRLPGYLETEKRRIAHDFLLPKQVEAHGLAASNLRISDNAVLEIIRSYTREAGVRNLEREIASVCRKAAMQVVEAGDKEKTLTVSRQNLGNFLGVKKYRHGEREDTSQVGVCTGLAWTEMGGELLVVETALMPGSGRVEITGKLGDVMTESAKAALSYLRSRSDLFGLRPDFHKEIDIHVHVPEGATPKDGPSAGITLATSMVSALLGIPVRNDVAMTGEITLRGRVLPIGGLREKLLAAHRGQIGKVLVPRENEKDLKEVPGEILKGLEIVFVDHVDEVLPQALMAQAESIFGGRTQSTPLYAKLRKDAQDGGATMPTAQ | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 91617
Sequence Length: 821
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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A5EWF3 | MTDKIYPILPLRDVVVFPHVIVPLFIGREKSIAALDAAMNGSQELLLVPQRDPAVVEPTLADLHEIGSLGRIVQMAKLSDGTVKALVEGLYRVHLEALNDDEKMFSAKKRNMLEKNSTKSEEHDSIVEILIEEFAKYLRNQERSADELLETLRGINDIGRISDTIAAHMDFRIEERVHLLAMEDAYERSQRLMILLAQESEKNELNKKIKNRVKQQMERNQREYYLNEKIKAIQKELGEMDEAQNDIELLEAQIKKAKMPVDVEKKALSELNKLKQMSAMSSEANVIRNYLEWLIDYPWAIEKPARYDLEEAARILDRDHYGLEDVKERILEYLAVQKRINEHNQKEAGTIGKGPIICLIGPPGVGKTSLGKSIAEATGRDFDRIALGGLHDEAEIRGHRRTYIGALPGKIVQKLCKLGSNNPVILLDEIDKIGHDHHGDPAAALLEVLDPAQNHTFNDHYLETDIDLSNVLFIATANTLNISEPLLDRMEVIRLPGYTTQEKIQIAKRYIVPRQRKENVLKASEFKIKNGVLNDVIEDYTREAGVRNLEREIGKLARKSVRRLQEGKQKSILITPNNLKDFLGVAKYHRNDEDLQAKIGSVTGLAWTSVGGELLQIEGVAFSGKGRLTHTGQLGDVMQESIRTALSVVRSYLDDLDDNFRFDEYDIHLHLPEGATPKDGPSAGIAMATALLSALSKQAVRGDLAMTGEITLHGKVLAIGGLKEKLLAAQRGRLKMVLIPEDNLKDLDEIPEEVKAALEIVPVSHIHEVFDHAFVADHAPFKARIEQKSLPTVSAVMHETPAGRC | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 90289
Sequence Length: 805
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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B5YFG2 | MEERELNQTQDIPEVLPILPLRETVVYPQMLIPLIVGREKSIRLVEDALSGNKLIGMCMQKTPVEDPTPDDIYRIGTVGIIVRSLRFPDNTLRLFVQGLQRIRVIEFLETEPYFKAKVEVIEEKVEKTVEIEGMMRNLLNLFQKMASLIPQFPEELLINAMNIQEPGRLADFIAFNTNLNINEKQEILETIDVKERLQKVTYYLTRELEILEIANKIQNEVKNEIEKSQKEYFLRQQMKAIQKELGEIDPREMEINELRQKLQEAKLPPEAMKEAERELERLSLMPPGSAEYTVTRTYLDWLISLPWAISTEDNLDIKRAEEILNEDHYDLEKVKERILEYLAVRKLKSDMKGPILCFVGPPGVGKTSLGKSIARALGRKFVRISLGGIRDEAEIRGHRRTYVGALPGRIIQGIRKAESNNPVFMLDEIDKLGSDFRGDPAAALLEVLDPEQNNAFVDNYLGVPFDLSKVMFIATANVLYTIPPALLDRMEVIELPGYTEYQKMGIAKGFLIPRQLKEHGLEKEQIEFSDDAIRKIIREYTREAGVRNLEREIASIIRKVAKGIAEGSITEKVIVKVEDVPKYLGPEKYTYGMKGEKDEVGVATGLAWTEAGGDILFVEALVVEGKGNLILTGKLGEVMQESAKTALSYVRSKLKDLNVSYELLEKADIHVHVPSGAIPKDGPSAGVTIATAIASALTRRPVKKDIGMTGEITLRGKVLPVGGIREKVLAAHRAGLTAVIMPKENKKDLEEIPEEVKKEITFYFVEHADEVLNLALLEVKESAEQRNPERIG | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 89422
Sequence Length: 792
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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B2KCC0 | MIAENKDYVKPDVNTLPAVLPAVAIRDVVMFPGMSLPLSVSRSKSIAAINLALDSNKYVVAVAQKEAEVEDPKAEDIYRFGVLSEITQSLKMPDGSIKVFLQGIARVKIEHLDFNNIANSWFASVFYPADEKVSGPEVTALMRQLLDEFEEYATVSRRIAVEGVSFFRQIEDPSRLADTIASNIIVKTSDRQDVLEAVNPKDRLELLIKILANEVEIISLEEKIHSKVRAQIEKNQKEYYLNEQMKAIQKELSQKDDFQKEIDELRSKIKKNGLPKNAKESAEKELDRLAKMAPFSPESTVSRTYLDWLVNMPWNSSTNDILDLKKAKEVMDADHYGLDKPKERILEYLAVSKLTNSLKGPILCFAGPPGVGKTSLAKSIASAVGRKFVRMSLGGVRDESEIRGHRRTYIGSMPGRIIQGISKAKSNNPVFLLDEIDKMGSDWRGDPAAALLELLDPEQNKDFSDHYLDVPFDVSKVMFITTANSLSSIPVTLRDRLEIIDFSGYTEYEKEAIAQNHLIPRQMKEHGLKEGSLEIGLPAVKLIMRDYVREAGVRNFEREISTICRKAAKMYVENCGKTVTVTKDNLHDFLGVPRYTNFTTEENGVGISTGLAWTSVGGETLSIEASEISDGKGRIMLTGKLGDVMKESVHAALTYARSKGYGKGIDFNKTDFHIHFPEGAVPKDGPSAGTAVTTALISLLTKNPVKKNLAMTGEVTITGRVLPIGGVKEKFMAAYREGVKTILYPHTNEKDVSEVPEVIRKQLKLIPVKHMDEIVKIAFEKGEPKSSFKKSKTAPKKESAKKAAKSKKPAVKKPAVKKTKQVKKTAKKKK | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 92244
Sequence Length: 830
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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A7HK39 | MPNKNDNKGKYSRLEKEAKKAREEKISIPNVLPAIAMRSNMVIFPNTVVPFYVGREISLMALEEAMEKTNQIVFVVNQKDPAVETPTEKDLYKVGTIVRIIQVGKLPDETFKVLVEGIARAKWIKNVGEKFFKFEIEILRTRYGKSKRLIALMRMVKEELHKYVQYSRKIPPETLMLLEDVDNPDVFADIAASLCPGNIEEKQQLLEIVHPANRLERILDILARETELLEIEQQLDQKVKERIEKSQREYYLREKLRVIRDELGGEEDIEIKELKEKIENNNYPEFVKEKARAEINRLEKMSPYAPEATVVRTYLDWILNLPWHEKTDDTDDINFAEKVLNEDHYGLDEPKRRILEYLATRKVSQKAKAPIICFVGPPGVGKTSLAKSIARAMNRKFGRMSLGGLRDEAEIRGHRRTYVGAMPGRIMQLIRKLGVKNPVILLDEIDKMGISFQGDPASALLEVLDPEQNKEFVDHYIELPYDLSEVLFVTTANVLYTIPPALRDRMEVIEISSYTDVEKFYIAKNYIIPKIESEFVEKADEIFSFKDTAIKKIINEYTLEPGVRELEREIRSVVRKATLDAIKTGKKIVISPEKVTEYLGPSKIKDEDKLEKPMIGVTTGLAWTPNGGTTLYIESTLIPGNGGLIITGQLGDVMKESVRIALSLARKIVGDEYAEKFTKNDIHVHVPEGAVPKDGPSAGVTITTALVSVVKNIPVRNDIAMTGEITLRGRVLPVGGIKEKVMAAYRKGIYHVILPKKNEVDIEKVPEVVRTKMKFTFVETIEEVLEVALNEDNSKESRKGRTRKGNSNTK | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 92111
Sequence Length: 810
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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B0S2N4 | MKEYYTISEKKLPIIALRGLWLFPNNIQHFEVGREVSLNALNASLLRNSEIFICTQKDPMLENITKEDFYHTGVLASIKQTIKMPNGNIRVLVEAYDRAKIVDFVENDSFLEANVEVMEYDKTKYHPTDKSLTMIRMIISSFESLAEIIKKPLPQDLLGGLLNEEDPSSLIDTIAMLISLNDKDSILLLETLDMDERIELVYKFVIKEIEFLKIKEDIEERTNKEISDTQKEYFLQEQLRQIKMELGEEYDIEDTDDYANRVKKLKLKKDSEEHVLKEINRLSSMNPNNPESTVIRNYIDQVLDIPWNKKSKSSIDLKVAEKVLNDGHFGLEDVKKRILEYLAVKKMTGSLKGPILCLVGPPGVGKTSIARSIADATNRKFVSMRLGGVRDEAEIRGHRKTYIGAMPGRIITQLQKAKKLNPVFLLDEIDKLASDFRGDPASALLEVLDPEQNSEFTDNYIEIPVDLSDVLFITTANSQEQIPDALLDRMEVIRVTSYTDSEKFEIANRYLLPRQLKENGMDKSQFHITRDAIYTIINNYTRESGVRELERNIGKVIRKAVVKIVKDDVKKVVVNNKNLEKFLGSKLVLDDEIPREDTVGVVNGLAWTQVGGVILTIEANVMDGSGKTQLTGKLGDVMKESAMAAISYIRSNQEALGIKGEFYKEKDIHIHVPEGAVPKDGPSAGVTMVTALVSALTGRKVKHDFAMTGEITLTGRVLAIGGVKEKVLAAHRYGINKVFLPKENKRDIQDIDPKIRQKIKFYFTSNVKEILDEVLI | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 87866
Sequence Length: 776
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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Q0RPW3 | MTQLPHVRVDHMPQIRVLPVLPLDDAVVLPGMVVSLDMSDEQTRAAVDAARTGGSAGSSDARAPGISSRAAGRPAEVLLVPRVGGELAEVATVGVIEQVGRLPRGGSAAVVRGTARAQVGGVRPAPAGTDTTGTGTADATSGAGSGAGVQWVDAVVLDDSAATPFGALDDPAGTRAGSPADEAARVDKLAKEYRALVTDLLRQRGAWQVVDSVSAITDPGTLADTAGYSSYLTTAQKIELLGTPAVGTRLERLLTWTKEHLAEQDVAETIRRDVQEGMDRQQREFLLRRQLEAVRKELSELDGSGGGADGASGSEPADYRARVEAADLPEKVRAAALKEVDKLERTSDSSPEGGWIRTWLDTVLDLPWNVRAEDSYDIIAARAVLDADHAGLDDVKDRIIEHLAVRRRRADAGLGVVGGRRGGAVLALAGPPGVGKTSLGESIARAMGRSFVRVALGGVRDEAEIRGHRRTYVGALPGRIVRAIREAGSMNPVVLLDEVDKLGADYRGDPTAALLEVLDPEQNHTFRDHYLEVELDLSDVLFLATANVLEAIPAPLLDRMELIRLDGYTEDEKVVIARDHLLHRQLDRAGLAEGDVSVGDDALHALAGEYTREAGVRDLERSIARLLRKVVAQVALGAAALPVTIDAGDLTGYLGRPRHTPESAERTALPGVATGLAVTGAGGDVLFVEASLADAETGGGGITLTGQLGDVMKESAQIALSYLRSHGVELELPVGDLADRGVHVHVPAGAVPKDGPSAGVTMTTALASLLSGRPVRADVAMTGEVSLTGRVLPIGGVKQKLLAAHRAGLTTVLLPQRNGPDLDDVPAPVRDALTVHLVTDVREVLDLALEPAFDADHGGRSPGRAGHSPTALAA | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 91415
Sequence Length: 874
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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B0TZA7 | MSEVLNVVPVIPLRDVVIYPSMTLPLNVGRKKSIEAVKQASNSYNNYILLATQKNGSSSGDVVDNIYDIGTLAKVVQIMKLPDGSLKIIVEGIAKRLVAKYESIDGCIYANLDSLHIDDNYDPSQIDKELKAILLSITDSLKKFVDISGKVSKESLATLINTEEPHKFIYEISTILNTEIAKKQKILEATDIKNKALLLLSCLYEELEILELEAKIKDRVKSQVDKNQREYYLNEQVKAIYKELGEADEESEVTALKSRIEATKMSKEAKEKCLKELKKLKAMPPSSSESAVSRNYIETILSLPWGKKAKVKKDINLAEKVLEKDHYGIKKVKERILEHLAVQIKRDTNAKAPILCLVGPPGVGKTSIGQSIARATGREYVRMALGGVRDESEIRGHRRTYIGSMPGQIIQKIIKSKTENPLFLLDEIDKISSDFRGDPSAALLEVLDPEQNSTFNDHYLEIDYDLSKVMFVATANSLDIDPALRDRLEIIHLSGYTEIEKQAIAKQYLVPKALENNGLTKNEINFTPKATLDIIRYYTREAGVRNLQQKIDGVCRKAVKNLLKDPEHGKVSITQNNLEDYLGVHQFDYGIKNAKPKVGQVTGLAWTSVGGELLTIEALAMPGKGKVKYTGSLGDVMKESIDAAFSVVRSISKDYKLEDDFYEKKDIHIHVPEGATPKDGPSAGIAMTTALVSVYTNKPVRNDIAMTGEVTLRGDVLAIGGLKEKLLAALRGGIKEVLIPKQNVKNLADVDKEILEKLEITPVNSIKEVLERVF | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 85998
Sequence Length: 774
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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Q8RHK0 | MLKAPFLPIRDLVIFPNVVTPIYVGRANSIATLEKAIANKTKLVLGLQKDASQENPTFDGDIYEVGVIANIVQIIRMPNNNIKVLVEAEDRVKIKNIEKEENEYVTTYTVIKETLKDSKETEAIYRKVFTRFEKYVSMIGKFSSELILNLKKIEDYSNGLDIMASNLNISSEKKQEILEISNVRDRGYRILDEIVAEMEIASLEKTIDDKVKNKMNEAQRAYYLKEKISVMKEELGDFSQDDDVIEIVDRLKNTELPKEVREKLEAEVKKLTKMQPFSAESSVIRNYIEAVLELPWNSETNDVLDLKKASQILERDHYGLKDAKEKVLDYLAVKKLNPSMNGVILCLSGPPGIGKTSLVKSIAESMGRKFVRVSLGGVRDEAEIRGHRRTYVGSMPGKIMKAMKEAGTNNPVMLLDEIDKMSNDFKGDPASAMLEVLDPEQNKNFEDHYIDMPFDLSKVFFVATANDLRNVSAPLRDRMDILQLSSYTEFEKLHIAQKFLLKQAQKENGLANIDIKIPDKVMFKLIDEYTREAGVRNLKREIITICRKLAREVVEKDTKKFNLKPTDLEKYLGKAKFRPEKSRKATGKIGVVNGLAWTAVGGVTLDVQGVDTPGKGEVTLTGTLGNVMKESASVAMTYVKANLKKYPPKDKDFFKDRTIHLHFPEGATPKDGPSAGITITTAIVSVLTNKKVRQDIAMTGEITITGDVLAIGGVREKVIGAHRAGIKEVILPEDNRVDTDEIPDELKSTMKIHFAKTYDDVSKLVFVK | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 86349
Sequence Length: 768
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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P58215 | MRPVSVWQWSPWGLLLCLLCSSCLGSPSPSTGPEKKAGSQGLRFRLAGFPRKPYEGRVEIQRAGEWGTICDDDFTLQAAHILCRELGFTEATGWTHSAKYGPGTGRIWLDNLSCSGTEQSVTECASRGWGNSDCTHDEDAGVICKDQRLPGFSDSNVIEVEHHLQVEEVRIRPAVGWGRRPLPVTEGLVEVRLPDGWSQVCDKGWSAHNSHVVCGMLGFPSEKRVNAAFYRLLAQRQQHSFGLHGVACVGTEAHLSLCSLEFYRANDTARCPGGGPAVVSCVPGPVYAASSGQKKQQQSKPQGEARVRLKGGAHPGEGRVEVLKASTWGTVCDRKWDLHAASVVCRELGFGSAREALSGARMGQGMGAIHLSEVRCSGQELSLWKCPHKNITAEDCSHSQDAGVRCNLPYTGAETRIRLSGGRSQHEGRVEVQIGGPGPLRWGLICGDDWGTLEAMVACRQLGLGYANHGLQETWYWDSGNITEVVMSGVRCTGTELSLDQCAHHGTHITCKRTGTRFTAGVICSETASDLLLHSALVQETAYIEDRPLHMLYCAAEENCLASSARSANWPYGHRRLLRFSSQIHNLGRADFRPKAGRHSWVWHECHGHYHSMDIFTHYDILTPNGTKVAEGHKASFCLEDTECQEDVSKRYECANFGEQGITVGCWDLYRHDIDCQWIDITDVKPGNYILQVVINPNFEVAESDFTNNAMKCNCKYDGHRIWVHNCHIGDAFSEEANRRFERYPGQTSNQII | Cofactor: Contains 1 lysine tyrosylquinone.
Function: Protein-lysine 6-oxidase that mediates the oxidation of peptidyl lysine residues to allysine in target proteins . Catalyzes the post-translational oxidative deamination of peptidyl lysine residues in precursors of elastin and different types of collagens, a prerequisite in the formation of cross-links between collagens and elastin . Required for somite boundary formation by catalyzing oxidation of fibronectin (FN1), enhancing integrin signaling in myofibers and their adhesion to the myotendinous junction (MTJ) (By similarity). Acts as a regulator of inflammatory response by inhibiting differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): acts by interacting with STAT3 in the nucleus and catalyzing both deacetylation and oxidation of lysine residues on STAT3, leading to disrupt STAT3 dimerization and inhibit STAT3 transcription activity . Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated . Also able to catalyze deacetylation of lysine residues on STAT3 .
PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.
Catalytic Activity: H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+)
Sequence Mass (Da): 83166
Sequence Length: 753
Subcellular Location: Secreted
EC: 1.4.3.-
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Q9Z175 | MRAVSVWYCCPWGLLLLHCLCSFSVGSPSPSISPEKKVGSQGLRFRLAGFPRKPYEGRVEIQRAGEWGTICDDDFTLQAAHVLCRELGFTEATGWTHSAKYGPGTGRIWLDNLSCRGTEGSVTECASRGWGNSDCTHDEDAGVICKDQRLPGFSDSNVIEVEHQLQVEEVRLRPAVEWGRRPLPVTEGLVEVRLPEGWSQVCDKGWSAHNSHVVCGMLGFPGEKRVNMAFYRMLAQKKQHSFGLHSVACVGTEAHLSLCSLEFYRANDTTRCSGGNPAVVSCVLGPLYATFTGQKKQQHSKPQGEARVRLKGGAHQGEGRVEVLKAGTWGTVCDRKWDLQAASVVCRELGFGTAREALSGARMGQGMGAIHLSEVRCSGQEPSLWRCPSKNITAEDCSHSQDAGVRCNLPYTGVETKIRLSGGRSRYEGRVEVQIGIPGHLRWGLICGDDWGTLEAMVACRQLGLGYANHGLQETWYWDSGNVTEVVMSGVRCTGSELSLNQCAHHSSHITCKKTGTRFTAGVICSETASDLLLHSALVQETAYIEDRPLHMLYCAAEENCLASSARSANWPYGHRRLLRFSSQIHNLGRADFRPKAGRHSWVWHECHGHYHSMDIFTHYDILTPNGTKVAEGHKASFCLEDTECQEDVSKRYECANFGEQGITVGCWDLYRHDIDCQWIDITDVKPGNYILQVVINPNFEVAESDFTNNAMKCNCKYDGHRIWVHNCHIGDAFSEEANRRFERYPGQTSNQIV | Cofactor: Contains 1 lysine tyrosylquinone.
Function: Protein-lysine 6-oxidase that mediates the oxidation of peptidyl lysine residues to allysine in target proteins . Catalyzes the post-translational oxidative deamination of peptidyl lysine residues in precursors of elastin and different types of collagens, a prerequisite in the formation of cross-links between collagens and elastin . Required for somite boundary formation by catalyzing oxidation of fibronectin (FN1), enhancing integrin signaling in myofibers and their adhesion to the myotendinous junction (MTJ) . Acts as a regulator of inflammatory response by inhibiting differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): acts by interacting with STAT3 in the nucleus and catalyzing both deacetylation and oxidation of lysine residues on STAT3, leading to disrupt STAT3 dimerization and inhibit STAT3 transcription activity . Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated (By similarity). Also able to catalyze deacetylation of lysine residues on STAT3 (By similarity).
PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.
Catalytic Activity: H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+)
Sequence Mass (Da): 83740
Sequence Length: 754
Subcellular Location: Secreted
EC: 1.4.3.-
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Q96JB6 | MAWSPPATLFLFLLLLGQPPPSRPQSLGTTKLRLVGPESKPEEGRLEVLHQGQWGTVCDDNFAIQEATVACRQLGFEAALTWAHSAKYGQGEGPIWLDNVRCVGTESSLDQCGSNGWGVSDCSHSEDVGVICHPRRHRGYLSETVSNALGPQGRRLEEVRLKPILASAKQHSPVTEGAVEVKYEGHWRQVCDQGWTMNNSRVVCGMLGFPSEVPVDSHYYRKVWDLKMRDPKSRLKSLTNKNSFWIHQVTCLGTEPHMANCQVQVAPARGKLRPACPGGMHAVVSCVAGPHFRPPKTKPQRKGSWAEEPRVRLRSGAQVGEGRVEVLMNRQWGTVCDHRWNLISASVVCRQLGFGSAREALFGARLGQGLGPIHLSEVRCRGYERTLSDCPALEGSQNGCQHENDAAVRCNVPNMGFQNQVRLAGGRIPEEGLLEVQVEVNGVPRWGSVCSENWGLTEAMVACRQLGLGFAIHAYKETWFWSGTPRAQEVVMSGVRCSGTELALQQCQRHGPVHCSHGGGRFLAGVSCMDSAPDLVMNAQLVQETAYLEDRPLSQLYCAHEENCLSKSADHMDWPYGYRRLLRFSTQIYNLGRTDFRPKTGRDSWVWHQCHRHYHSIEVFTHYDLLTLNGSKVAEGHKASFCLEDTNCPTGLQRRYACANFGEQGVTVGCWDTYRHDIDCQWVDITDVGPGNYIFQVIVNPHYEVAESDFSNNMLQCRCKYDGHRVWLHNCHTGNSYPANAELSLEQEQRLRNNLI | Cofactor: Contains 1 lysine tyrosylquinone.
Function: May modulate the formation of a collagenous extracellular matrix.
PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.
Sequence Mass (Da): 84483
Sequence Length: 756
Subcellular Location: Secreted
EC: 1.4.3.-
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Q924C6 | MMWPQPPTFSLFLLLLLSQAPSSRPQSSGTKKLRLVGPTDRPEEGRLEVLHQGQWGTVCDDDFALQEATVACRQLGFESALTWAHSAKYGQGEGPIWLDNVRCLGTEKTLDQCGSNGWGVSDCRHSEDVGVVCHPRRQHGYHSEKVSNALGPQGRRLEEVRLKPILASAKRHSPVTEGAVEVRYDGHWRQVCDQGWTMNNSRVVCGMLGFPSQTSVNSHYYRKVWNLKMKDPKSRLNSLTKKNSFWIHRVDCLGTEPHLAKCQVQVAPGRGKLRPACPGGMHAVVSCVAGPHFRRQKPKPTRKESHAEELKVRLRSGAQVGEGRVEVLMNRQWGTVCDHRWNLISASVVCRQLGFGSAREALFGAQLGQGLGPIHLSEVRCRGYERTLGDCLALEGSQNGCQHANDAAVRCNIPDMGFQNKVRLAGGRNSEEGVVEVQVEVNGVPRWGTVCSDHWGLTEAMVTCRQLGLGFANFALKDTWYWQGTPEAKEVVMSGVRCSGTEMALQQCQRHGPVHCSHGPGRFSAGVACMNSAPDLVMNAQLVQETAYLEDRPLSMLYCAHEENCLSKSADHMDWPYGYRRLLRFSSQIYNLGRADFRPKAGRHSWIWHQCHRHYHSIEVFTHYDLLTLNGSKVAEGHKASFCLEDTNCPSGVQRRYACANFGEQGVAVGCWDTYRHDIDCQWVDITDVGPGDYIFQVVVNPTNDVAESDFSNNMIRCRCKYDGQRVWLHNCHTGDSYRANAELSLEQEQRLRNNLI | Cofactor: Contains 1 lysine tyrosylquinone.
Function: May modulate the formation of a collagenous extracellular matrix.
PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.
Sequence Mass (Da): 84779
Sequence Length: 757
Subcellular Location: Secreted
EC: 1.4.3.-
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P24095 | MFGIFDKGQKIKGTVVLMPKNVLDFNAITSIGKGGVIDTATGILGQGVSLVGGVIDTATSFLGRNISMQLISATQTDGSGNGKVGKEVYLEKHLPTLPTLGARQDAFSIFFEWDASFGIPGAFYIKNFMTDEFFLVSVKLEDIPNHGTIEFVCNSWVYNFRSYKKNRIFFVNDTYLPSATPAPLLKYRKEELEVLRGDGTGKRKDFDRIYDYDVYNDLGNPDGGDPRPILGGSSIYPYPRRVRTGRERTRTDPNSEKPGEVYVPRDENFGHLKSSDFLTYGIKSLSHDVIPLFKSAIFQLRVTSSEFESFEDVRSLYEGGIKLPTDILSQISPLPALKEIFRTDGENVLQFPPPHVAKVSKSGWMTDEEFAREVIAGVNPNVIRRLQEFPPKSTLDPTLYGDQTSTITKEQLEINMGGVTVEEALSTQRLFILDYQDAFIPYLTRINSLPTAKAYATRTILFLKDDGTLKPLAIELSKPHPDGDNLGPESIVVLPATEGVDSTIWLLAKAHVIVNDSGYHQLVSHWLNTHAVMEPFAIATNRHLSVLHPIYKLLYPHYRDTININGLARQSLINADGIIEKSFLPGKYSIEMSSSVYKNWVFTDQALPADLVKRGLAIEDPSAPHGLRLVIEDYPYAVDGLEIWDAIKTWVHEYVSLYYPTDAAVQQDTELQAWWKEAVEKGHGDLKEKPWWPKMQTTEDLIQSCSIIVWTASALHAAVNFGQYPYGGLILNRPTLARRFIPAEGTPEYDEMVKNPQKAYLRTITPKFETLIDLSVIEILSRHASDEIYLGERETPNWTTDKKALEAFKRFGSKLTGIEGKINARNSDPSLRNRTGPVQLPYTLLHRSSEEGLTFKGIPNSISI | Cofactor: Binds 1 Fe cation per subunit. Iron is tightly bound.
Function: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure.
Catalytic Activity: (9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-octadecadienoate
Sequence Mass (Da): 96817
Sequence Length: 864
Pathway: Lipid metabolism; oxylipin biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.13.11.58
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Q44467 | MNNNDIEYNAPSEIKYIDVVNTYDLEEEASKVVPHGGFNYIAGASGDEWTKRANDRAWKHKLLYPRLAQDVEAPDTSTEILGHKIKAPFIMAPIAAHGLAHTTKEAGTARAVSEFGTIMSISAYSGATFEEISEGLNGGPRWFQIYMAKDDQQNRDILDEAKSDGATAIILTADSTVSGNRDRDVKNKFVYPFGMPIVQRYLRGTAEGMSLNNIYGASKQKISPRDIEEIAGHSGLPVFVKGIQHPEDADMAIKRGASGIWVSNHGARQLYEAPGSFDTLPAIAERVNKRVPIVFDSGVRRGEHVAKALASGADVVALGRPVLFGLALGGWQGAYSVLDYFQKDLTRVMQLTGSQNVEDLKGLDLFDNPYGYEY | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of (S)-lactate (L-lactate) to pyruvate, with a reduction of O2 to H2O2 . Cannot oxidize D-lactate, glycolate, and D,L-2-hydroxybutanoate . May be involved in the utilization of L-lactate as an energy source for growth (By similarity).
Catalytic Activity: (S)-lactate + O2 = H2O2 + pyruvate
Sequence Mass (Da): 40933
Sequence Length: 374
EC: 1.1.3.-
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F4G5A4 | MSPSDRIPPGVWNAIDYERLAPQAMDAGRHAYVAGGCGWDATVAANRAAFAGWAVLPRLLRDVRAGHTRLQLAGMDLPHPLLLAPVAHQRLAHPDAEIATARAAQATGSCLVASTLSSCTLEDIAAASGPARWFQLYLQPEREHSLDLLRRAEAAGYRAIVLTLDASIQLASRGALQAGFAMPADCVSANLARYPQPAPAQPAAGESRIFQGAMRHAPRWDDLRWLLASTRLPVWIKGVLHPEDARELQAAGAAGLIVSNHGGRSLDGAPASLRMLPALRTAVGAGYPLLLDGGVRSGQDAFKALALGADAVLVGRLQVYALAVAGALGVAHMLQMLVEELHACMAQAGCARLSDITHDTLTPSC | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of (S)-lactate (L-lactate) to pyruvate, with a reduction of O2 to H2O2. To a lesser extent is also able to use glycolate as substrate.
Catalytic Activity: (S)-lactate + O2 = H2O2 + pyruvate
Sequence Mass (Da): 38409
Sequence Length: 365
EC: 1.1.3.-
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F8WQN2 | MADLSFLNLEEVEEEAKKVMPKMAFDYYSTGSDTCYTVGENRSCFSRYLLLPRMLRNVSRVDTSHELFGIRSSMPVWVAPMAMHGLAHPGREVATCRAAAAAGVPFTFSTVATSSLQEIQETGHDNRIFQLYVIRNREVVRRWVTEAESRGFKALMVTVDAQRLGNREADARNKFTLPPGLALRNLEYLSSASTVQARDSQDGSGLMKLFTSEVDDSLTWEFIPWLRGVTKLPIIVKGLLSPADAELAVQYGVDGIVVSNHGGRQLDYAPSGLHMLPAVVAAVRGCGSSIPVLVDGGVRRGTDVIKALALGASGVLLGRPVLYGLAVGGQAGVERVLQLLRSEIELSMALAGCSSVQQIGPQLLLPAPSAGPAPPMPAAQLCKL | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of (S)-lactate (L-lactate) to pyruvate, with a reduction of O2 to H2O2. Also shows a low oxidase activity with glycolate in vitro. The very low glycolate oxidase activity indicates that this enzyme is unlikely to be involved in photorespiratory glycolate metabolism, a pathway in which the oxidation of glycolate is taken over by glycolate dehydrogenase (GlcD).
Catalytic Activity: (S)-lactate + O2 = H2O2 + pyruvate
Sequence Mass (Da): 41308
Sequence Length: 384
EC: 1.1.3.-
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A0A5N1I561 | MTVYYKGFPQSDRNEAIKMVNVDELEDRVRKVMPEAAYYYIASGSENEWTWRNNTAAFNHFQIVPRSLTNMDNPSTETQFMGMDLKTPIMICPIACHGIAHKDAEVATAQGAKAAGALFSSSTYANRSVEDIATATGDSPKFFQLYLSKDWDFNKMVFDAVKSAGYKGIMLTVDALVSGYREANLRTNFTFPVPLDFFTRYVGAEGEGMSVAQMYANSAQKIGPADVAKIKEMSGLPVFVKGVMNAEDAYMAIGAGADGIVVSNHGGREIDTAPATIDMLPEIAAAVNGRVPIILDSGVRRGSHVFKALALGADLVGIGRPFLYGLALGGAKGVESVINQINNEFKILMQLTGCKTVEDVKHADIRQINYTADNLPSNTDPSVRRAYPVTKENQMEGTQDAATGASKH | Cofactor: Binds 1 FMN per subunit.
Function: Oxidase that catalyzes the oxidation of a broad range of 2-hydroxyacids in vitro, such as (S)-lactate, 2-hydroxyoctanoate, and to a lesser extent glycolate, mandelate and 2-hydroxyoctadecanoate, to the corresponding 2-oxoacids, with a reduction of O2 to H2O2 . May be involved in the utilization of L-lactate as an energy source for growth (By similarity).
Catalytic Activity: a (2S)-2-hydroxycarboxylate + O2 = a 2-oxocarboxylate + H2O2
Sequence Mass (Da): 44229
Sequence Length: 408
EC: 1.1.3.-
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C2K1F0 | MVDAVKADPFGKVNAIDVLDLASLEARAEKVLGRGEFGYISEGSDDGYTMHRNTTAFQDVHMLPRVLQGVENPDQSTTFMGAKLASPLLTAPIASNTLAHPSGELGLAKGAKEAGIMMSQSTFASKTIAETAAVSDGAPYMFQLYMPKDWEYCQYLLDEAKQAGALAIILTADSTLGGYREKDVMNHYHLKGRLANLEGYNTGQSGVGAGGLFKESMQKLDLGLISKLASYSGLPIIIKGIQHPADAVAAITAGAAGIYVSNHGGRQLDGAPGAIEQLPAIAAAVDHRVPIIFDGGVQRGTHVLKALALGADLVGIGRPFSYGLALGGWQGVKDVADHLKMEINIAMQLTGCQTMADVKQMKVKTTFA | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of (S)-lactate (L-lactate) to pyruvate, with a reduction of O2 to H2O2. To a lesser extent is also able to use 2-hydroxyoctanoate as substrate . May be involved in the utilization of L-lactate as an energy source for growth (By similarity).
Catalytic Activity: (S)-lactate + O2 = H2O2 + pyruvate
Sequence Mass (Da): 38777
Sequence Length: 368
EC: 1.1.3.-
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B1HZY7 | MTNTTDGDLLLKNITAQAPFPICFADLEKAVAEKIPAGPFGYIRSGAGGEQTLRNNRSAFEKYSIVPRFLNDVSNVHTSINLFGKTYPTPLLFAPVGMNGMVHEEGELAAVRAAQQLNMPYIQSTVSTYALEDVAEAAPSATKWFQLYWSTNEEIAFSMAARAESAGFEAIVLTVDTVMLGWREEDVRNQFSPLKLGYAKGNYINDPVFMASLPNDSFESYVQGVLQNVFHPTLNWEHVRELKRRTNLPILLKGILHPEDAKLAIVNGVDGIIVSNHGGRQLDGVIGSLDALPSIVSAVKGQIPIILDSGVYRGMDALKALALGADAVAIGRPFIYGLALEGQQGVERVMTNIYDELKVSIALAGTTSIEGLRTITLVKNDGMEVK | Cofactor: Binds 1 FMN per subunit.
Function: Oxidase that catalyzes the oxidation of a broad range of 2-hydroxyacids in vitro, such as (S)-lactate, 2-hydroxyoctanoate, mandelate, 2-hydroxyoctadecanoate and (S)-2-hydroxyglutarate, to the corresponding 2-oxoacids, with a reduction of O2 to H2O2 . May be involved in the utilization of L-lactate as an energy source for growth (By similarity).
Catalytic Activity: a (2S)-2-hydroxycarboxylate + O2 = a 2-oxocarboxylate + H2O2
Sequence Mass (Da): 41916
Sequence Length: 386
EC: 1.1.3.-
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Q8Z0C8 | MTAISSPINLFEYEQLAKTHLSQMAFDYYISGAGDEITLQENRAVFERIKLRPRMLVDVSQINLTTSVLGQPLQLPLLIAPMAFQCLAHTEGELATAMAAASAGTGMVLSTLSTKSLEEVAEVGSKFSPSLQWFQLYIHKDRGLTRALVERAYAAGYKALCLTVDAPVLGQRERDRRNEFVLPPGLHLANLTTISGLNIPHAPGESGLFTYFAQQLNPALTWDDLEWLQSLSPLPLVLKGILRGDDAARAVEYGAKAIVVSNHGGRQLDGAIASLDALPEIVAAVNGKAEVLLDGGIRRGTDIIKALAIGAQAVLIGRPVLWGLAVGGQAGVSHVISLLQKELNVAMALIGCSQLQDIDTSFLHL | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of (S)-lactate (L-lactate) to pyruvate, with a reduction of O2 to H2O2. In extant N2-fixing cyanobacteria such as Nostoc, this enzyme primarily serves as an O2-scavenging enzyme, protecting nitrogenase that is extremely sensitive to O2, and is therefore an essential partner in N2 fixation. Also shows clear oxidase activity with glyoxylate in vitro, and low activity with glycerate, hydroxypyruvate and glycolate. The very low glycolate oxidase activity indicates that this enzyme is unlikely to be involved in photorespiratory glycolate metabolism, a pathway that seems to exist in this cyanobacterium, but in which the oxidation of glycolate is taken over by glycolate dehydrogenase (GlcD). Is not able to use D-lactate as substrate and does not show any dehydrogenase activity with NAD(+) or NADP(+).
Catalytic Activity: (S)-lactate + O2 = H2O2 + pyruvate
Sequence Mass (Da): 39165
Sequence Length: 365
EC: 1.1.3.-
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Q8RNT4 | MKRRSVLLSGVALSGTALANDSIFFSPLKYLGAEQQRSIDASRSLLDNLIPPSLPQYDNLAGKLARRAVLTSKKLVYVWTENFANVKGVPMARSVPLGELPNVDWLLKTAGVIVELIVNFVASLPASAAAQFERIAAGLSGDLEAARQVHEALLEEAKNDPAAAGSLLLRFTELQTRVIALLTRVGLLVDDILKSASNLVTQGGQGDGLNRFRAVFGTLRLPEVADSFRDDEAFAYWRVAGPNPLLIRRVDALPANFPLGEEQFRRVMGADDSLLEAAASRRLYLLDYAELGKLAPSGAVDKLLTGTGFAYAPIALFALGKDRAGLLPVAIQCGQDPATHPMFVRPAESESDLYWGWQMAKTVVQVAEENYHEMFVHLAQTHLVSEAFCLATQRTLAPSHPLHVLLAPHFEGTLFINEGAARILLPSAGFIDVMFAAPIQDTQATAGGNRLGFDFYRGMLPESLKARNVDDPAALPDYPYRDDGLLVWNAIRQWAADYVAVYYASDGDVTADVELAAWVGEVIGSGKVAGFRPITGRSQLVEVLTMVIFTASAQHAAVNFPQPSMMTYAPAICAMSAAPAPDSPSGKSEADWLKMMPPTLVALEKVNIYHLLGSVYHGRLGDYRQTGFPYAPVFSDRRVTASGGPLERFQARLKEVEATIRTRNQARRKPYEYLLPSRIPASTNI | Cofactor: Binds 1 Fe cation per subunit.
Function: In presence of oxygen, converts linoleate into (9S)-hydroperoxy-10,12-octadecenoate (9HPOD), which spontaneously decomposes to the corresponding 9-hydroxy-10,12-octadecenoate (9HOD), and into 13-hydroperoxy-9,11-octadecenoate (13HPOD) which spontaneously decomposes to the corresponding 13-hydroxy-9,11-octadecenoate (13HOD). Also active on linolenate. To a lesser extent, is also able to convert oleate into (10S)-hydroperoxy-8E-octadecenoate, which spontaneously decomposes to the corresponding 10-hydroxy-8E-octadecenoate. Is almost not active on arachidonate.
Catalytic Activity: (9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-octadecadienoate
Sequence Mass (Da): 74519
Sequence Length: 685
Subcellular Location: Periplasm
EC: 1.13.11.12
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B7RR92 | MESADLRDPDGMPVTLSDFEIDAAGRLSADLLAYLEGGAEAGQSVTENRAAFGRIGLLPKLLSPCAGGHTRTTILGKQAPHPIMVAPMAFQNLFHPQGESATAMAAAAQDATMVLSCQTSTPPEDIATIPGRRWFQLYMQADHEATMALVTRAVDCGADALVVTLDAPINGLRDREVAAGFTLPDDVRPVMLDVLPQPPRPHLRDGQSVVFDGMMVFAPTADDLARLIADSPVPVIVKGCLRPADATRLIDLGAQGIIVSNHGGRVLDTVPAPITQLAAVVDAVAGAVPVYVDGGIRRGSDVFKALALGAQAVLVGRPVMHGLIVDGPRGASQVLRRLRDELEVTMALCGCATVADITPDLLTGFSGTGS | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of (S)-lactate (L-lactate) to pyruvate, with a reduction of O2 to H2O2. Is also able to use glycolate and to a lesser extent 2-hydroxyoctadecanoate as substrate.
Catalytic Activity: (S)-lactate + O2 = H2O2 + pyruvate
Sequence Mass (Da): 38615
Sequence Length: 370
EC: 1.1.3.-
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O33655 | MENKSEMINATTIEFKTSSAEGSVDFVNVFDLEKMAQKVIPKGAFGYIASGAGDTFTLHENIRSFNHKLIPHGLKGVENPSTEITFIGDKLASPIILAPVAAHKLANEQGEIASAKGVKEFGTIYTTSSYSTTDLPEISQTLGDSPHWFQFYYSKDDGINRHIMDRLKAEGVKSIVLTVDATVGGNREVDKRNGFVFPVGMPIVQEYLPNGAGKTMDYVYKATKQALSPKDVEYIAQYSGLPVYVKGPQCAEDAFRALEAGASGIWVTNHGGRQLDGGPAAFDSLQEVAESVDRRVPIVFDSGVRRGQHVFKALASGADLVALGRPVIYGLAMGGSVGTRQVFEKINDELKMVMQLAGTQTIDDVKHFKLRHNPYDSSIPFSPKCFKIRLIFRRPNQILGQFF | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of (S)-lactate (L-lactate) to pyruvate, with a reduction of O2 to H2O2. Is likely involved in the L-lactate aerobic metabolism of S.iniae that enables the bacterium to utilize L-lactate as an energy source for growth under aerobic conditions in the absence (or at low concentrations) of glucose.
Catalytic Activity: (S)-lactate + O2 = H2O2 + pyruvate
Sequence Mass (Da): 44120
Sequence Length: 403
EC: 1.1.3.-
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O13629 | MLEAVTNPKSSLATFSKQLNGLLQAKVVVCKSVNPYFNLALENYLYENSTAKHCLLLYTNSPSVIIGRNQNPWVEANVKLCRDNFVNIIRRKSGGGTVFHDFGNLNYSVLMNREEFSHTENASIMIQALRNLGVHARLNQRHDIVLAQSQRKISGSAYKISRNRCYHHGTMLLNSDLEGVREYLRSPSTGILSKGVSSTRSPVSNTKLLKAEFIKQVISCFLLHKSHSTTTKPLSKPRASSKRLYDIEPKSVITLEQNDLLGVPSILKAVNELQSWEWTFGQTPSFKQHLESTELSVSMDISVVHGRLEKVIFSTPNATLEHELSSIPWTGLCYESGFANTFLISGIHSKEAISILKWISDSI | 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.
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H(+)
Sequence Mass (Da): 40652
Sequence Length: 363
Pathway: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.1.20
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Q9ZU49 | MTIGSFFSSLLFWRNSQDQEAQRGRMQEIDLSVHTIKSHGGRVASKHKHDWIILVILIAIEIGLNLISPFYRYVGKDMMTDLKYPFKDNTVPIWSVPVYAVLLPIIVFVCFYLKRTCVYDLHHSILGLLFAVLITGVITDSIKVATGRPRPNFYWRCFPDGKELYDALGGVVCHGKAAEVKEGHKSFPSGHTSWSFAGLTFLSLYLSGKIKAFNNEGHVAKLCLVIFPLLAACLVGISRVDDYWHHWQDVFAGALIGTLVAAFCYRQFYPNPYHEEGWGPYAYFKAAQERGVPVTSSQNGDALRAMSLQMDSTSLENMESGTSTAPR | Function: Plays a general role in cellular responses to stress, may be by attenuating the signal produced by phospholipases. Exhibits both diacylglycerol pyrophosphate (DGPP) phosphatase and phosphatidate (PA) phosphatase activities. Substrate preference is diacylglycerol pyrophosphate > phosphatidate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36683
Sequence Length: 327
Subcellular Location: Membrane
EC: 3.1.3.-
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Q5PH64 | MNRTKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNQATKYRK | Function: A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non-covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 8391
Sequence Length: 78
Subcellular Location: Cell outer membrane
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Q04396 | MISVMADEKHKEYFKLYYFQYMIIGLCTILFLYSEISLVPRGQNIEFSLDDPSISKRYVPNELVGPLECLILSVGLSNMVVFWTCMFDKDLLKKNRVKRLRERPDGISNDFHFMHTSILCLMLIISINAALTGALKLIIGNLRPDFVDRCIPDLQKMSDSDSLVFGLDICKQTNKWILYEGLKSTPSGHSSFIVSTMGFTYLWQRVFTTRNTRSCIWCPLLALVVMVSRVIDHRHHWYDVVSGAVLAFLVIYCCWKWTFTNLAKRDILPSPVSV | Function: Catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Together with DPP1, regulates intracellular DGPP and PA levels which are phospholipid molecules believed to play a signaling role in stress response. Can also use lysophosphatidic acid (LPA) as a substrate. Substrate preference is PA > DGPP > LPA.
Catalytic Activity: a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31586
Sequence Length: 274
Domain: The phosphatase sequence motif I (including Arg-143) and II (including His-189) are part of the cytoplasmic loop 2 and phosphatase sequence motif III (including His-235) is part of the cytoplasmic loop 3.
Subcellular Location: Golgi apparatus membrane
EC: 3.6.1.75
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P0A0V1 | MKNQVKKILGMSVVAAMVIVGCSHAPKSGISKSNKAYKEATKGAPDWVVGDLEKVAKYEKYSGVFLGRAEDLITNNDVDYSTNQATAKARANLAANLKSTLQKDLENEKTRTVDASGKRSISGTDTEKISQLVDKELIASKMLARYVGKDRVFVLVGLDKQIVDKVREELGMVKK | Function: Could play a role in the pathogenesis of H.pylori by serving as an inflammatory mediator.
Location Topology: Lipid-anchor
Sequence Mass (Da): 19108
Sequence Length: 175
Subcellular Location: Cell outer membrane
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Q9XI60 | MPEIHLGAHTIRSHGVTVARFHMHDWLILLLLIVIEIVLNVIEPFHRFVGEDMLTDLRYPLQDNTIPFWAVPLIAVVLPFAVICVYYFIRNDVYDLHHAILGLLFSVLITGVITDAIKDAVGRPRPDFFWRCFPDGIGIFHNVTKNVLCTGAKDVVKEGHKSFPSGHTSWSFAGLGFLSLYLSGKIRVFDQRGHVAKLCIVILPLLVAALVGVSRVDDYWHHWQDVFGGAIIGLTVATFCYLQFFPPPYDPDGWGPHAYFQMLADSRNDVQDSAGMNHLSVRQTELESVR | Function: May play a general 'housekeeping role' in lipid metabolism. Exhibits both diacylglycerol pyrophosphate (DGPP) phosphatase and phosphatidate (PA) phosphatase activities with no preference for either substrate. May play a role downstream of the ABA signaling pathway during seed germination and in stomatal movement in leaves.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32702
Sequence Length: 290
Subcellular Location: Membrane
EC: 3.1.3.-
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E8XH69 | MNRTNQLILGAVVLGSTLLAGCSSNAKIDQLSSDVQTLSAKVEQLSNDVNAMRSDVQAAKDDAARANQRLDNKVFRICK | Function: A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non-covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 8492
Sequence Length: 79
Subcellular Location: Cell outer membrane
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Q8Z6K1 | MNRTNKLILGAVVLGSTLLAGCSSNAKIDQLSSDVQTLSAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNKVFRICK | Function: A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non-covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 8478
Sequence Length: 79
Subcellular Location: Cell outer membrane
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Q8LFD1 | MARFSFPCFPNFGGFNQAVTNRGPEISETADNWVSPSDIPLIEPNSKEHRMREAQLGGHTLRSHGMTVARTHMHDWIILVLLVILECVLLIIHPFYRFVGKDMMTDLSYPLKSNTVPIWSVPVYAMLLPLVIFIFIYFRRRDVYDLHHAVLGLLYSVLVTAVLTDAIKNAVGRPRPDFFWRCFPDGKALYDSLGDVICHGDKSVIREGHKSFPSGHTSWSFSGLGFLSLYLSGKIQAFDGKGHVAKLCIVILPLLFAALVGISRVDDYWHHWQDVFAGGLLGLAISTICYLQFFPPPYHTEGWGPYAYFQVLEAARVQGAANGAVQQPPPQVNNGEEEDGGFMGLHLVDNPTMRREEDVETGRG | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40775
Sequence Length: 364
Subcellular Location: Plastid
EC: 3.1.3.-
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Q9HVV7 | MRFVNTLPLIFGLTAALGSSMALALPSDREQPIRVQADSAELDDKQGVAVYRGDVVVTQGSTKLTGNTVTLKQDKNGDIEVVTSVGKPAYYEQKPAPDKDVTKAYGLTIQYFVTQNRVVLIDQAKVIQEGNTFEGEKIVYDTQRQIVNAGRATGSQVTSPRPRIDMVIQPKKKAQ | Function: Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. May form a bridge between the inner membrane and the outer membrane, via interactions with LptC and LptD, thereby facilitating LPS transfer across the periplasm (By similarity). Binds LPS . Important for cell envelope stability and essential for growth, cell viability and ability to cause infection in different animal models .
Sequence Mass (Da): 19126
Sequence Length: 175
Domain: Adopts the canonical beta-jellyroll structure present in E.coli Lpt proteins.
Subcellular Location: Periplasm
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P24693 | MSELLQAQSLFKSYRRRVVVRDVSVQVATGEVVGLLGPNGAGKTTTFYMMVGLVRPDRGHIFLQQRDITALPMHERARMGLGYLPQEPSVFRQMSAADNVLAVLETLPLSPVERQERQEQLLSELHLHALRDTKGHSLSGGERRRVEIARALAMSPRFILLDEPFAGIDPISVLEIQRLIRDLRARGIGVLITDHNVRETLGICERAYILHDGKVLTAGSPQEIVDDPMVRQVYLGDQFQI | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Probably responsible for energy coupling to the transport system (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27023
Sequence Length: 241
Subcellular Location: Cytoplasm
EC: 7.5.2.-
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P0A9V3 | MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDDDISLLPLHARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGEDFRL | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Probably responsible for energy coupling to the transport system (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26801
Sequence Length: 241
Subcellular Location: Cytoplasm
EC: 7.5.2.-
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P45073 | MSILTAENLAKSYKSRKVVSDVSLTVNSNEIVGLLGPNGAGKTTTFYMVVGLVRQDQGKIVIDGEDISLLPMHNRAQRGIGYLPQEASIFRRLTVYENLMAVLEIRKDLTPQQRREKADELIEEFNISHIRDNLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVSDIKKIITDLRNRGLGVLITDHNVRETLDVCERAYIVGAGKIIATGTPEQVMNDEQVKRVYLGEQFKL | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Probably responsible for energy coupling to the transport system (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26814
Sequence Length: 241
Subcellular Location: Cytoplasm
EC: 7.5.2.-
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P11160 | IDIKRIIEHLPRQRLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPQQILEDEQVKRVYLGEDFRL | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Probably responsible for energy coupling to the transport system (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 7914
Sequence Length: 68
Subcellular Location: Cytoplasm
EC: 7.5.2.-
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P20162 | LETRKDLDRDGRRKVLESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGRLIAEGDAETILANELVKEVYLGHEFRLXPGTRLKYWQTALKLRVKLLLYSRQTLQFKAXNLLDLALRRPRVVDGACAPANKVLSPC | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Probably responsible for energy coupling to the transport system (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22274
Sequence Length: 198
Subcellular Location: Cytoplasm
EC: 7.5.2.-
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Q8ZQZ7 | MRYLVTLLLSLAVLVTAGCGWHLRSTTQVPASMKTMILDSGDPNGPLSRAVRNQLRLNNVNLLDKDTTRKDVPSLRLGTVTILQDTASVFQDGQTAEYQMVMTVNASVLIPGHDIYPISTKVYRSFFDNPQMALAKDNEQAMIVQEMYDKAAEQLIRKLTSVRAADIQATKEEATADNETAAPASTPARVSTTLSN | Function: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 21458
Sequence Length: 196
Subcellular Location: Cell outer membrane
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Q2NUU8 | MRYWTLALVLGLAVTITAGCGYHLRGTTDQVPTEMKTMTLNSYDPYGPLTRAVRAELRLNDVTLVDDAQDKNNTLPSLRIVNSSENQVTASVFQDGKTAEYQMTLGVHAQVLMPGEDYYPIDVKVYRSFFDNPLTALAKDAEGDIIRQEMRQQAAQQLVRKLLTVHAAEEADKALDAKLKQQQPPQPVAPAS | Function: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 21292
Sequence Length: 192
Subcellular Location: Cell outer membrane
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A7FKW1 | MRHRILTLLLGLAVLVTAGCGFNLRGTTQVPTELQKLLLESSDPYGPLARSIRQQLRLNNVTIVDDAMRKDIPTLRIIGSSESQETVSIFRNGVAAENQLVLHVQAQVLIPGHDIYPLQVNVFRTFFDNPLTALAKEAEAEVLRQEMREQAAQQLVRQLLTVHAAEVKNTQKNGDKPVSDANAAQGSTPTAVNETTLGEPAVSTSAK | Function: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22570
Sequence Length: 207
Subcellular Location: Cell outer membrane
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Q8RFU2 | MVDIHSTAIIEDGAIIEDGVKIGPYCIVGKDVVIKKGTVLQSHVVVEGITEIGENNTIYSFVSIGKDNQDLKYKGEPTKTIIGNNNSIREFVTIHRGTDDRWETRIGNGNLIMAYVHVAHDVIIGDDCIFSNNVTLAGHVVIDSHAIIGGLTPIHQFTRIGSYSMIGGASAVSQDVCPFVLAAGNTVVLRGLNIVGLRRRGFSDEEISNLKKAYRILFRQGLQLKDALEELEKDFSEDKNVKYLVDFIKSSDRGIAR | Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo-[ACP]
Sequence Mass (Da): 28198
Sequence Length: 257
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6.
Subcellular Location: Cytoplasm
EC: 2.3.1.129
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Q62JD7 | MAFQLTPLRVALVAGEPSGDLLGASLLGGLHARLPASSRYYGIGGPRMSAVEFDAHWPMEKLAVRGYVEALKHIPEILRIRGELKRQLLAEPPDAFVGIDAPDFNFGLEQALRGAGIPTIHFVCPSIWAWRGGRIKKIVKAVDHMLCLFPFEPELLEKAGVAATFVGHPLADEIPLEPDTHGARIALGLPGGGPVIAVLPGSRRSEIELIGPTFFDAMELMQQREPGVRFVVPAATPALRALLQPLVDAHPSLSVTLTEGRAQVAMTAADAILVKSGTVTLEAALLKKPMVISYKVPWLTGQIMRRQGYLPYVGLPNILAGRFVVPELLQHFATPDALADATLTQLRDDANRRALADIFTDMHLALRQNTAQRAAEAVAHVIDSRKPR | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Mass (Da): 42012
Sequence Length: 388
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.4.1.182
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Q9PIK8 | MKTFLVCALEPSANLHLKEVLKAYKKDFGEFELHGIYDESLCKEFDLNSKPLYSSHEFSAMGFIEVLPLIFKAKKAIKELANLSFTQKINGILCIDSPAFNIPFAKALKKAGSKIPRIYYILPQVWAWKKGRIPIIESHFDILASILPFDNQFFNKSTYIGHPLLDEIKEFKNQEDINHTFSKKDDEKTIAFLPGSRRSEIRRLMPIFKELSQKFKGKKILCVPSFNLEKLEVYGDISEFKIESNTPKVLKKADFAFICSGTATLEAALVGTPFVLAYKAKAIDIFIAKLFVKLKHIGLANIFCDFAGKEALNPEFLQDKVNVLNLYEAYNKYDYKAFFAKVDFLKEYLQFGSAKNLAKILNEI | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Mass (Da): 41581
Sequence Length: 364
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.4.1.182
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B8E7Q3 | MSNKTPLVFAMVAGELSGDILGAGLMAALQKNHPDARFVGIGGPRMEALGFRSLFAMEELAVMGIVEVLSRLPRLLTVRASLIKEITALKPDCFIGIDAPDFNIGLELKLKARGIKTVHYVSPSVWAWRPKRIFKIAKATHMVLSLLPFEKAFYDQHQVPCTFVGHTLADDIPFQSDKAAARALLGLDADAEYLAILPGSRGGELKQLAEPFVKAALLIRQNFPDIRFVTPLVNQKRRDQFEQALKDFAPDLEIHMIEGQSREVMAAADGILLASGTATLEAMLVKRPMVVAYRVSPITYRIAKRMMQVERFSLPNLLAGKDLVPELIQEDCTPEKIAAAVTLELNRDFAPLKAEFEALHQVLRRDASLKAAEAVMALVEPKHTQAKSPEAN | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Mass (Da): 43181
Sequence Length: 392
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.4.1.182
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Q8EGG2 | MSKKSQLVFAMVAGELSGDILGAGLMAALQKTHPNARFVGIGGPRMEALGFESLFAMEELAVMGIVEVLSRLPRLLHVRASLIKSITELKPDCFIGIDAPDFNIGLELKLKAQGIKTVHYVSPSVWAWRPKRIFKIAKATNMVLSLLPFEKAFYDKHQVPCTFVGHTLADDIPLESDKACARQVLELDQEAEYLAILPGSRGGELKQLAEPFVKAALLIKQQFPDIRFVTPLVNQKRREQFEQALKDHAPDLEIHMVEGKSREVMAAADGILLASGTATLEAMLIKRPMVVAYRVSPLTYSIAKRMMQVNRFSLPNLLAGCDVVPELIQHDCTPEKIAAAVGVELNRDFAPIKAEFERLHQVLRCDASQKAAEAVLALVDFKEVN | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Mass (Da): 42517
Sequence Length: 385
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.4.1.182
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Q72RV5 | MKEILYRRSIQDTVRIKGIGLHSGKEVNLTAHPAPSGTGIVFEYRKGLEKASISAELSNVVDTSNATTLGDGIHKIQTVEHLLAAVYALGLTDLILEIDAVEVPIMDGSSLPFLQALESAGIIEYPEIVEPIYIQSPLWVVDGDKYLVLLPSDELKVTYTIDFNHPLLKGQSITVSLDREKIKQEILPARTFGFLKDVEALQARGLAMGGSLDNAIVLTQDGYLNQQLRFENECVRHKILDLFGDISIAGRPIIGHYLASKAGHALDISMAKLVMSNVTGDEISKYKSRRIPLFKRKAVVV | Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Catalytic Activity: a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
Sequence Mass (Da): 33088
Sequence Length: 301
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 2/6.
EC: 3.5.1.108
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Q2W0G6 | MRQRTLKSAIGCTGVGLHSGAKVTMVLHPAEAGTGIRFRRVDIAGGGAIVPALWSSVGDTRMNTCLKNEAGVVVGTVEHLMSALAGMQIDNCLIEINGPEVPVMDGSAAPFLFLIECAGVVEQEAPRQAIKILKRVAIKDGERTASLTPSSGFSVRFEIDFGASAISRQEFFVNLTRGTFKAEVSRARTFGFEQEVAMLRAHGLARGGSLDNAVVIDSTGTKVLNDDGLRYQDEFVRHKVLDAVGDLYLAGAPLLGHYHGVRAGHAVTNQLLRALFADATAWELTTIAPGSAAAPFAAQPLAIAANG | Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Catalytic Activity: a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
Sequence Mass (Da): 32379
Sequence Length: 307
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 2/6.
EC: 3.5.1.108
|
Q1GZ08 | MLKQRTLKKEISATGVGLHSGDKVTLTLRPAAPDTGIVFRRIDLPDTAEFKVQPHLVTDTKLCSALECNGARVATIEHLMSALAGLGIDNIRIELNAGEVPIMDGSAGPFVFLLQQAGIVEQDAMKKFIRIKKTVEYREGDKWVRFDPYFGFKLDFTIDFNHPAVEHTGQRITIDFADNSYIKEISRARTFGFMHEVEALRSMGLARGGSLDNAIVLDEFRVLNSDGLRYDDEFVKHKMLDAIGDLYVLGHPLIGAFSAYKAGHYMNNQLLRALLADGDAWEYATFAKIEEAPGAFRNPIGLPPALQYV | Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Catalytic Activity: a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
Sequence Mass (Da): 34331
Sequence Length: 309
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 2/6.
EC: 3.5.1.108
|
F4JGP6 | MANSLRTLFSVSTHGVFLNKRSSYRVRKVFVGMPLRICSEIPRFVSVSCIRSDMCGIMMLGKDVHDLLETSSGGNVEKGFLRWRNGGGMYHRSALIDSSALVEFGAVVHQEAILGAEVHIGSNTVIGSSVKIGPSTKIGNCSIGDLCVIHNGVCIGQDGFGFYVDDNGNMVKKPQTLNVKIGNRVEIGANTCIDRGSWRDTVIGDDTKIDNLVQIGHNVIIGKCCLFCGQVGIAGSAEIGDFVALGGRVAVRDHVSIVSKVRLAANSCVTKNITEPGDYGGFPAYKKTEPDSAFASDKHCFILQKILIQVPIHQWRRQIVEAQISSKRKP | Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. Lipid A-like molecules in plants may serve as structural components of the outer membranes of mitochondria and/or chloroplasts, or may be involved in signal transduction or plant defense responses.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 35708
Sequence Length: 330
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 3/6.
Subcellular Location: Mitochondrion
EC: 2.3.1.191
|
Q14JF8 | MQYTLKQISEHLNAKVINEPSGEVIITGLTYAEQAKENDLTLIDKQEHIKLWQNSKATAAIVSKKISKELAQVNDKPLIVVNNADLAMAKILELFSVPYPEQNGIHEKAIIDPTAKIGKNVSIGPSAYIGKNVEIGDNTIIYANVCIYNDAKVGTNCIIWPSVIIRDRTIIGHFCRLCSNCSIGSDGFGYRPSEDGRTIVRIPHIGNVVIGSFVDIGSNTCINNAKYGSTIIGDYTKIDNLVQIGHNVIIGKGCMICGQAGISGSVTIGDGVIIAGNAGIKDHTNIGSDARIGGKAGVMWDVPAGESHMGYPAYKDSELAKQWIAIRKLPETMKKLKAIAKSLNIDL | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 37384
Sequence Length: 347
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q7NJG8 | MGVQFSAAELTDLVGGELSGDPGRLVVGARPPEEAEGGDLTFALDLHARKLIETTRAGVAITPVRWPFEHLTQIVVANPRLAMAQVLAHMFPQPIAMPPAGIHPSAVVHPSAVVHPSASVAALVYVGPRAAVGANTHLFPGVYVGAEAVVGSECLIYPNVVLMDGIRLGDRVVIHAGSVLGSDGYGFVPTGERHLKVPQVGTVVIGDDVEVGANVAVDRATMGQTEIQAGTKIDNLVHIGHNDRIGRHCLIVSQVGLAGSVKVGDRTVIAGQAGVANQTTVGADCLVLARSGVTKDLPDHSKVSGFPAQDHLLELKQQAARSRLPQIVEQMRQMQRRIEQLEVQLLGRL | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 36734
Sequence Length: 349
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q5X0C0 | MNSSLRDIANLVQGMVIGNDAITVSTLSPIDNILPGSLVFAEGEDNIKLAENSEAAAILIGQGTIDSPKPLIQVKNPFKAFIALLNHFYPPRRISPGVHPTAVIGAEVQLGDEVYVGPFVVIESGSIIGNHSVLKSHIHIGHNVVIGDHTTIHPQVTIYDNCRIGSNVTIHASTVIGSDGFGYTFVDGQHLKVPHSGYVVIENNVEIGANTAIDKATLGATVVGEGTKIDNLVQIAHSVKLGKHNIICAFTGIAGSTTTGNNVIFAANVGVSDHVHIEDEVILGARTGVPPHKHLKKGTVYLGNPAKPKDVAIKHELSVNRIPLIRKNIKSLTEQVAVINKKLDIKAKEVE | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 37285
Sequence Length: 351
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q30RG5 | MNLKDIAKIINSDFSGEYFEITKMNTLRDATKSEISFVANAKYIKEIQNSNAGAIIVSKDTKEFVPSGCVALVVENPYWEMATLSKYFAPSIEDETLPEPKIGEGTTISPRAEIARGAIIGKGCTIMAHVYIGTNAVIGDNTIIYPSVTVYRDCRVGSECIIHANTTIGSDGFGFATNKQGEHRKIYQNGNVEIEDNVEIGSSTTIDRAVFGTTLIKYGVRIDNLVQVGHNCVIGEHSVLVAQAGISGSTTMGRNVVMGGQSATAGHLSIAPFTTMAARSGVTKSIDKSGLTFAGFPLLEHRLWLKLQAKIARLIKQN | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 34282
Sequence Length: 318
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
F4JIP6 | MAATLWRLYSKSICNSLQGIILNKPFIQKQLLLSSRTRSLSFSSDSQFGSATAEVCSNTGLKTGGGIIVKEGFLRWENGGGTCHSSAQIYSSALVEFGAVVHEKAVLGAEVHVGSGTVIGPSVDIGPSTRIGYNVSISNCSIGDSCVIHNGVCIGQDGFGFYVDEHGNMVKKPQTLNVKIGNRVEIGANTCIDRGSWRETVIEDDTKIDNLVQIGHNVIIGKCCLLCGQVGIAGSVTIGDYVALGGRAAVRDHVSIVSKVRLAANSCVTRNITEPGDFGGFPAVPIHEWRKQIVRAQIANKREI | Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. Lipid A-like molecules in plants may serve as structural components of the outer membranes of mitochondria and/or chloroplasts, or may be involved in signal transduction or plant defense responses.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 32331
Sequence Length: 304
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 3/6.
Subcellular Location: Mitochondrion
EC: 2.3.1.-
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Q14G52 | MYSLDFLASKLDGEVKGDKNVEIKKIATLSQAGEGDISFCTNPKYLKALSETKASAVLITEEVLEFCNTNAVVLSNPYMALAKVMELFDKSPRPDGKIHSKAVIAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDTLIKSNVSIAHDVVIGTGCIIHQNAVIGCDGFGNARDEDGSWTKIPQLGRVIIEDDVEIGSGTTVDRGAIDDTIIKKGARIDNLVQIAHNVVIGRNTALAGVTAVAGSTTIGDNCLIGGQSAITGHISICDNTIIGGASNIGKSITKPGMYYAAFEAKPRIQWGRFVAKLAKIDTLITKVKQLEEKIK | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 35443
Sequence Length: 337
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q7NJ21 | MKLSDISAKLGCALEGDGQVDIVGIAGIEEAEAGHLTFLSNPKYKAKLRHTKASAAIVPADFEASAAWPLPLLRHANPYLTFAHAIELFYSPPPAPHGVHPTAVVAPTAVCGHNVRIGASSVIGEGVVLADGVTVYPNCTIYPGVRIGRNSTIHSNCVVREHVVIGEDCIVQNGAVIGADGFGYAKQADGTWYKIVQSGSVVLENRVEIGACTTVDRATIGETRIKSGSKLDNLVMIGHGSSVGENTLLCGQVGLAGSSTVGRNVMLAGQVGVAGHLHIGDNVVATVKSCIWKSVEANQVLYGNIPASDSHTWLKASAVFRQLPHMQKSVQQMQKRIAVLEEPFKTNGKSGQADAPPKVALECHGTTGDAPQG | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 39027
Sequence Length: 373
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q1H149 | MNKSYSLREIVSTLGGELLGKDDVLISRVASLANAQPGQISFLTDSKYRSVLATTNASAVILTPQNRDITALPRILTDNPYAYFAKVSDLLNPKPEYVAGVDDTAVIAPSAQVPASCTIMAKAVVGANVVLGEHVVVHPGCVIGEGVEIGAHSVLHANVTIYHHCMIGERCNIFSGSVIGGDGFGYAPEEGRWVKIPQVGRVVIEHDVDIGANTTIDRGAIDDTIIHEGCKIDNLVQIGHNCRIGAHSVIAGCVGIAGSAVLGKHCRIGGAAMILGHLEIADGVTVSPGSMITRSLMKAGTYTALMPFQSHDEWLRTAAGIRRLGELAERVKQLEKQLAPQQVSGIQRDK | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 37051
Sequence Length: 350
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
B3E0P9 | MISYSVKQLASLVGGIVEGEPEIEITGISDILDAKKGQITFLSNPRYEAAVEKTQASAIVVSKSYKSSSPITLIRVDSPSLAFSQIISLFSPQPFSYEPGIHPTALIGREVEIGKEVSIQPYAVIEDKVKIGDGCVIGAYVFIGRESIIGEKSFFYPHVTIRERSRIGKRVILHPGAVIGSDGFGYEQTNGRHEKIPQVGIVQIDDDVEIGANTTVDRGRFGKTWIQEGCKIDNLVQIAHNVIIGKNSIIAAQTGISGSTSLGEHVTLAGQVGIAGHIHIGDGATITAQSGVTKDVPPRAVLSGRHARPINLTHKLEVLYNKLPELWERLKKLEKKYDGDSPRPEADPYNS | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 37997
Sequence Length: 351
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
B8INJ6 | MSDPVFFSSVGPILLAEVAALAGAALPEGLDRELAIRGAAPLESAGPDDLAYMDNAKYAEALGLTRARACLVSPRFAARVPEGTIALVTPQPYRGFAKVLARLFPSAARPTSLFGATGVSPGSFVHPAARLEPGVVVDPGVVIGPGAEIGAETVLAAGAVIGPGTRIGRGCAVGPGASVLHALIGNRVIIHGGARIGQDGFGFAMGAGGHLKVPQVGRVIIQDDVEIGANTTIDRGASRDTIIGEGTKIDNLVQIAHNVVIGRHCVIVAQVGISGSTTLEDYVVLGGQVGVVGHLRIGMGAQIAGSSNINKDVPPGARWGGTPAKPVREWFREMTTLKRIAARERLAEDTAE | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 36034
Sequence Length: 352
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q1D385 | MPRQLGELAAHVGGELLGDPSQLIHGLNGLEEAGPGDVSFYGNPRYRRQFEATRASAVLVGADVPPREGVALVRVANPHLAYAKLLRLFHAPERPAAGVRPGAWVHPEATVHPEAVLLPGASVDRGGRVGARTVLYPGAYVGEQAEVGEDCVLYPNVTVRERCIVGARVILHASSVVGADGFGFAFNPEGEAGPEHFKIPQVGIVRIEDDVEVGACTCIDRATVGETVVGRGAKLDNLVQIAHNVRVGPLSLICAQAGVSGSAEVGTGVVLAGQVGVVGHIRVGDLAKVGAQSGVAHDVPDGQVVSGSPAVPHREWLRASAAAGQMADLLKEVRALRRRVETLEKEKGP | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 36382
Sequence Length: 349
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
P95377 | MIPATYTLSQITARLGGEWRGEDISVTAVRPLADAQAEHISFLANPKYKAEVHDSSAGAVIVSAKAADGFEGRNLIVADDPYLYFAKVARLFSPVVKARGGIHPTAVVEPGATVPTSCEIGANVYIGANTVLGEGCRILANAVVQHDCKLGDEVVLHPNAVVYYGCTLGRRVEIHSGAVIGADGFGLAFADDSWFKIPQTGAVTLGDDVEIGSNTNIDRGAMSDTTVGNGTKIDNQVQIGHNCKIGSHTVIAAKTGISGSVTIGSYCIIGGGVGTVGHIEIADKTTIGGGTSVTHSITESGKHLAGIFPMSTHKEWARNAVYIHRLSEMNKRLKTLEQQLSDAGQDSK | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 36449
Sequence Length: 348
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
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Q3JEI7 | MEIRLSEIAQFLGCAIEGDGEAPIRGIAPLHQAQASELSFYTNRKYAAQARLSKAGAIIVGAKDREQFAGRRLLISDNPYRDFARVVDRWFNRSYRPAPGVHPTAIVGDDVQIAENCSIGAYCVIEDGVTIKAHTVLFPFCYVGAKTILGEHCLLYPRVTLLERVRIGHRVILHPGVVIGGDGFGFAPDPPQGYFKVPQVGWVEIADDVEVQCNTAIDRGALGPTRIGQGSKIDNLVQVGHNVEIGEHSIIVSQVGISGSSKIGNWVTLAGQVGLVGHIRIGDGAVITAQSGVAKDVPPKAIMTGSPVQPMMENRRALAELNRLRELRKKVRELERRLTVLEQVESC | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 37696
Sequence Length: 347
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
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Q312H3 | MKVSDIAGALGLKLKGPDREISGVNTLEAAGPEEISFLANPKYIPMLAGTRAAAVIVSEEYAGQVETALISANPYFDFGRTLHLFARPQGSFSGISDMAYIHPEAEIGGGCTIYPHVYIGARARIGEGTTLFPGCYVGEDCAVGENCLLYPNVTLMAATTVGDDCVLHSGVVLGADGFGFARTEYGIQKIPQIGRVHVGNDVEIGANTAIDRAVLGVTTIGDGTKMDNLVQVGHNVTIGNDCLIVAQVGISGSTHVGDRVTMAGQVGVAGHLTIGDDVTVGPKSGIARSIEPGKTMGGQPAVERDVYMRTLTVMPKLPDMYKRLRKLEKELEALKGESGRDS | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 35906
Sequence Length: 342
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
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C5B8V8 | MATLFIADLHLSQQEPAITAGFLRFLAEEAPKAEALYILGDFFDYWIGDDDPQPLHRQVAGALRQLSDNGVPCYFICGNRDFLLGKSYAKRCGMTLLPDEQIITLYGQPILLLHGDTLCSDDRDYQRYRRRVHNPLLQWLFRRLPLRLRLKIAVGMRQQSQRSNSAKAMTIMDVNQETVCATLRRHGVQRMIHGHTHRPALHHFSLDDGRCALRAVLGAWHTHGSMIRVDAQGIHLIELPAHPAEDEIITTRLRSANLV | Cofactor: Binds 2 Mn(2+) ions per subunit in a binuclear metal center.
Function: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: H2O + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine = 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + 2 H(+) + UMP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29503
Sequence Length: 259
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 4/6.
Subcellular Location: Cell inner membrane
EC: 3.6.1.54
|
P44046 | MKHSYFISDLHLSETQPELTALFVDFMQNLAPQAERLYILGDLFDFWIGDDEQSALIQQVKDLIKFVSDQGVQCYFQHGNRDFLIGERFSKETGAQLLPDYQLITLYDKKILLCHGDTLCIDDEAYQQFRRRVHQKWLQRLFLCLPLKVRVIIAEKIRAKSNQDKQAKSQEIMDVNQAFTAEKVQEFGVNLLIHGHTHREAIHQQEEFTRIVLGDWRKNYASILKMDESGEFGFIKD | Cofactor: Binds 2 Mn(2+) ions per subunit in a binuclear metal center . May bind a third metal with significantly weaker affinity that might facilitate the catalysis but only binds LpxH in the presence of the substrate .
Function: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: H2O + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine = 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + 2 H(+) + UMP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27786
Sequence Length: 237
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 4/6.
Subcellular Location: Cell inner membrane
EC: 3.6.1.54
|
Q2SK43 | MPTLFISDLHLEIEKPDLTRFFFNFLDKVAPNAEALYILGDFFEVWVGDDEQSPLQVEVAQRLHKLAEAGTHIHLMHGNRDFLIGETYAKQCGATLLAEPHALDLYGVPSLLMHGDSLCTLDAAYQKARATFRNPAFQSQFLSRPLDQRQLTARQMRQISMAKNQGKAEVIMDVAPDEVINTFNTYGIELLIHGHTHRPDTHRYNLPQGEVKRIVLGDWGEETWYGRADADGFQLLNLKAEDIA | Cofactor: Binds 2 Mn(2+) ions per subunit in a binuclear metal center.
Function: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: H2O + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine = 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + 2 H(+) + UMP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27659
Sequence Length: 244
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 4/6.
Subcellular Location: Cell inner membrane
EC: 3.6.1.54
|
P27300 | MIEKIWSGESPLWRLLLPLSWLYGLVSGAIRLCYKLKLKRAWRAPVPVVVVGNLTAGGNGKTPVVVWLVEQLQQRGIRVGVVSRGYGGKAESYPLLLSADTTTAQAGDEPVLIYQRTDAPVAVSPVRSDAVKAILAQHPDVQIIVTDDGLQHYRLARDVEIVVIDGVRRFGNGWWLPAGPMRERAGRLKSVDAVIVNGGVPRSGEIPMHLLPGQAVNLRTGTRCDVAQLEHVVAMAGIGHPPRFFATLKMCGVQPEKCVPLADHQSLNHADVSALVSAGQTLVMTEKDAVKCRAFAEENWWYLPVDAQLSGDEPAKLLTQLTLLASGN | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: ATP + lipid A disaccharide (E. coli) = ADP + H(+) + lipid IVA (E. coli)
Sequence Mass (Da): 35589
Sequence Length: 328
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
|
C5BAE1 | MIARIWSGRSPLYLLLLPLSWLYGLVALLRRQAYRRGWIRVWRAPLPLVVVGNLTAGGNGKTPLVIWLVEQLQRRGYRVGVVSRGYGGRATCYPLVLGPDTRSVECGDEPLLIAQRTGARVAVAPQRSAAVQALLAQEPLDVVITDDGLQHYALARDMELVVIDGERRFGNGWWLPAGPMRERAARLCSVDAVIVNGGLPRTGEIPMALTGHTLVNLRSGERRVAGQFVTPVVAMAGIGHPPRFFHTLTQLGIPLQATHAFADHQAYQAQVLAALTPQAQPLLMTEKDAVKCRAFAQDNWWYLPVSATLPAEAGDRLLARIAALVAAQPRG | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 36113
Sequence Length: 331
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
|
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