ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P61196 | MNIHRKPEWLRKKINPAAHGAMDELLGELRLHTVCREARCPNITECFRERQATFLILGAECTRLCSFCNVTKGEPLPPDPDEPARVAQAVVRLSLAHVVITSPTRDDLPDGGAGHYVATVATIGRVAPATVVELLIPDFLGSRAALADVVAAAPRIIGHNVETVPRLYAIRAGADYGRSLAVLRTLRELAPGCATKSGLMLGLGETEEEVLAVMADLRRVDCTYLSLGQYLAPSRFHHPVREFVLPETFDRLKELAEKMGFRHVESGPYVRSSYHAAGYGGGTRTDQPVASGCLSDQEGVSAQ | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
Q62N15 | MPVTVRWLGETPYDACFDAMRAFTDARTPDTDDEIWVVEHPPVYTLGQAGNPAHLLVADSGVPLVKVDRGGQITYHGPGQIVAYLLVDLRRRKLMVRTLVTRIEEAVIETLAAYNLASARKAGAPGIYVESGPHRGAKIAALGLKIRNGCSYHGLSVNVKMDLRPFLAINPCGYAGLETIDMASLGATADWHEVAQTLVRRLIAHLDGATAAAALPQQALEQSND | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
A4JI72 | MSVSPVAIVSTPVAVSASPAGSPAQHDAPLTVRWRGTEAYQTSFDAMRAFTDARTAETPDEIWIVEHPPVYTLGQAGDPAHLLVADSGVPLVKVDRGGQITYHGPGQIVAYLLLDLRRRKLMVRTLVTRIEEAVIETLAAYNLASVRKAGAPGIYVASGVHGGAKIAALGLKIRNGCSYHGLSLNVKMDLRPFLAINPCGYAGLETVDMASLEVAADWNDVARTLVGRLIANLDGASAAADKPHALEHSND | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q8R9E0 | MRRGEVLKLGVVPYLEGKEIQLKAFEKVKKEETDGILILLQHKPVYTIGVSGGYDEDILVPIDYIKEKAELYKVERGGKITFHGPGQVVAYPIFNLAKWQKDVHLFVHNLEEAVIRLLREYGIIAGRKEKYTGVWVGDEKICAIGIAVKRWITWHGIALNVNTDLSYFGLINACGITEFGVTSMKKLGIEVEIEEVMDRLVDKFEEVFEIKFEEIDLTRLAVVDSAKA | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q82UJ6 | MFTVTVKNMGTTEYLTAWQAMKNFTAQRTCETPDEIWLLEHPPVYTQGIAGKPEHLLFPNQIPVIKTDRGGQITYHGPGQIILYLLLDLHRWRLNIRQLVRKMEGAVIDLLSEYDVVAQGDENAPGVYVDGAKIASLGLKIRRGACYHGIAFNADMDLTPFTAINPCGYRGLRVTQAKDLGIADCKEMLATKLAQSFINQLTDV | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q2Y7I8 | MIQPVSLEFVPGPSGLEVKYAAVMDYLSIWQAMKAFTASRTQNTPDEIWLLQHWPVYTQGVAGKPEHLLCNPGIPVVRTDRGGQITYHGPGQIIAYLLLDMRRLKLGVRDLVRKMEGAVVDLLDEYRVNACGDEDAPGVYVGGAKIAALGLKIKNGCCYHGLALNVSMDLAPFMAINPCGYTGLRVTQTSDLGITDELETLQGKLAEKLKARLKQ | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q3J7W3 | MDKRIPVGADTLRIRNLGLQDYDTVWQAMRDFTVRRDSATVDELWWVEHPPVFTLGLNGQECHLRDVGDIPVVRCDRGGQVTYHGPGQSIVYILVDLRRRALGVRQLVDALELSVVDLLQSYEIETERRANAPGVYVQGRKIASLGLRVRKGCCYHGLSLNVAMDLSPFYRIDPCGYSGMEVIDLKRLGMELPLADVQQNLSRYLVRRLGYSAPFYGEENRMIK | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q5YZ58 | MNDTRTSRSARFDTTPVVVEDLGLIDYHAAWELQRTIAAERAEGAGSDRLLLLEHPSVYTAGRRTEDADLPIDGSPVVQVDRGGKITWHGPGQLVGYPIVRLAEPVDVVDYVRRLEEALISVCTELGLTVGRVEGRSGVWLPATETLAERKIAAIGIRVQRGVALHGISFNCNSALDGFQAIVPCGIQDAGVTTLTRELGREVTVAEVKPMVATAVVQALNGDLPVRDHDLPRPGTTPAAPNSTRVRSMT | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
B3CRE6 | MVEWIEIQYPIEYGEAYKMMKSRLTGILNGTASEAVFILEHQDVYTAGISAKNDELLNCYDIPVHHTDRGGKFTYHGPGQIIIYPVINLAVNGRVKDIRNYVNNLASLVINSLKFFNITGITVQDTIGVWIDSEFGRKKIASIGVRIHKWITYHGVAINVCPDLKKFKGIIPCGDRDTIVTSISELLDQKIDLDYYKAILKQEFYKIF | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
A1R5J6 | MTLEFSQLGLAPDFVDYMQGWDLQRDIHNKVVAGEKNSTVLILEHAAVYTAGKLTEDHERPFDGTPVVPVDRGGKLTWHGPGQLIAYPILKLKNRAGIRDYVERLEAIMIAVMQDYGIKAVTVKGRAGVWILADDKGPDRKIAAIGIRVLDGVTMHGVAINCSNDLAPYAQIIACGITDASVTTMSLETGRTINPADIVDRFVEEFSKHDEALVSTPEGALQ | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
A6L9E1 | MESFRYHDLGRIAYADALEYQTAAFEVLLDAKATGKKEDNQLFFCEHLPVLTIGKSGKDSNLLIPEETLRERGVSFYHINRGGDITYHGPGQITGYPVFDLEYWNLGLKQYIHMLEETIIRFLSLYDLKGERLEGATGVWLDPEVPGRARKICAIGVKSSRFVTMHGFALNINTDLSYFSLINPCGFTDKGVTSLAMELGVPQDFELAKSQLRSIFMEIFA | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
A1B3D5 | MTEWITAPGLTDYQEALAFMEARAAAIAAGEAGELVWLVEHPPLYTAGTSAKAADLLEARFPVHAVGRGGQYTYHGPGQRVVYVMLDLNRRGRDVRAFVKALENWVIDALAEFNLRGEIRDGRVGVWIARPDKAPLPDGSMREDKIAAIGVKLRRWVSFHGIAINVEPDLNHYAGIVPCGISGHGVTSLVDMGLPVGMDDLDLALRRSFARNFPPLAG | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
P42969 | MVLRYTALGDSLTTGRGSGLFSPGFVQRFGDMMEADLKTRTAINIFARSGLNTEEILGLLSYPYVQKCIRDADMITITGCGNDLIDSVLAYQTSKDETIFSRVSAHCHENFEKMIAKVAEIKGENPSPYAIRVFNLYNPFPEIDIAGKWITSFNSHLETLASAPHVKIADAYSIFKGKEQEYLSFDGVHPNSKGYQAMAEAVHKLGYKELSVS | Function: Lipase involved in spore germination.
Sequence Mass (Da): 23606
Sequence Length: 213
Subcellular Location: Spore coat
EC: 3.-.-.-
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P11150 | MDTSPLCFSILLVLCIFIQSSALGQSLKPEPFGRRAQAVETNKTLHEMKTRFLLFGETNQGCQIRINHPDTLQECGFNSSLPLVMIIHGWSVDGVLENWIWQMVAALKSQPAQPVNVGLVDWITLAHDHYTIAVRNTRLVGKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSSIGGTHKIGRITGLDAAGPLFEGSAPSNRLSPDDANFVDAIHTFTREHMGLSVGIKQPIGHYDFYPNGGSFQPGCHFLELYRHIAQHGFNAITQTIKCSHERSVHLFIDSLLHAGTQSMAYPCGDMNSFSQGLCLSCKKGR... | Function: Catalyzes the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins, including chylomicrons, intermediate density lipoproteins (IDL), low density lipoproteins (LDL) of large size and high density lipoproteins (HDL), releasing free fatty acids (FFA) and smaller lipoprotein pa... |
P96402 | MNQRRAAGSTGVAYIRWLLRARPADYMLALSVAGGSLPVVGKHLKPLGGVTAIGVWGARHASDFLSATAKDLLTPGINEVRRRDRASTQEVSVAALRGIVSPDDLAVEWPAPERTPPVCGALRHRRYVHRRRVLYGDDPAQLLDVWRRKDMPTKPAPVLIFVPGGAWVHGSRAIQGYAVLSRLAAQGWVCLSIDYRVAPHHRWPRHILDVKTAIAWARANVDKFGGDRNFIAVAGCSAGGHLSALAGLTANDPQYQAELPEGSDTSVDAVVGIYGRYDWEDRSTPERARFVDFLERVVVQRTIDRHPEVFRDASPIQRVT... | Function: Esterase that can hydrolyze short-chain esters with the carbon chain containing 2 to 10 carbon atoms. Does not have lipase activity. Is highly immunogenic and elicits strong humoral immune responses in both HIV-negative (HIV-) and HIV-positive (HIV+) tuberculosis (TB) patients. Also elicits pro-inflammatory c... |
P07867 | MGNHLQISVSLVLCIFIQSSACGQGVGTEPFGRNLGATEERKPLQKPEIRFLLFKDESDRLGCQLRPQHPETLQECGFNSSHPLVMIIHGWSVDGLLETWIWKIVGALKSRQSQPVNVGLVDWISLAYQHYAIAVRNTRVVGQEVAALLLWLEESMKFSRSKVHLIGYSLGAHVSGFAGSSMGGKRKIGRITGLDPAGPMFEGTSPNERLSPDDANFVDAIHTFTREHMGLSVGIKQPIAHYDFYPNGGSFQPGCHFLELYKHIAEHGLNAITQTINCAHERSVHLFIDSLQHSNLQNTGFQCSNMDSFSQGLCLNCKKG... | Function: Catalyzes the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins, including chylomicrons, intermediate density lipoproteins (IDL), low density lipoproteins (LDL) of large size and high density lipoproteins (HDL), releasing free fatty acids (FFA) and smaller lipoprotein pa... |
P40600 | MKKKLIYAAVVSALLAGCGGSDDNKGDTSSYLDYLLTGSNAVGPSALAARAWDGTLKFSTETADLSNPVSAMSTLDGWSTTQAIQIVPVTSSGITVQAPTTAEFGASVAPLYLLEVTFDSTALRPSGVKKVLTYGVDFVVAASAWQAEPGSAQAVEPLPCLANDSGHRTAERQSRRCLKAGSDYGNYKNNAGSNAQEQTINGLIALQEGLFKAATGIATDHVIFSDWFGTQSGADVLVAVKGAAASVLKADPVTLDAAKLWKQDAWEHQPARHLYPGRDRPTCLPDPAGCRAVPAAEQKDAIATAFGPVLRSTRLLKRPR... | Function: The optimum chain lengths for the acyl moiety is C6 for ester hydrolysis and C6 and C8 for triacylglycerol hydrolysis.
Catalytic Activity: a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+)
Sequence Mass (Da): 71904
Sequence Length: 684
Subcellular Location: Secreted
EC: 3.1.1.3
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Q8I0F4 | MVLTSKQKEELNGSILDYFESSQYKSSFEEFKKETGTELDVKKKGLLEKKWTSVIRLQKKVLDLEAKVAQLEEELNSGGGRGGGRGRGKEDALPRPPEKHILTGHRNCINSVKFHPSFSLMVSASEDATIKVWDFESGEFERTLKGHTNAVQDIDFDKTGNLLASCSADLTIKLWDFQTYDCVKTLHGHDHNVSCVRFTPSGDQLISSSRDKTIKVWEAATGYCIKTLVGHEDWVRKITVSEDGSCIASCSNDQTIKTWNIVKGECLATYREHSHVVECLAFSTANIIDIPGSLLSTPEGKSKVKQGPGGNLVGQCGYLA... | Function: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the coupli... |
Q7KNS3 | MKMVLSQRQREELNQAIADYLGSNGYADSLETFRKEADLSTEVEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKFSLTGHRASITRVIFHPIFALMVSASEDATIRIWDFETGEYERSLKGHTDSVQDVAFDAQGKLLASCSADLSIKLWDFQQSYECIKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDQTIRVWLTNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKT... | Function: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as nuclear migration during cell division, mitoti... |
Q00664 | MSQILTAPQAEALHKAMLAYLSVINAPQTAETLREELHFDESYNEATCKKFEGVLEKKWTGIARLQRRINDLEAEVRSLQAELEASPSAARAKNQDPTNWLPKPSSTHTLTSHRDAVTCVAFHPVFTSLASGSEDCTIKIWDWELGEIERTLKGHIRGVSGLDYGGQKGNTLLASCSSDLTIKLWDPSKDYANIRTLSGHDHSVSSVRFLTSNDNHLISASRDGTLRIWDVSTGFCVKVIKSATESWIRDVSPSFDGKWLVSGGRDQAITVWEVSSAEPKAALLGHENFIECCVFAPPASYEHLATLAGLKKPPPATSSC... | Function: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for nuclear migration during vegetative growth as well as development. Required for retrograde early endosome ... |
P52922 | MDPSSLSNPQECKVTSLNLVLSVNFEKSQLQGYVEVASQIVKEGTESLILDTNQLEISHCNDVTSNPINFKLSEEHKVFGKALIISIPEGLRSVGKEFIVRVYYNTTVDSNALQWLTKDQTAGKLHPYLFSQCQAIHARSLVPCQDSPSNKVKYQAEITVPKPLTALMSALSTGKTESTDSSVFTFTQEIPIPTYLIAIVVGDLESRVIGPRSKVWSEPSMVAAAEYEFANTEKFIAVGEDLLTPYVWGRYDILLLPPSFPYGGMENPLLTFVTPTLLAGDRSLEGVVAHEIAHSWCGNLVTNKYWSEFFLNEGFTVFVE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotrien... |
Q5B0W8 | MATLMNPVRDPNTLSNYNNWLCTHTTANFEIFFEEKKLVGNVVHKLRSITNAETDEIILDSHHVDIRNVQVAGLPVKAWELLPPLGPYGTALKIKLENPVGLNEIIDVDIAVQTTKECTALQWLTPAQTSNKKHPYMFSQCQAIHARSIFPCQDTPDVKCTFDFNITSPLPVIASGLPVRSTSTVPQSGVKTLHRFHQKVPIPSYLFALASGDIAEAAIGPRSVVATSPDKLEECKWELEADTERFIKTIEEIIYPYAWGEYNVLILPPSFPYGGMENPVFTFATPSIISKDRENVDVIAHELAHSWSGNLVTSASWEHF... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotrien... |
P09960 | MPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLVLDTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTGNLVTNKTWDHFWLNEG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Bifunctional zinc metalloenzyme that comprises both epoxide hydrolase (EH) and aminopeptidase activities. Acts as an epoxide hydrolase to catalyze the conversion of LTA4 to the pro-inflammatory mediator leukotriene B4 (LTB4) . Has also aminopeptidase activity, with high... |
A5DSS4 | MEELKAYRPKTSPELDPSTLSNYTCFTVKLTTLHFDIDFEKKIVSGKVKYDLLNKSETDHVDLDTSYLDITKVSIQNESCDNQYKLHSRKEPLGSKLHILIPASTPKNFQLEIEFSTTSKCTALQFLDKEATDGKNHPYLFCQCQAIHARSLFPSFDTPGIKSPYKFSAKSPLKTLLSGLLIKEDNENNTVYFEQPVPIPSYLVSIALGDIARTSIGPRSDVMTEPVNLAKCKWEFERDMENFIQVAEKLIFEYEWQKFDSLVLPASFPYGGMEIPNLCQLTPTLICGDRSLVNVVAHELAHSWSGNLVTNCSWEHFWLN... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotrien... |
A4QUC1 | MAARDPSTASNYDAWKTKHTTANLRIDFDDKCLRGSVVLELESRTAKESKEIVLDSSYVSVESIKLNDVQTKWEIKERNGPMGSPLHISVPEGADSGEVVRLEMAVKTTPQCTALQWLTPAQTSNKKAPFMFSQAQACHARSLFPCQDTPDVKSTYSFNITSPHVVVASGVANDGDKAEADGGDKVYKYEQNVPIPSYLFALASGDIAMAPIGPRSSVATGPDEVKECQWELEEDMGKFMDAAERLVFPYKWGEYNVLVLPPSFPYGGMENPIYTFATPTIISGDRQNTDVIAHELSHSWSGNLVTSCSWEHYWLNEGWT... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotrien... |
Q7S785 | MWGRGFLQRARFAQLSPSSSSSRSLLSAASAAPPNLLYSHYQRGRWFGCSTANMAPVRDPNTLSNYDAWRTRHTTANLKIDFTAKCLRGSVILELESQTDKASKEIVLDSSYVTVNSIKLNSAPSLWETKARTEPNGSPVHIAVPEGAAKGEVVKVEIELATTDKCTALQWLTPAQTSDKAAPFMFSQCQAIHARSLFPCQDTPDVKSTYDFNITSPYVVVASGVPVPDETKDLGEEKLYKFQQKVPIPSYLFALSSGEIASAPVGKRSCVCTGPNELKASQWELEGDMDKFLEAAEKIVFPYRWGEYNVLVLPPSFPYG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotrien... |
Q84TA3 | MPPVDPHSYTDGDHPVTAKAALAFYLDFAASTIHASALLTLSAPHSGDLLLDTRALAVHSASTASGPPSPIPFSLADAADPVLGSALTLTLPPDTTSFLLTFSTSPSASALQWLSPPQTASSLPFVFSQCQSIHARSVFPCHDTPAARITFDLLLNVPTQLSAVAAARHVSRRDPLPSDHRGACDDALWCAPGRIVEEFQMEQSVPPYLFAFAAGGIGFRDLGPRTRVYAEGGDKVLDEAAREFAGVEEMVKVGESLFGPYEWERFDLLVLPPSFPYGGMENPRMVFLTPTVIKGDAAGAQVVAHELAHSWTGNLITNKT... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotrien... |
O94544 | MKLRLDPSTQSNYHDVSISKLDWHARIDFDQELLHGKVSFVIQSARVSQALSHIILDTSYLEIKNVTINDIPTPFRVDKRRGFLGSALHIVPADEIPSSKSCILTILYSTTKDCTALQFLKPEQTIGGKFPYVFSECQAIHARSFIPCQDTPSVKVPCTFKIRSKLPVIASGIPCGTANFCNGSLEYLFEQKNPIPSYLFCILSGDLASTNIGPRSSVYTEPGNLLACKYEFEHDMENFMEAAEQLTLPYCWTRYDFVILPPSFPYGGMENPNATFATPTLIAGDRSNVNVIAHELAHSWSGNLVTNESWQCFWLNEGMT... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotrien... |
Q6IP81 | MADPSSFASPEKFNIKHMHLKLHVDFTSRAIAASTSLTVRSLQDSLASLILDTKDLTIKKVAVNGKDATFALGTTHSFKGTPLEITLPFSLTRGQEVIVEIDSVTSPKSSALQWLNKEQTAGKIHPYLFSQCQATHCRSIIPCQDTPSVKFTYYSQVSVPKELMALMSALRDGELSEQSDSNRKIYRFKQNVPIPSYLIALVVGALEGRKVGPRTTIWTEKELLEPSVYEFAETEKMLKYAEDLAGPYVWGQYDLLILPPSFPYGGMENPCLTFVTPTVLAGDRSLASVIAHEISHSWTGNLVTNETWENFWLNEGHTVY... | Cofactor: Binds 1 zinc ion per subunit.
Function: Bifunctional zinc metalloenzyme that comprises both epoxide hydrolase (EH) and aminopeptidase activities . Acts as an epoxide hydrolase to catalyze the conversion of leukotriene A4 (LTA4) to the pro-inflammatory mediator leukotriene B4 (LTB4) . During the conversion of ... |
Q6C3E5 | MFSLRALSGVVTRSLVRAPHRRTMSHAARLLPHRVPQKKGPERDPSTLSNYEHFKPTNTTVCLKVDWTDQKLAGSVTYDLTVENSPKNLVLDTSYLDIQEVQVNGHKADFSIGERHNIFGSPLTITLPPNSGDKLQVKIAYSTTPSCTALQWLTPEQTAGKKAPYFFSQCQAIHARSVMPAFDTPSVKSTFDIEIESDHPVVASGLPIKSSNDTGKFVFRQKVPIPAYLFALAGGDLDSAPIGPRSDVYSEPCDLHKCQYEFEADTEKFINAAENIVFPYEWEKYDVLVLPPSFPYGGMENPNITFATPTLVSGDRQNVD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotrien... |
P13285 | MGSLEMVPMGAGPPSPGGDPDGYDGGNNSQYPSASGSSGNTPTPPNDEERESNEEPPPPYEDPYWGNGDRHSDYQPLGTQDQSLYLGLQHDGNDGLPPPPYSPRDDSSQHIYEEAGRGSMNPVCLPVIVAPYLFWLAAIAASCFTASVSTVVTATGLALSLLLLAAVASSYAAAQRKLLTPVTVLTAVVTFFAICLTWRIEDPPFNSLLFALLAAAGGLQGIYVLVMLVLLILAYRRRWRRLTVCGGIMFLACVLVLIVDAVLQLSPLLGAVTVVSMTLLLLAFVLWLSSPGGLGTLGAALLTLAAALALLASLILGTLN... | Function: Maintains EBV latent infection of B-lymphocyte, by preventing lytic reactivation of the virus in response to surface immunoglobulin (sIg) cross-linking. Acts like a dominant negative inhibitor of the sIg-associated protein tyrosine kinases, LYN and SYK. Also blocks translocation of the B-cell antigen receptor... |
Q9XYS8 | MVKRGCCHRKMVNHKGCLVSGIFLAVIGAVLFILAFALLPHLINQTTQNAVIQAVIVDSTSSQRYNDWAGQQSIENYYQQYFYAWNLTNPNEFLNGSIPIFETVGPFNYKYEFNFSNVTFQDGGNLATYTQSKSFIYQSDMSPNDPNEIMITNINPAYLGLMFQLAPNAELLDNMPAENLLIALSGCGQMRLFLEYLSSDNFTNIVYFTQNPKLYQEQYLNILKSLNGDEQYFYQQWANATSIPQKGNGWYGMLVSSVNNNNESSNISILSAKLLFNSSNENSILNQEIGSTLWINALLGDKTSITVLTSELQLTVDQID... | Function: May act as a lysosomal receptor (By similarity). May be involved in macropinocytosis and fluid phase exocytosis. Binds to the anionic phospholipid phosphoinositol 4,5-bisphosphate, but not to phosphatidylcholine and only weakly to phosphatidylserine.
PTM: Heavily glycosylated.
Location Topology: Multi-pass me... |
Q9BKJ9 | MKHIGRIVSFPIGLVLIAVGIIIFVVVNRTIKDEFKKAAVVIPDNGAEEIVDPWVRFIGNEGDPNNVRTYTFMAYNLTNPIETMQGHLPKYQEVGPYSYNYIYERINANLYEDDEKLSFKLWKRYFPIVADGYRDPTKDTIYHFNLVYGAAVKQAGSEVALSVALTAAAMGKIITGLTDPSFKVKAGFAAAPTVTAGAFSNLLTAAGNDPATACGLWQTSTSSSTPLVPFSVPIIAGSPSDISQAQCQALFDPSNKFSLTDPTNVGVYLLNPAGSKAALLASPFGLTSVQADLIMKYQLALTSTFVPTTLVSRFAECSDP... | Function: May act as a lysosomal receptor (By similarity). May be involved in macropinocytosis and fluid phase exocytosis.
PTM: Heavily glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 82572
Sequence Length: 755
Subcellular Location: Lysosome membrane
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Q55FQ9 | MVANNKGLLIAGLLLSVIGAALFVISLALLPSVLNVATNNAIVDAVIVDSFKSQRYNDWAGQKSVDNYFKQYYYLWNLTNPNEVLNGKNCNFEKIGPFNYKYEWNNSKVSFSDDGNLINYIQSKSYKWIEGEDSLNPFTVSTTNFNPAYLGLLSTLSKNSITLGMTAEDLLYTLASAPQTKQFLEYLSSDNFTMIAYFYNGPKYFNQQYQLLLSTINNNLTTTPTIYFLEQWSNSTIIPTNGNSSLWDNMLISYGLDSPSGISLQSALEILNPMNQYSLLNSTNGISYWINAVFNGPNSNSYQILEQELGINQAQLTLVM... | Function: May act as a lysosomal receptor (By similarity). May be involved role in macropinocytosis and fluid phase exocytosis.
PTM: Heavily glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87876
Sequence Length: 782
Subcellular Location: Lysosome membrane
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Q5JGG6 | MTPEEVVERYSQVISRASHVTYVPIVPSRAENALVWDIEGRAYIDFLADAAVQNVGHNNPRVVEAVKKTADRLLHFTFIYGFPVEPLLLAEKLREIAPLEGAKVAFGLSGSDANDGAIKFARAYTGRRSIIGYLRSYYGSTYGAMSVTGLDFEVRSKVGQLSDVHFIPFPNCYRCPFGKEPGKCRMECVSFLKEKFEGEVHAEGTAALIAEAIQGDAGMVVPPENYFKKLKRILDEHGILLVVDEVQSGLGRTGKWFAIEHFGVEPEIITLAKPLGGGLPISAIVGRGEIMDSLPPLGHAFTMSGNPVASAAALAVIEEI... | Function: Amino acid racemase that shows relatively high activity toward leucine, which is the preferred substrate, and methionine . Also exhibits lower levels of activity toward phenylalanine and alanine, and trace activities toward isoleucine and valine .
Catalytic Activity: L-leucine = D-leucine
Sequence Mass (Da): ... |
P97046 | MERGPQMANRIEGKAVDKTSIKHFVKLIRAAKPRYLFFVIGIVAGIIGTLIQLQVPKMVQPLINSFGHGVNGGKVALVIALYIGSAAVSAIAAIVLGIFGESVVKNLRTRVWDKMIHLPVKYFDEVKTGEMSSRLANDTTQVKNLIANSIPQAFTSILLLVGSIIFMLQMQWRLTLAMIIAVPIVMLIMFPIMTFGQKIGWTRQDSLANFQGIASESLSEIRLVKSSNAEKQASKKAENDVNALYKIGVKEAVFDGLMSPVMMLSMMLMIFGLLAYGIYLISTGVMSLGTLLGMMMYLMNLIGVVPTVATFFTELAKASG... | Function: Efflux transporter for a variety of amphiphilic cationic compounds, including antibiotics.
Catalytic Activity: ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64617
Sequence Length: 590
Subcellular Location: Cell membrane
EC... |
P46104 | MSVFARATSLFSRAARTRAADEAARSRSRWVTLVFLAVLQLLIAVDVTVVNIALPAIRDSFHVDTRQLTWVVTGYTVVGGGLLMVGGRIADLFGRRRTLLFGAFLFGASSLAAGLAPNLELLVLARFGQGAGEALSLPAAMSLIACSSRTAPFQGVERLASVASVGLVLGFLLSGVITQLFSWRWIFLINIPLVSLVLVAVLLLVKKDETTARNPVDLPGALLFTAAPLLLIFGVNELGEDEPRLPLAVGSLLAAAVCAAAFVAVERRTAHPLVPLTFFGNRVRLVANGATVLLSAALSTSFFLLTMHLQEERDLSPIEA... | Function: Proton-dependent transporter. May mediate the efflux of lincomycin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50421
Sequence Length: 481
Subcellular Location: Cell membrane
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O35018 | MILETTAKASQQYKVMPIMISLLLAGFIGMFSETALNIALTDLMKELNITAATVQWLTTGYLLVLGILVPVSGLLLQWFTTRQLFTVSLIFSILGTFIAALAPSFSFLLAARIVQALGTGLLLPLMFNTILVIFPPHKRGAAMGTIGLVIMFAPAIGPTFSGLVLEHLNWHWIFWISLPFLVLALVFGIAYMQNVSETTKPKIDVLSIILSTIGFGGIVFGFSNAGEGSGGWSSPTVIVSLIVGVVGLILFSIRQLTMKQPMMNLRAFKYPMFILGVIMVFICMMVILSSMLLLPMYLQGGLVLTAFASGLVLLPGGILN... | Function: Proton-dependent transporter. May mediate the efflux of lincomycin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51709
Sequence Length: 479
Subcellular Location: Cell membrane
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P94441 | MKKSIWIAWKDVKIRITDRKGFMMLILMPLILTCILGAALGSVVDGGSRIDDIKVGYIQSDQSDTANMFTKDVLKKMKSIKVTKVGSKDKMKKLIDEKKIDVGIVIPNHWEAGKTSAVVNAAPDQTLKSSIIETAASSFIEQYKAVKEAASGSMDYISKTEAVKQGKLDPAQFAEKLAKTLEKETGDKLTIAEKSVGSKAVTSFQYYSAAMLCMFMLFHITVGAKSFLQEKDTETLARMLMTPAQKSVILFGKWLGTYLFAIIQFFIFLIVTINVFGVDWGGNLLLVSVLGLSYAAAVSGISMLLASCISDMKTADAIGG... | Function: Required for resistance to linearmycins, a family of antibiotic-specialized metabolites produced by some streptomycetes . Part of the ABC transporter complex LnrLMN that probably facilitates linearmycin removal from the membrane. Responsible for the translocation of the substrate across the membrane . Also me... |
P94442 | MKKILAICGIELSLIFKKPQNYLIMFAAPLLLTFVFGSMLSGNDDKVRLAIVDQDDTILSQHYIRQLKAHDDMYVFENMSESKASEKLKQKKIAGIIVISRSFQTQLEKGKHPELIFRHGPELSEAPMVKQYAESALATLNIQVTAAKTASQTAGENWKAAYKTVFAKKHEDIVPAVTRQTLSDKKEGAEASDTASRAAGFSILFVMLTMMGAAGTILEARKNGVWSRLLTASVSRAEIGAGYVLSFFVIGWIQFGILLLSTHWLFGINWGNPAAVIVLVSLFLLTVVGIGLMIAANVRTPEQQLAFGNLFVIATCMVSG... | Function: Required for resistance to linearmycins, a family of antibiotic-specialized metabolites produced by some streptomycetes . Part of the ABC transporter complex LnrLMN that probably facilitates linearmycin removal from the membrane. Responsible for the translocation of the substrate across the membrane . Also me... |
D5SL78 | MQEFEFAVPAPSRVSPDLARARARHLDWVHAMDLVRGEEARRRYEFSCVADIGAYGYPHATGADLDLCVDVLGWTFLFDDQFDAGDGRERDALAVCAELTDLLWKGTAATAASPPIVVAFSDCWERMRAGMSDAWRRRTVHEWVDYLAGWPTKLADRAHGAVLDPAAHLRARHRTICCRPLFALAERVGGYEVPRRAWHSSRLDGMRFTTSDAVIGMNELHSFEKDRAQGHANLVLSLVHHGGLTGPEAVTRVCDLVQGSIESFLRLRSGLPELGRALGVEGAVLDRYADALSAFCRGYHDWGRGASRYTTRDHPGDLGL... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: In vitro, catalyzes the formation of R-linalool from geranyl diphosphate (GPP). Can also accept farnesyl diphosphate (FPP) as substrate to produce trans-nerolidol.
Catalytic Activity: (2E)-geranyl diphosphate + H2O = (R)-linalool + diphosphate
Sequence Mass (Da): 363... |
Q8F724 | MFYNFISKDSILYRLILCFGIGIGTVFGLSPFSFFSAGVFASISCIFLFFSLNRTSIWKAFLWLLILSQILNFTAFYWIPGAISRISGVNTFVSILFFFLYGLISHLKFFLFYTLFRFSKIDSASKTYILLIFPAAGTLSDMITFQIFPWYWGNLISGSIVFEQFASICGVYGLSFLLLFISSTFLILVNYYKYKNSKEFKTSIASLICITFIYGFGLYRIGYINQSQNELKPKNLSVLMIQPDTSPGTKDLKADASYLSATMSKVFSLAIPTFENSPSLIVIPESAIPFHGTIDSEENRKEKIYSSTMEGIILYLSKHT... | 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... |
P61037 | MKNKFIFFTLNLLLAVLGAVLFALSHPNYLNLNGFPFFAYIALIPFFLLLKRTKLKFSFLWGAFSGALSYFIFNFWIIFFHPLAIYIIIAKYCILYSVLFFVLKIIDSYFSRYSFIFQTIAWVAFEYLNTLGFLGYSYGIMGYTQWNFPILIRVSSIFGVWGISFLLVFFSACSASFLFEFYKEKDIKNVYQRYKLPMMIWVGTFFAFILYGAFTKIDLSEAQRARIALVQPNRDPWLGNLEVYRNNYEELKNLSEKALKNFPDIELVVWPETAFIPMIRWHYKYTSTYNPNSLLVRELLHFLDNQKVPFLIGNDDGVLD... | 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... |
O83279 | MRIEEWCRSRLGEFLLFVLAVSLFALSHPNPLLPRGCALLAYGALAPLFLLVRWASGFAVVFWGGAYGAFSYGAFSYWLFVFHPVALCVVAGFSALFLAALCLALKAGGAFWQRRALLVQCLVWLGYEYAKTLGFLGFPYGVMGYSQWRVLPLIQVASVFGVWVVSALVVFPSAWLASVLGQWVEESERNARAFLSAAYSHWVSALVWVGLCGFCVCAAKAGWWPDCTAHTRAKVALVQPNGDPRRGGIESYRADFSTLTYLSDWALERYPDVDLVVWPETAFVPRIDWHYRYRHEQQSFQLVCDLLDYVNAKNCPFIIG... | 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... |
Q8EYY4 | MDTLHHRFQQFQKTIWFNIFCYLWTGIFSFLAFAPVSLTHFVWIAPFGFFWLSLKYHGKYKKLFFHGLLIGVVFYAISFHWIIHMAITFGNFPYVVAILILLFAGLLFGLKFPIFMMSFSFLSGKIGRHSVWVAGFCGLLSELIGPQLFPWYWGNLAAGNIILAQNAEITGVYGISFLVFIVSYTLFQSNPWHWKEIIHSKEKRKQYLRFITLPALLLLTFIVSGIFLFKKWENVKPVKSLNVLIVQPDAPLSFRDGREIKESIEALMARIEKLTDEGAVRLGKKPDLIVLPEAGVPFFSAHKTEITTKVRRMYWDRFDS... | 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... |
P61038 | MRFFLSFFIIFISSVLFSFGIPNEILNFGSAIAGFSGLVLVYYALLNCGSHKRAAFLYGFFVSFVHLMSSFWLAFFEDFAIFTLGASTLAYFFIAMPFGFLLYHSLQKRENLRPFFFAAIWLLWEFAKSTGFLAYPWGTAPMICFNLKPFIQFVDITGVWGLSFIVPLIAACLGEALQTYAYSANSKAFFKGLTEIKSPLIFTAFLVLIINIYGITILSIEMKPATFLNTVIVQQNTDPWDNSQFEENIKTSQALSRKAIFSANKKPDLIVWSESSLIVPYKDNEDFYGILPYDDPFTRFLADTDTPIIVGSPYIDGKKQ... | 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... |
O83432 | MLCTAPLVSSAASAVLLAFAIPNEFWLAGSSVLGLGALVPLYVGFLLSPAKKHVACSYGLFVALVHACSSFWLKNFQGFALFTLGASTVGYFFYALPFGVAFACILRKQAPARACAFALVWTLWEWVKSTGILAYPWGTVPMTAHSLSHLIQIADITGVWGLSFLIPLANACVAESLHFFIKKRDSVPVFRLWLLTGCLYCLCSLYGAYRIATLGAPRTTLALAIVQQNADPWDTXSFEKNLTTAIHLTETALRTQTAPPLPTTPYRKEKTLTHASARAPVDMVVWSESSLRYPYEQYRHVYNALPAARPFSAFLRTLGA... | 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... |
O67000 | MLTDRHKEVLKGLLAGILFYLSFSKLNLYFLVFPALFLGIRKNFLRLFSFGFSAFFLSLLWIRIPLIDYGNINPFIAYPALVLLVLFLSLYQFGLTYLLWRVFKFSFFAFPFLYTLVEILRSHLPYGGFPWLLLGVNLVDIPVLRYTLNAGTVFLGSFVVLLISLFPLFNKKEKIFSLAIITPLLIYGFIKETSYRVTHYGLKIALIQPFVPQDVKLNRELFELKYGEIIELVKKAVEKKPDLVVLPESAFPFYLGELEEKGKEILELSKKVPIITGFIEIDEGFKPYNTVVLLKDGRVIEKYRKIKLVPFGEYTPFPFK... | 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... |
P61032 | MDSLTLYVTNTMMKRWFQFFKHKAYDFRWAILSGILVGTSYIPFPPWALIFCYTPLWIYVTEESSSVKKSFWAGWVTQFILTLIGFHWIAYTAHEFGQLPWAVSYLALLLFCAFMHLYIPVAVAAGTWLRLRFKLSGGQTLFTIALLHALLERTWPVIFEWHLGYTLIWSKIPMYHLADLVGFHGLSAVVLLFNAWMGYVWLKQSFVKKALSHLSLLALTFAALVGWGFWHGKAWNKFDGETKATVVQANIGNLEKIYAEQGRAYQEVITRKFLDLSFAAMQKYPQTDILIWPETAFPDYLDQHLLDRKHAQILISGLQP... | 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... |
Q7VRA5 | MFISKAKYFFQLILSLTFGICGVFAFSPYDFWPLSIISITGLLIIILSNITWKQIIWNTLFWGIGFFSVGLHWIYIGIDQFIPTHKNMNFFLIAFLIIYLTCYSVLFSIILVTLRLFITQWSFLSITAATLWLIIDRLRGNEFIGFPWLQFGYSQISGPIRGIGPLLGVEGITFCLVLISSLLALSIRTVQPSPYYISLIILACLYPLSWIQWYQVQPQRMTTIALVQGNINQHLYWNTENIQKTLKIYLQHTLPLLGKVKIIIWPESAIPGNELAHNELLVSLDYQLRKHHTYLITGIIDSRLINNSYYHHYNSIIVLG... | 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... |
F2JXJ3 | MALSVHPSIGVARLGNANTDNFVLNPMEIGGLPYEHDVDLKPTTTVVNFKDEAGCIRRQGQVFKVFGASNEELTLDSPNVKNIEWTVHLANKKAAWYEFRELNGNLLYGRDNSYSARGVPWRNASKTASSERQSLIIDLGPRSVSGVMATVEISINNIPETYLHPSYPSGELLQGSKHFESLGTLRTDSQGRLIVLGGYGFAGGNTDLSGYGGGDDWYDDISDGSVTCVVTYSDDSSETSTAWMVVGSPDFAPEIVNISTLSDTCFDVGVRNFDLVPDMYDSATGHYKSDYVANFDRDILPIIQRISQYQWVSNVQSMSG... | Cofactor: Contains 1 cysteine tryptophylquinone per subunit.
Function: Has antibacterial activity against a wide spectrum of Gram-positive and Gram-negative bacteria including nosocomial isolates of S.aureus and Pseudomonas sp. The antimicrobial activity is due to hydrogen peroxide generated by its lysine oxidase activ... |
F2JXJ2 | MESYDAIVIGGGPAGAASALSLLTHHNKRVLLLERGDFSQARIGEQVSHSIFDFLAYLDLPVSEFGESCFSPNYGKTSLWGSSIESHHLSMFATQGATYQLDRAAFDETLLMAFVERGGTVIPRCKQMKIEQSDSVWQVQFVHPEQGEQTVCCDYLVDASGRQSKLSAMLGVEPVMDDQLVGVGAFIRNPDNAFEQHQRIESCEYGWWYMAGLSSELAVVTCFTDMDIMREMRLNKASVWNQYLAETSAIADCVKGSETTHPKLWVKQAHSQYCTSELPDRFIAVGDAALSFDPVSSMGIGFAMTSACHSTRALVSDSKD... | Cofactor: Binds 1 FAD per subunit.
Function: Is required for lysine-epsilon oxidase (LOD) activity in M.mediterranea. May be involved in the generation of the quinonic cofactor of LodA, leading to the active form of LodA containing a tyrosine-derived quinone cofactor.
Sequence Mass (Da): 41421
Sequence Length: 369
Subc... |
Q9S752 | MGNISSSGGEGRRRRRRNHTAAPPPPPPPPSSSLPPPPLPTEIQANPIVFAAVTPYPNPNPNPVYQYPASYYHHPPPGAMPLPPYDHHLQHHPPHPYHNHSWAPVAMARYPYAGHMMAQPTPYVEHQKAVTIRNDVNLKKESLRLEPDPDNPGRFLVSFTFDATVSGRISVIFFAKESEDCKLTATKEDILPPITLDFEKGLGQKFKQSSGSGIDFSVFEDVELFKAAADTEIYPLAVKAEAAPSGGENEEEERSGSKNAQITQAVYEKDKGEIKIRVVKQILWVNGTRYELQEIYGIGNTVEGDDDSADDANDPGKECV... | Function: Acts as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates (in vitro). Required for GLUTAMINE DUMPER 1(GDU1)-induced amino acid secretion and for amino acid homeostasis. Ubiquitinates GDU1 (in vit... |
Q8RUN2 | MEIESKFKRICVFCGSSAGNKVSYKDAAIELGTELVSRNIDLVYGGGSIGLMGLISQAVFNGGRHVIGVIPKTLMPREITGETVGEVKAVADMHQRKAEMAKHSDAFIALPGGYGTLEELLEVITWAQLGIHDKPVGLLNVEGYYNSLLSFIDKAVEEGFISPTARHIIVSAPSAKELVKKLEDYVPRHEKVASKKSWEMEQIGLSPTCEISR | Function: Cytokinin-activating enzyme working in the direct activation pathway. Phosphoribohydrolase that converts inactive cytokinin nucleotides to the biologically active free-base forms.
Catalytic Activity: H2O + N(6)-(dimethylallyl)adenosine 5'-phosphate = D-ribose 5-phosphate + N(6)-dimethylallyladenine
Sequence M... |
Q5BPS0 | MEETKSRFRRICVFCGSSSGNKTTYHDAALQLAHQLVERNIDLVYGGGSVGLMGLISQAVHDGGRHVLGIIPKSLAPREITGESIGEVITVSTMHQRKAEMGRQADAFIALPGGYGTFEELLEVITWSQLGIHTKPVGLLNVDGFYDSLLTFIDKAVDEGFVSSTARRIIVSAPNAPQLLQLLEEYVPKHDDFVSKMVWDNTTDAFTLEGDSF | Function: Cytokinin-activating enzyme working in the direct activation pathway. Phosphoribohydrolase that converts inactive cytokinin nucleotides to the biologically active free-base forms.
Catalytic Activity: H2O + N(6)-(dimethylallyl)adenosine 5'-phosphate = D-ribose 5-phosphate + N(6)-dimethylallyladenine
Sequence M... |
Q8L8B8 | MEIKGESMQKSKFRRICVFCGSSQGKKSSYQDAAVDLGNELVSRNIDLVYGGGSIGLMGLVSQAVHDGGRHVIGIIPKTLMPRELTGETVGEVRAVADMHQRKAEMAKHSDAFIALPGGYGTLEELLEVITWAQLGIHDKPVGLLNVDGYYNSLLSFIDKAVEEGFISPTAREIIVSAPTAKELVKKLEEYAPCHERVATKLCWEMERIGYSSEE | Function: Cytokinin-activating enzyme working in the direct activation pathway. Phosphoribohydrolase that converts inactive cytokinin nucleotides to the biologically active free-base forms.
Catalytic Activity: H2O + N(6)-(dimethylallyl)adenosine 5'-phosphate = D-ribose 5-phosphate + N(6)-dimethylallyladenine
Sequence M... |
A1S8R4 | MINLRRFTKFTLAGLTALSLLGGCSVTPKVALQPVSVENASDAKAWELKGKLLIRTNGDKVSANLFWLNTPDNAELRLTSMLGTTVLLLTQNRDGATLEVDGKRYSDLSPQRLLDGLSGFTLPIDALPFWITGQPMAGDEVEFDTLNRPKTIISADGEWTINISSWQTQSGAPVPRMLELTHASAVIKLQTNEWQALANATGSKGAR | 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): 22466
Sequence Length: 207
Subcellular Location: Cell outer membrane
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B8E817 | MNNLKRLTKTIFSCFTLSALLLLAGCETLPPMTDLSPITVIDARQATAWELQGKLAIKTPDDKLSANIYWRHSEDRDELTLTTMLGTTVLTLNSTPNSAHLHIDGKDFRDDNAQRLLERVSGWSIPLADLPLWITGQVGPNDQVIESDSQGKPKQLTNTQTPPPWQVAFLSWQSQSGASVPHQLKLERGDLQLKLQLNQWQALGKPAILVGEQP | 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): 23753
Sequence Length: 214
Subcellular Location: Cell outer membrane
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Q12QS0 | MPVNLNHTLLLCLLVAASLLSGCSSTLGEQYQTLNVSQSKQAKAWELQGKIAVKSPTDKFSTNLYWFHLGEENQLSLTTMLGTTVLTLNSKPGLARLEVDGKEYVDSNPQDLLEAVSGWSIPLDNLPLWITGQVGVNDEISAYHDDGLIKSLISPAPEHNWQVSFLSWQQQSGASVPKQIKIERAGVQVRIQINRWQALKTQQ | 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): 22466
Sequence Length: 203
Subcellular Location: Cell outer membrane
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A4Y3J6 | MNNLKRFTESIFSCIALSTLLFLGGCQTLPPADDLTPITVSHPDQAKAWELQGKLAIKTPEDKLSANLYWRHSEERDELTLTTMLGTTVLTLEATPNSAHLHIDGKDFKDNNAQDLLERVSGWSIPLADLPLWITGQIGSQDRVLSRDSKANPKQLINDQTPPSWVVEFLSWQLQSGAHIPHQLKLERGDLQLKLQINQWQALGKATIMIGEKP | 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): 23936
Sequence Length: 214
Subcellular Location: Cell outer membrane
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Q3A558 | MSRGAAMIEVTNLCKSFVSGTRRVDVLSHVDMKIDAGERVAVVGASGAGKTSLMHILGGLDRPTSGDVLYDKQDIFSLKGAGLDDFRNRTLGFVFQFHQLLPEFTALENVMLPALIARWSRAKAKSAARELLTEVGLESRLSHKPGELSGGEQQRVAIARALVGSPRVLFADEPTGNLDSNTSESIYRLLSRLHETRGLTLFIVTHDARLAAGLDRVVHMADGRITG | 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 ... |
Q73L25 | MSKDIVLISGLTKTFSSASEKLVIFDKLNFSIEEGKKISITGESGSGKSTFLNILGGLESADSGEIIAGSYKVHSLDEKSLTEYRSSFLGLVFQFHYLLKDFTALENVMLPALIAGRSKKEIKEKALSLLEDVKLAERKNHFPSQLSGGERQRVAVARSLINSPSLILADEPTGNLDPANAETVQNLLFSVVDKHKKTLVLVTHDQNIASMTDISYKLYKGNLEEV | 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 ... |
O83590 | MNDPILSVEQVSKSFCCATERIQILSDVSFSVPRAVKVAITGESGCGKSTLLNIIGGMEHADSGIVRVLSCDVLTLHEHALTEYRRQFLGLVFQFHHLLRDFTALENVMLPGLIAGKSYREVRARAYELLEKVRVVQRAHHFPAQMSGGERQRTAVARALINDPTLILADEPTGNLDPKNALIVQDLLFSLTEEYQKTLLIVTHDPRIASMTDYRYQLQQGSLIRI | 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 ... |
B8CY71 | MDQEMVTKETEKYIELPLLASRGVVVFPHMVIPLLVGREKSIEALEKAMVKDKEIIILSQKDEKIEDPDPEDLYTIGTIAEVKQLVKLPNGMLKVVVEGIKRARIIDFIEIDEYFEVRAEILDQTVPEVDLEMKALMKAVLNKFQEYIKYNRNLPSETIMTVTNIEEPARFSDTIASHLELKFRQEQDLLEAISIKERLNKLLEIIKDEIEILKVEQKIQKKVRKQVEKTQKEYYLREQLKAIKEELDEDEEDDEIEEYRNKAEELDLPEKIREKVDKEIEKLKKTPSMSPEATVIRNYLDCVLDLPWNKVREEKIDLDE... | 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 ... |
B0TFI9 | MAEEEKIRQTIQELPLLPLRGIIVFPYMVMHLDVGRERSVNAIEEAMAQDRIIFLATQKEAQTDQPGAEDIYQIGVIAEIKQLLKLPGGTIRVLVEGLARAEILEYIDMEPLIRVRVREHIEPDVKSNAVEALMRSLINQFEQYVKISKKIPPETFVSVVAVEDPGRLTDTISSHLTLKTQDKQRILEALDVTERLEILTEILAREMEILELERKINVRVRKQMEKTQKEYYLREQIKAIQKELGEKEDRQAEGEDLRNKIAKAKLPKEVEEKALREVERLEKMPPMVAEATVVRNYLDWLLALPWAKQTKDRLDIDKAE... | 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 ... |
P55995 | MTEDFPKILPLLVEEDTFLYPFMIAPIFLQNNASIKAVAYAKNNKSLVFIACQKDKLNDNEAPYYDVGVIGSVMREANMPNGRVKLLFNGIAKGRILEPAKENEQGFLEAQISPIEYLEYDKENIQAIVEVLKEKVITLANVSSLFPPDLIKALEDNDDPNRIADLIAAALHLKKDQAYSLFANNNTEQRLLDLIDIVIEETKTQKLQKEIKSKVHQKMEQTNKEYFLKEQLKQIQKELGTDKQRDEDLNQYYQKLESIKPFLKEEAFKEIKKQIDRLSRTHADSSDSATLQNYIETMLDVPFGQYGKKALDIKHVREQL... | 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 ... |
Q1IPZ8 | MANEAHNIEHTDPEFRDDSADARTLPLLPVRDTVLFPHAVLPLTVGRESSVQLINSLGEDKTIVVVAQREARVDSPQPSDLFAIGSLAVVHKVVKMPNQSLFVFAEGLERVRVTEYVQLNPYMRATVETVPEAFPPKSAEIEALQRNVLTLFQQIVTGSPTLSDELSTVAMNIEEPGRLVDFVASSLPSLSTKDKQEILETADVQIRLDKINQHLAKELEVQQLRNKIQSEVQDRVQQTQREYYLREQLKAIQKELGEQDDSTRDADELREKVEAAGMPDDVKKEALKELGRLARMSPMAADYSVTRNYIEWLAVLPWQK... | 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 ... |
A9KH99 | MSEYTRQLPVVALRNMAVMPGMLIHFDVNRKVSIEAIEAAMLLNQQVLLVSQIDAETENPTADDLYRVGTIAEIKQMIKLPGNVIRVLVTGLERATLDSLVSEQPYLKAQLTSKEAELLNLTEAEEEAMVRALRDLFEVYTTENNKLNKDIIRQVEASREIEKMVEQLSIHIPMTLEDKQLLLAASDLMEQYERLCLILADEIEVMRIKRELQNKVKDKVDKNQKDYIMREQLKVIKEELGETSSVSDIMQYLEQLKELVASDEVKEKIKKEIERFQNVAGSNSESAVARGYVETLLSLPWDKVSEDFMDLAYAKEVLET... | 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 ... |
Q72UP9 | MEGGPLEPLEDLSGIEENSIIPLDSILPPELFLIPIKSRPVFPGIITPLIVPSGKFAKAVEETVKGNSFLGLVLLKDEENEKETSENIYQYGVVAKILKKVNLPDNAVNILVNTIRRFKIESFVNKDPLVARVSYPEEEPGAPKNTTKAMMRTLLVMTRELAQNNPLFTEEMKLTMLNVNEPGKMADFVCSILNLEKEEYQSVIESNILKTRIEKVLLFLKKEIELVSIQREISDQIQDKIDKQQRQFFLREQLKAIQNELGIKDDKFEKKYEKFLERLKNLNADPEVIEEVTRELDKFSYADPNTGDYNVIRNYLDILE... | 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 ... |
A0L516 | MSEQRSDEPEVVDAIIEDQQGAQATTDATPPVRIENSLPTELVIYPLGGRPFFPGMLTPIQVEGSPYYETIKKAMDSHGRLFGILASHAEDGQEVFDANQLFGIGTVVRILEASVNEEAKQIKLLAEGLWRFEVRDVVSVGPPIVAQVTHHNNPVSVVDTDALKPYTMAVINTLKEILKYDSLYQEQVKMFLSRHNFSEPDRLADFVASMTSSSREELQEVLETLPIMARLEKVLTLLKKELEVVKLQNKIQRQVEEGIAEHQRQFFLREQLKEIQKELGITKDDRTAEIDRFRERLEKLTLSEEAEQKIEEELDKLAIL... | 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 ... |
Q600B5 | MPTNSYRFLVASEDIYFQNTLQQSITFSDPESIKVLKDFYHSNSRPTLTNKDFLIVYRKEKEKDTKKKNSSVIKFPRNDFNSFEDSKNDIQNQAKILNGKVGDFENSLLPRIYDLDELSKYASLARIQSYRAKTSPDKSEWQTVILDFIVTEKVQLVELINDPQNPKVGQIIIKPVRETIKSPEIHINLINDLLEMARKAKNFRIPTELLLIVDKFGANSEYSTNEYIKGVTNTLSCSPSLTYPQKYQLFSYNSYPAKIKKLYEHIHTFAEQIKLEDEINVILKTNLDKQQTEFILKEKIKAIRKKLGEDSRYEDEIEEL... | 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 ... |
Q6KI22 | MKYPFMATRGVITFIGNSSTIEVGRPLSLAAIDLAKSDFENKLVLIPQKNIKQNEIEFEKDLENVGILTKIKSIKILSNGNRKIIVEGVERIKLDSIEKDKNNNDIIANLSLYPVLKNENGSSETIIEKMQTSLNNIIESNLPLVANQELSKHESSERYTYILAHYLTMPFEKKFEIFAKKSLTEMLELIFSFLVELKNIQKLDVDLDKDIKKNLDSQQREYLLRERLKVIQKKLGDDENDEEEIEEKLNSKYGKEQYPEEVIKTIKNEKRRLKNMMSSSPEANTSRTYIEWLTNLPWRKVSVDKTNLVKSKEILDSYHY... | 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 ... |
Q469F5 | MRRLTMYPEQPDENRESIVMPLFEVVVYPKSRAKFLADKVTGEILLNDMKNAESVSAIGLTVKNGTKASDLSEESLYKIGNLLNITYVQPSDDGYLVVAKGIERVEAVSLYQKNGLFYATYRPVHDLPDFDEDAETEVMANIKKTIHEISARFQGSEQFTKSIDKMDSIDQIMGFVMPYIPVKLAEKQRLLELASVRERYLLFLHILTKHKENINLQIEMAKKVTDKISKSNREAMLREQLKVIQEELNEGDDSASGDAAYREKIENSTMPDEVKKKAFSELKKLETGGSHNPEAPGIRNYLDLLLDLPWITEEKKSIDI... | 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 ... |
B8EMF2 | MESFAPTRKGRAVFSADAAATAAPGSAGAGETLDPAKDALIIVPVRGFVLFPGIVMPVVLNGPAAIAAAQEAVRQQRSVGILMQRESGAEEASPLNMHRFGVVANILRYITAQDGGHHLICQGEQRFHVEEFLRERPYLAARVKRIEEPDERSPDIEARFVHLQGQASEALQLLPQTPPELIAAVNSAPSPGALTDLVAAYMDASPAQKQDILETIDLRARMDMVAKLLAQRIEVLRLSQEIGRQTKASLDERQREMLLREQMASIQRQLGEGDGKAQEIAELTEAIAKAKMPAEVEEAARKELRRLERMPDASAEYGMI... | 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 ... |
Q2NEP8 | MTQEMENENLSFTQQLRKDGFIKDIDTNPTCFDDTDSQNQLPIIFIPNTILLPHTDITLNLDKQHTDNLLHTVDDNNHGIILTPKKLEEGNGNVEFYDVGVILEIKSLTEDKENELLPEEYVLELKVKDKVYVNKILKKDGFFHAQYKILPEENTLTEDEITELNKNIDETVLEIAKFLPNTDKYTRKILGKLDTQDKLAEVFPFLKVPINKKQELLELDSVKIRALKVIQLLLEQKDAIGIQMELAKKLNKKMNETHKNTLLREQMKLIQEELNMTDDTPAHKTYRERIKDAQLPKEVEEAALEEVTKLERQGQNNAEE... | 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 ... |
A5IYF2 | MLFDREVAKLEITDELITQTTYWKQIIDEYTKDNSNGAEIINKARIMLVYYRPAEDNRVILESELQSKPTATYADVLENVNISNLDSNMTLCQVESVEKVYDNGSQKWHYIATLKAIHKYILQDIYGDEETISSSSIDIEKLPLKYIEGMVATRFGSENNGDEMALADPSLDFNGFEEVINTLIYDRNWNDAMLLYRYIRGYSAKEIRNWTKGTSEMMPDFINDDESRLETLVRALTGFFLLPPYELFTIYSMPSALHQFEALKSNFVLMVRLIKKFINELNLGNTDKLLNIYNALTDNELFKNSMEQIKENSELEVQFN... | 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 ... |
R9WS04 | MLKPQIHKPHLVNKLPLGTPFIPSHASIASFSTTSLRTLSVQKCYRRYIRYTSSNIKAIMPDSIGKSIRKKCVVTVQPTISGALTAVTVGLLGTVADSVSDFLGRSFLLELVSSDLDSSGKEKDTVKAYATYDELDKESKLYKYQCEFEVPDDFGEIGAVLVQNERHRDAYVKNIVLDEIVTFTCDSWIHSKFDNPDKRIFFLNKSYLPSETPEGLKSLRQKDLESLRGNGEGERQSFDRIYDYDTYNDIGDPDTDSDMARPVLGGNEHPFPRRCRTGRKMTSTEPWSESRTTLPFYVPRDEDFAEIKQITRGATTLYSV... | Cofactor: Binds 1 Fe cation per subunit.
Function: Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure.
S... |
O24371 | MALAKEIMGISLLEKSSSFMNSSSMALFNPNNYHKENHLWFNQQFQGRRNLSRRKAFRQSTMAAISENLIKVVPEKAVRFKVRAVVTVRNKNKEDLKETIVKHLDAFTDKIGRNVTLELISTDMDPNTKGPKKSNQAVLKDWSKKSNLKTERVNYTAEFIVDSNFGNPGAITVTNKHQQEFFLESITIEGFACGPVHFPCNSWVQPKKDHPGKRIFFSNQPYLPDETPAGLKSLRERELRDLRGDGKGVRKLSDRIYDYDIYNDLGNPDKGIDFARPKLGGDDNVPYPRRCRSGRVPTDTDISAESRVEKPNPTYVPRDE... | Cofactor: Binds 1 Fe cation per subunit.
Function: Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Required for the regulation of wound-induced gene expression, but is not involved in the b... |
F1RD85 | MLRSELRDMVVAMVLWGILLPFCLSQTTSPSQDGKIKFRLAGYPRKHNEGRIEVFYNREWGTICDDDFTLANAHVLCRQLGFVEALSWSHSAKYGPGSGKIWLDNVICGGSENSIEKCVSRGWGNSDCTHQEDAGVICKDERLPGFAESNIIEMQVDEKRMEKIRLRPLKGAHAGRLPVTEGVVEVKFKEGWGHICNTGWTIKNSRVVCGMMGFPSQRSVGKKPNSLKSAYRIHSVTCSGNEAHLSACTMEFSRANSSAPCPGGGAAVVSCVPGLQFTQGRVRKAKLNPVPQMRLKGGARAGEGRVEVLKGSEWGTVCDD... | 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 prerequis... |
B8A4W9 | MELHQWCRHIIVFLLNVWIPSCFAQTTPPARSSPTPTPQTADNPDSLKFRLSGFPRKHNEGRIEVFYKGEWGTICDDDFSLANAHVLCRQLGFVSATGWTHSAKYGKGAGKIWLDNVQCSGSERSVSVCKSRGWGNSDCTHDEDAGVICKDERLPGFVDSNVIEVQVDENRVEEVRLRPVFTTATKRMPVTEGVVEVKNKDGWAQICDIGWTPKNTHVVCGMMGFPHEKKVNKNFYKLYAERQKNFFLVHSVACLGTEVHLAACPLEFNYGNATESCPGGMPAVVSCVPGPLYTQSPTMKKKLKMPPTTRLKGGAKYGEG... | Cofactor: Contains 1 lysine tyrosylquinone.
Function: Protein-lysine 6-oxidase that mediates the oxidation of peptidyl lysine residues to allysine in target proteins (By similarity). Catalyzes the post-translational oxidative deamination of peptidyl lysine residues in precursors of elastin and different types of collag... |
Q9LNR3 | MALAKELMGYPLITERSSLVSSASHFKKRTQSTQFSINPFDRRPRKTKSGVVAAISEDLVKTLRFSTTTGDRKSEEEEKAAVKFKVRAVVTVRNKNKEDLKETLVKHLDAFADKIGRNIVLELISTQLDPKTKLPKKSNAAVLKDWSKKSKTKAERVHYTAEFTVDAAFGSPGAITVMNKHQKEFFLESITIEGFALGPVHFPCNSWVQSQKDHPDKRIFFTNQPYLPNETPSGLRVLREKELKNLRGDGSGVRKLSDRIYDFDVYNDLGNPDKSSELSRPKLGGKEVPYPRRCRTGRQSTVSDKDAESRVEKPLPMYVP... | Cofactor: Binds 1 Fe cation per subunit.
Function: 13S-lipoxygenase that can use linolenic acid as substrates. Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyzes the hydroperoxidatio... |
Q9LUW0 | MIHTDIAEILCVKPKTTKKTKTMEEDVKKTTTMKIEGEVVVMKKNLLDFKDVMASLLDRVNELLGRRVSLHLISSHQPDPANEKRGRLGKAAHLEKWVTKIKTSVTAEETAFGVTFDWDESMGPPAAFVIKNHHHSQFYLKSLTLRGFPDGEGGATAIHFICNSWIYPNHRYRSDRVFFSNKAYLPSETPELIKELREEELKNLRGNEKGGEFKEWDRVYDYAYYNDLGAPDKGPDSVRPVLGGSPELPYPRRGKTGRKSTKSDPKSESRLALLNLNIYVPRDERFSHVKFSDFLAYALKSVTQVLVPEIASVCDKTINE... | Cofactor: Binds 1 Fe cation per subunit.
Function: 9S-lipoxygenase that can use linoleic acid or linolenic acid as substrates. Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyzes the ... |
P09917 | MPSYTVTVATGSQWFAGTDDYIYLSLVGSAGCSEKHLLDKPFYNDFERGAVDSYDVTVDEELGEIQLVRIEKRKYWLNDDWYLKYITLKTPHGDYIEFPCYRWITGDVEVVLRDGRAKLARDDQIHILKQHRRKELETRQKQYRWMEWNPGFPLSIDAKCHKDLPRDIQFDSEKGVDFVLNYSKAMENLFINRFMHMFQSSWNDFADFEKIFVKISNTISERVMNHWQEDLMFGYQFLNGCNPVLIRRCTELPEKLPVTTEMVECSLERQLSLEQEVQQGNIFIVDFELLDGIDANKTDPCTLQFLAAPICLLYKNLANK... | Cofactor: Binds 1 Fe cation per subunit.
Function: Catalyzes the oxygenation of arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) to 5-hydroperoxyeicosatetraenoate (5-HPETE) followed by the dehydration to 5,6- epoxyeicosatetraenoate (Leukotriene A4/LTA4), the first two steps in the biosynthesis of leukotrienes, which ar... |
Q7XV13 | MRGGAGMCFASMEAAGSRGMGKGASRRRTARSTAPVGALVERVVVAPAPVEQQRGAGRPEAHPQSVAARAVVTVRRRRKEDAKDRFAEQLDALADRVGRSVLLELVSTETDPRKGTPKKSKPSALVGWFDKKDVKAERVVYTAEFAVDAGFGEPGAVTVLNRHQREFYIESIVVEGFPTGPAHFTCNSWVQPTRVSRDRRVFFSNRPYLPSETPPGLRELRLRELADLRGDGTGERRITDRVYDYDVYNDLGNPDKGVASARPVLGGEQMPYPRRMRTGRPSTATDASAESRVEYPEPIYVSRDEEFEEGKNEMLSEGAI... | 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. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-p... |
Q9CAG3 | MFVASPVKTNFNGVSLVKSPAFSALSCRKQHRVPISRQVRAVISREEKAVDQEDGKKSTNKPLINSSQFPWQRSKYTGSKTVTAVVKIRKKIKEKLTERFEHQLELFMKAIGQGMLIQLVSEEIDPETGKGRKSLESPVMGLPKAVKDPRYLVFTADFTVPINFGKPGAILVTNLLSTEICLSEIIIEDSTDTILFPANTWIHSKNDNPQARIIFRSQPCLPSETPDGIKELREKDLVSVRGDGKGERKPHERIYDYDVYNDLGDPRKTERVRPVLGVPETPYPRRCRTGRPLVSKDPPCESRGKEKEEFYVPRDEVFEE... | Cofactor: Binds 1 Fe cation per subunit.
Function: Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure (B... |
Q8H016 | MELTGLTRAAAAATVTPPAPRRGWGELRFAPLLPGERHGRRKVVVAAISEEVPRLAASPSSGIKGGGAGERRPAPEKVALRAALTVRRKQKEDIKEAVAGHLDALWDMVGRNVVLELISTKIHPRTKKPMQSGRVSIKDWCQKRGAKGDHVVYTAEFTVDADFGEPGAIAVANRHNREFFLESIVVEGGGLPCGPVHFACNSWVQSTRELPTKRVFFSNKPYLPSETPPGLRELREKELKDLRGDGTGVRKLSDRIYDYATYNDLGNPDKGKEFIRPILGGEKIPYPRRCRTGRPPTDTNMLAESRVEKPHPIYVPRDEA... | 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. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-p... |
O53505 | MARTRRRGMLAIAMLLMLVPLATGCLRVRASITISPDDLVSGEIIAAAKPKNSKDTGPALDGDVPFSQKVAVSNYDSDGYVGSQAVFSDLTFAELPQLANMNSDAAGVNLSLRRNGNIVILEGRADLTSVSDPDADVELTVAFPAAVTSTNGDRIEPEVVQWKLKPGVVSTMSAQARYTDPNTRSFTGAGIWLGIAAFAAAGVVAVLAWIDRDRSPRLTASGDPPTS | Function: A putative lipoprotein that seems to be specialized for the initial steps of macrophage infection . A non-acylated fragment (residues 26-185) binds phosphatidyl-myo-inositol mannosides (PIMs) . Limits, in a TLR2-dependent fashion, bacterial uptake by host (mouse); this effect may be mediated by nonacylated fr... |
P31554 | MKKRIPTLLATMIATALYSQQGLAADLASQCMLGVPSYDRPLVQGDTNDLPVTINADHAKGDYPDDAVFTGSVDIMQGNSRLQADEVQLHQKEAPGQPEPVRTVDALGNVHYDDNQVILKGPKGWANLNTKDTNVWEGDYQMVGRQGRGKADLMKQRGENRYTILDNGSFTSCLPGSDTWSVVGSEIIHDREEQVAEIWNARFKVGPVPIFYSPYLQLPVGDKRRSGFLIPNAKYTTTNYFEFYLPYYWNIAPNMDATITPHYMHRRGNIMWENEFRYLSQAGAGLMELDYLPSDKVYEDEHPNDDSSRRWLFYWNHSGV... | Function: Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Contributes to n-hexane resistance.
PTM: Contains two intramolecular disulfide bonds. At least one disulfide bond is required for activity, and protein is probably fully oxidized in vivo.
Sequence... |
Q8UFL3 | MSTIAASAKIHPTAVVEDGAVIGENVVIGALAYVGPKVTLHDDVRLHNHAVVSGLTVIGRGSVVHPMAVIGGTPQAVRHDGSETTLEIGERCIMREGVTMNAGSSDGGGKTIVGDDNLFLANSHVAHDCRLGRHIILSNNVMLAGHVTIEDRAILGGGCAVHQFTRIGRQAFIGGLSAVNYDVIPYGMLNGNPGILGGLNVVGMTRSGIERADIHKVRRVYKAIFEAEGTIRGNAAAIDRNDYLDCPQALEIIDFIGAGSDRAISSPNRGK | 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 (... |
B2ULY0 | MPEIHPTAVVHPAAEIADDVKIGPFCVVGEHVKLGPGCVLHSHVVIDGPSSFGSGNEFFPFSVIGLKSQDLKYKGEPTYLEVGDNNVFRENATINRATDIGGATRIGNNNLFLVSCHAGHDCQIGNHVIFSGFATAAGHVTVGDYAILAGCCAVHQFVSIGEHAMVGAMARVSQDVLPYTIVEGHPAVTRSVNSIGMQRRGFSEEDLKAVRMCYKKLFVNKKLTVHEALEELRHSGYAENACLRRIIQFVETSERGFCH | 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 (... |
Q0A7J1 | MTRIDPKAVVDPSAELDEGVTVGPFTVIGPDVQVGAGTRVGPHVVINGPTRLGRNNRIHPFASIGDDPQDKKYAGEPTRLEIGDDNVIREYVTLNRGTPEAGGLTRLGDRNWIMAYSHVAHDCRLGNDITFANSASLAGHVDVEDHAILGGFALVHQFCRIGAYAFCGFGSVINRDVLPFTTVSGHMAQPHGINVVGLRRHGMGPERIRELKRAYRLIFKSGKRLDDALEELRLLGKENPDLEHLAAFIAASNRGILR | 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 (... |
Q46481 | MRIHPTAIVEDGAQLHDSVTVGPYSIIESGAVIGEGCRIESNVRIFGVTRMGAHNRVCHGATLGSEPQDLSFTPEKARPLIIGDHNHFKECVNISGGIKSEGGTRIGSHNYWMAFSHAGHDCVVGDHNVFANTATLAGHVEIDDHCFLSGQVAVHQFCRIGSYVMIAGVTGVPQDVPPYMLADGHRARLIGLNVVGLRRNGFGQEQRTRIKQVYRLILRSGLRLDDALQRAEDEYPGPETKRIVAFIRASRRGIVSFG | 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 (... |
A7H9D6 | MAIHPTAVVEPGAQVDPSAEIGALAVVGPHVRVGPRTVVGPHAVLAGRTTLGEGNRIFPHAVVGEVPQDLKYRGEPTELVVGDRNTFREGVTISTGTVQGGGVTRIGSGCLFMANSHVGHDCVIGDGAIIANSVALAGHVELEDHVHFSGLAAAHQFCRIGRLAFVSGLTGVTMDVPPFCTVAGPRAELAGLNAVGMQRAGLSEERIGRVKQAYKIVFRSNLGLAEAIAQVEAELGMHEDVAHFVRFLKGTQRGITR | 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 (... |
O66862 | MKVHSSVLIEGEVEIPEDVEIGAYTVIQGNVKIGKGTKIGNRVTIKGNVTIGENCKIFDGAVIGEAPQHLKYEGEETSVEIGNNVIIREYVTIHRGTKLDKGKTVVGDNVMLMAYSHVAHDCVVGNNVIMANCATLGGHVVVGDYALIGGLSAVHQWARVGEHAMVGGLTGVSLDIPPYTVASGQHAKLYGINIIGLRRRGFPEEVIKAISKAYRIIFRSPLPRQKAPEIVFQELGQYEEVRKMVEFIKSSKRGVARHHKD | 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 (... |
Q9SU91 | MISLLKAREKLLSPLVSSTIRRLSSSLSYSREDSRDSEVLIHPSAVVHPNAVIGKGVSVGPYCTIGSSVKLGNGCKLYPSSHVFGNTELGESCVLMTGAVVGDELPGYTFIGCNNIIGHHAVVGVKCQDLKYKHGDECFLCIGNNNEIREFCSIHRSSKPSDKTVIGDNNLIMGSCHIAHDCKIGDRNIFANNTLLAGHVVVEDNTHTAGASVVHQFCHIGSFAFIGGGSVVSQDVPKYMMVAGERAELRGLNLEGLRRNGFTMSEMKSLRAAYRKIFMSTETVSLSFEERLTELEQDQELYSVPAVSAMLQSIRDSFTE... | 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 t... |
A8I491 | MNVALIDPTARVADGAWLADDVEVGPYCIVGPDVTLEDGVRLHAHVNVQGVTTLGARTQVYPFASLGTPPQSVHYKGEKTSLVVGTDCQIREHVTMNTGTASGRGVTRVGNNCMLMTAAHVAHDCLVGDNVIFANNATLGGHVEVGDNVFLGGLSAVHQFVRIGAQVMIGGVTGVREDVIPFGYAIGQNANLVGLNVVGMKRRGFSKSELHAARAAYRDLFFGEGTFAERLAGLRERQDASPFIKALVSFVDAGGKRALCHPSRGVVAQED | 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 (... |
A8GUZ4 | MSNSNIHPTSIIAEGAKLGKNVKVGPYCIIGPEVILHDNVELKSHVVIEGITEIGESTVIYPFASIGQPPQILKYNNERSNTIIGSNNIIREYVTVQAGSQGGGMITRIGNNNLFMVGVHIGHDCKIGNNVVFANYVSLAGHIEVEDYVIIGGLSAVHQYARIGKHSMIGGLSPVGADVIPFGLASGKRAVLEGLNLVGMNRKGFDKAESLNALKIVQEIFLGEGNFADRIKQAQEKYKNNTIVMQIIDFLEHGSNRSFCSFEKTMSLRGELQSNLTKQPN | 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 (... |
Q92JQ9 | MSNSNIHTTAVIAEGAKLGKNVKIGPYCIIGPEVVLHDNVELKSHVVIEGITEIGENTVIYPFASIGQPPQILKYANERSSTIIGSNNTIREYVTVQAGSQRGGMMTRVGNNNLFMVGVHIGHDCKIGNNVVFANYVSLAGHIGVGDYTIIGGLSAVHQYARIGEYSMIGGLSPVGADVIPFGLVSSKRAVLEGLNLIGMNRKGFDKVKSLSALKAIEEIFSGEGNFAERIKQVAEKYNNNSIVIQIIDFLNQDSNRAFCRFEK | 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 (... |
Q9ZED5 | MSNSNIHTTAIIAEGAKFGKNVKVGPYCIIGPEVVLHDNVELKSHVVIDGITEIGENTVIYPFASIGQPPQILKYANERSSTIIGSNNTIREYVTVQAGSKSGGMITRVGNNNLFMVGVHIGHDCKIGNNLVFANYVSLAGHIKVGDYAIIGGLSAVHQYTRIGEYSMIGGLSPVGADVIPFGLVSSKRAVLEGLNLIGMNRKGFDKADSLTALNAVEEIFLGEGNFVDRIKQVAEKYKNNSIVTQIIDFLNQDSSRAFCHFKK | 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 (... |
A0L8R9 | MGRPLRIAIVTGEASGDLLAASLVSGLKKRFPRMQIYGIGGPRMKMLGLDSMADAQELSIIGVVEVLNRFPRIRTIFNALLKRLQSEPPDLLITVDLPDFSLRMARKAKQLGIPTVHYVSPQVWAWRSGRAKTIASYLDLLLCLFPFEPRYYANTGLEAHFVGHPLVQEAVPSYSRSEARKILGVSEAGQLVAIMPGSRRSEIQRLLETFLRTAERLWKRRTNLSFVLIQAETISDQQLYEVWPEALRDLPVIVRHGNAYNWLAASDALLVASGTATLEAALIGIPMVVAYKVNPLTYQIGKQLIKSKFISLPNLIAQSA... | 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... |
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