ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
Q9FY49 | MAPIDPHSFTDSSHPLTTHVALSLYLDFNTSIIHGSALLTLSSAFSGELSLDTRCISIAMVLDPLTLEPIPYSVSTTPDRIRGTEVVVVLSGQSSLLIVYSTSPSASALQWLSPLQTFSKLHPYVYTQCQAIHARSIFPCQDTPAARIRYDVVMNIPNSLSAVMSARHVRRRLAVPEEAKHLEAGSLGSSLWCGEDRVVEEFAMEQPIPPYLFAFAVGELGFREVGPRTRVYTESAAIEVLDAAALEFAGTEDMIKQGEKLFGDYEWERFDLLVLPPSFPYGGMENPRMVFLTPTVIKGDATGAQVVAHELAHSWTGNLITNINNEHFWLNEGFTTYAERRIVEVVQGADIATLNIGIGWRGLTDEMERFKDNLECTKLWNKQEGVDPDDVYSQVPYEKGFQFVLRIERQIGRTAFDEFLKKYIATFKFKSIDTNTFLEFLKANIPGIEKEINLQLWTEGVGIPEDAYEPVSTIYTKIISLAKEFKEGKMPSEDDVAEWNGQEWELYLENLPKSCEPSQVMALDKRYRLAESKDYEVKVSFLQLAVTSKCREYHGEVKKTLKEVGRMKYLRPLFTALAQSGGTEEKQLAKQVFAEARETYHPIAQGVVESILSKYI | 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 leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro).
Catalytic Activity: an epoxide + H2O = an ethanediol
Sequence Mass (Da): 69266
Sequence Length: 616
Subcellular Location: Cytoplasm
EC: 3.4.11.-
|
Q75B10 | MKLPAVLEERRAAATDRSTLSNYEDFAVRHTNLELEVAFDERQIRAEVCYDLEQTGKGVAEVHLDTSYVQLECILVDGKRVPWELRERQEPLGSQLVITPEGGLPARFQLTCRSVTTARSTAVQWLGGAQTAGKPYVYTQLESVHARSLVPCFDTPACKSPFTVRVRSPLRAVVAGQEQPGSGKDGVYVFEQPVPIPIYLLGLAAGDIACAPLGPRSNVYCEPALLEAAAGEFGGEIERFLDAAEELLPRYIWGNYNLLVCPSSYPYGGMEVAGTSFISPSVIAYDRSNNDLIVHEMAHSWSGNLITNANWGHFWLNEGWTVYLERRITGALHGEDTRQFSSLLGMAELEVAIRASNGASFALVEDVSESVNPDNVVSLAAYEKGSALLLHLERELGGTAAFDPFIKHYFGKFGGQSLTTWQFLDILFDFFADKREKLERIDWKTWLFAPGMPPKLTYSTSLADDVYDLAEQWLEKAVQLRLPEEFAAEFSGSVLAAFTTAQQILFLNTIIQGGVSPDNTFDWTQHPVAAAALLSVYADTLGKSRNQEIIYRRYNFQLTAGMEDAYPEITTWLGSTGRMKHVRPIYRRLASIDKALAASTFQEHREKYHPICRAAIQADLGLS | 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 leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro).
Catalytic Activity: an epoxide + H2O = an ethanediol
Sequence Mass (Da): 69174
Sequence Length: 623
Subcellular Location: Cytoplasm
EC: 3.4.11.-
|
Q59NB8 | MTRAIVESIKKRFHELDPCTNSNYSKFKVIHTDLTLTVSFESKTLDGTVVYDLKNLDNASEVILDTSALNIKSTKVNGKEVSFELKPVTPIYGAPLRIPINPNESEIQVEISFTTTDKCTAIQFIQGDTGPYVFSQCEAIHARSLFPCFDTPAVKSPYKFTGHSPAVVTMSGRAQPTDEPNTYHFDQPIPIPSYLVSITSGNLLKAPIGPRSDVYSEEPSLKKCQWEFEKDMENFIQIAEKIVFEYEWSRFDSLVLPSSFPYGGMEIPNMTQLTPTLISGDRTQTKVMAHELAHSWSGNLVTNSSWEHFWLNEGWTVYLERRIIGAIAAAEAKEEGRKDAEKYGEQVRHFNMINGWNELADTCETFDKRYTKLVLDLENGDPDDSFSRIPYEKGFFFLYHLETKLGGIKEFDPFIKYYFNKFKYQSLNTAQFVDTLYEFYEPKGKAEILDNIDWETWLFVSGLPEKPEFDVTLANQVYALVDKWVAYVKNGGELPGDETADFEGEQDMLFLETLTEKFKTLDVKPEIIRLFPEIYPKYGASKNGEIISRWNELLISYGKYSSQDKLVQSFASWLGTIGRMKYVRPGYLLLRKGISHEFALEVFKKYEHIYHPICRTMVKKDLS | 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 leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro).
Catalytic Activity: an epoxide + H2O = an ethanediol
Sequence Mass (Da): 71463
Sequence Length: 623
Subcellular Location: Cytoplasm
EC: 3.4.11.-
|
Q6FTM0 | MINRLIQRIVPFSRPLSTVKKTMLTPFLESKRPQQSPEYDYSTLSNYKSFQIKHTTLNFLLSFEKSTVSGDVVFDLTTLKEAVKHIDLDTSYLDVNEVLVDDKPVEFKIEERKQPLGSKLVIAAELEAERQFKLRVKFSTTKDCTALQWLTPQQTSGDKPYMFSQLEAIHARALFPCFDTPSYKSTFTANIESTLPVVFSGIATGSTPNGESTVYHFKQDIPIPAYLVGIASGDLVSASIGPRSKVYTEPHRLDDCVWEFSNDVEKFIKTAENLIFDYEWGTYDILVNVDSYPYGGMESPNMTFATPTLIAHDKTNIDVIAHELAHSWSGNLVTNCSWNHFWLNEGWTVYIERRIVGALHGEPTRHFSALIGWSDLENSINSMRNPEKFSTLVQNLNDGTDPDDAFSTVPYEKGFNLLFHLETVLGGPQEFDPFIRHYFKKFARQSLDTFQFLDTLFEFFENKREILENVDWETWLFKPGMPPKPQFITTMADNVFSLVNKWIVKAQELKTTEEFSKEFSESDLSEFNSNQVVLFLEELVAQNCVPVESKIEWSKYSVASESLLSIYKKQVTESQNAEVVFKNYKFQTTARIQPSYQQLANWLGTVGRMKFVRPGYRLLNAVDRDLAIATFEKLKDTYHPICKQLVKQDLEL | 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 leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro).
Catalytic Activity: an epoxide + H2O = an ethanediol
Sequence Mass (Da): 74823
Sequence Length: 652
Subcellular Location: Cytoplasm
EC: 3.4.11.-
|
Q2GY21 | MAPVRDPNTLSNYNEWRTKHTTADFKVDFTAKCLRGSVVLELESQTDKASKEIILDSSYVDVSAITLNSTPSQWEVRDRTGPSGSPVRVAVPNGAGKGEVVKLEIELATTDKCTALQWLTPAQTSNKKAPFMFSQCQAIHARSIFPCQDTPDVKSTYDFIIRSPHVVVASGVPVPGEPESVGEDKVYKFHQKVPIPSYLFAVASGDIASAKIGRCSSVATGPNELKASQWELEDDMDKFLDAAEKIVFPYQWGEYNVLVLPPSFPYGGMENPIFTFATPTIISGDRQNIDVIAHELAHSWSGNLVTSCSWEHFWLNEGWTVYLERRILASIHKNDSYFDFSAIIGWKHLEEAIEEFGKDHEYTKLSIKHDGIDPDDAFSSVPYEKGFHFIWSLDRLVGRENFDKFIPHYFSKWQNKSLDSFEFKDTFLEFFSAPEYSKLKDKISQIDWEGRFFNPGLPPKPEFDTTLVDGCFQLANKWKSKDFSPSPSDTSSWTGNQLLVFLNVVQDFEEPLTAEQSQNMGKIYALADSKNVELKAAYYQIAMKAKDTTSYPGVAELLGNVGRMKFVRTLFRTLNKVDRDLAVKTFQKNRDFYHPICRQLVEKDLGLGESK | 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 leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro).
Catalytic Activity: an epoxide + H2O = an ethanediol
Sequence Mass (Da): 69072
Sequence Length: 611
Subcellular Location: Cytoplasm
EC: 3.4.11.-
|
Q96L50 | MKLHCEVEVISRHLPALGLRNRGKGVRAVLSLCQQTSRSQPPVRAFLLISTLKDKRGTRYELRENIEQFFTKFVDEGKATVRLKEPPVDICLSKAISSSLKGFLSAMRLAHRGCNVDTPVSTLTPVKTSEFENFKTKMVITSKKDYPLSKNFPYSLEHLQTSYCGLVRVDMRMLCLKSLRKLDLSHNHIKKLPATIGDLIHLQELNLNDNHLESFSVALCHSTLQKSLRSLDLSKNKIKALPVQFCQLQELKNLKLDDNELIQFPCKIGQLINLRFLSAARNKLPFLPSEFRNLSLEYLDLFGNTFEQPKVLPVIKLQAPLTLLESSARTILHNRIPYGSHIIPFHLCQDLDTAKICVCGRFCLNSFIQGTTTMNLHSVAHTVVLVDNLGGTEAPIISYFCSLGCYVNSSDMLK | Function: Substrate recognition subunit of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins . ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction during S-phase (By similarity). May negatively regulate the 4-1BB-mediated signaling cascades which result in the activation of NK-kappaB and JNK1 .
Sequence Mass (Da): 46723
Sequence Length: 414
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
|
D3YY91 | MRLPCEVEVRSCHLPTLGLKSRGKGVRAVVSLCQAPGRNELQPEARAEPGGHACLLVSTMKDRQGTSYKLRENIEQLFTKFVDEGKATVRLKEPPVDICLSKANPGNLKTLLSAMRLAHRGCDVNTPLSTLKPVKTSEFEKYKTKMVITSKKDYPLSKNFPYFLEHLQASYCSLARVDMRMLCLKNLTKLDLSHNCIKKLPATIGDLTHLQELNLNDNQLETFSVPLCTSTLQKSLHSLDLSKNKIKALPVQFCQFRELTNLNLNDNELIHLPFKIGQLTNLRFLSAARNKLRNLPSEFKMLSLEYLDLFGNTFEKPEVIPIIKLQVPLTLLESCEQAVLFYRIPYGPDIIPYHLCQDLDTAKTCVCGRFCLQSFIQGTTTMNLHSVAHTVVLVDSMGRTEAPVVSYFCSLTCFVKSSDMLN | Function: Substrate recognition subunit of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins . ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction during S-phase . May negatively regulate the 4-1BB-mediated signaling cascades which result in the activation of NK-kappaB and JNK1 (By similarity).
Sequence Mass (Da): 47514
Sequence Length: 422
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
|
Q5ZT84 | MQNNNPCGLDGFAFLEFSGPDRNKLHQQFSEMGFQAVAHHKNQDITLFKQGEIQFIVNAASHCQAEAHASTHGPGACAMGFKVKDAKAAFQHAIAHGGIAFQDAPHANHGLPAIQAIGGSVIYFVDEEHQPFSHEWNITSPEPVVGNGLTAIDHLTHNVYRGNMDKWASFYASIFNFQEIRFFNIKGKMTGLVSRALGSPCGKIKIPLNESKDDLSQIEEFLHEYHGEGIQHIALNTNDIYKTVNGLRKQGVKFLDVPDTYYEMINDRLPWHKEPLNQLHAEKILIDGEADPKDGLLLQIFTENIFGPVFFEIIQRKGNQGFGEGNFQALFEAIERDQVRRGTLKELS | Cofactor: Binds 1 Fe cation per subunit.
Function: Catalyzes the transformation of p-hydroxyphenylpyruvate into HGA. Has hemolytic and brown pigment production activity.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 38923
Sequence Length: 348
EC: 1.13.11.27
|
Q9H0V9 | MAATLGPLGSWQQWRRCLSARDGSRMLLLLLLLGSGQGPQQVGAGQTFEYLKREHSLSKPYQGVGTGSSSLWNLMGNAMVMTQYIRLTPDMQSKQGALWNRVPCFLRDWELQVHFKIHGQGKKNLHGDGLAIWYTKDRMQPGPVFGNMDKFVGLGVFVDTYPNEEKQQERVFPYISAMVNNGSLSYDHERDGRPTELGGCTAIVRNLHYDTFLVIRYVKRHLTIMMDIDGKHEWRDCIEVPGVRLPRGYYFGTSSITGDLSDNHDVISLKLFELTVERTPEEEKLHRDVFLPSVDNMKLPEMTAPLPPLSGLALFLIVFFSLVFSVFAIVIGIILYNKWQEQSRKRFY | Function: May be involved in the regulation of export from the endoplasmic reticulum of a subset of glycoproteins. May function as a regulator of ERGIC-53.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 39711
Sequence Length: 348
Subcellular Location: Endoplasmic reticulum membrane
|
P59481 | MAAASRPSWWQRWRRRAWARDGAKLLLFLLLLGSGPGPRHVRAGQAVEYLKREHSLSKPYQGVGTSSSSLWNLMGNAMVMTQYIRLTPDMQSKQGALWNRVPCFLKDWELQVHFKIHGQGKKNLHGDGLAIWYTKDRMQPGPVFGNMDKFVGLGVFVDTYPNEEKQHERVFPYISAMVNNGSLSYDHERDGRPTELGGCTAIVRNIRYDTFLVIRYVKRHLTIMMDIDGKHEWRDCIEMPGVRLPRGYYFGTSSITGDLSDNHDVISLKLFELTGVRTPEEEKLHRDVFLPSVDNLKLPEMTVPPTPLSGLALFLIVFFSLVFSVFAIVIGIILYNKWQDQSRKRFY | Function: May be involved in the regulation of export from the endoplasmic reticulum of a subset of glycoproteins. May function as a regulator of ERGIC-53 (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 39881
Sequence Length: 347
Subcellular Location: Endoplasmic reticulum membrane
|
P49257 | MAGSRQRGLRARVRPLFCALLLSLGRFVRGDGVGGDPAVALPHRRFEYKYSFKGPHLVQSDGTVPFWAHAGNAIPSSDQIRVAPSLKSQRGSVWTKTKAAFENWEVEVTFRVTGRGRIGADGLAIWYAENQGLEGPVFGSADLWNGVGIFFDSFDNDGKKNNPAIVIIGNNGQIHYDHQNDGASQALASCQRDFRNKPYPVRAKITYYQNTLTVMINNGFTPDKNDYEFCAKVENMIIPAQGHFGISAATGGLADDHDVLSFLTFQLTEPGKEPPTPDKEISEKEKEKYQEEFEHFQQELDKKKEEFQKGHPDLQGQPAEEIFESVGDRELRQVFEGQNRIHLEIKQLNRQLDMILDEQRRYVSSLTEEISKRGAGMPGQHGQITQQELDTVVKTQHEILRQVNEMKNSMSETVRLVSGMQHPGSAGGVYETTQHFIDIKEHLHIVKRDIDNLVQRNMPSNEKPKCPELPPFPSCLSTVHFIIFVVVQTVLFIGYIMYRSQQEAAAKKFF | Function: Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins.
PTM: The N-terminal may be partly blocked.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 57549
Sequence Length: 510
Domain: The FF ER export motif at the C-terminus is not sufficient to support endoplasmic reticulum exit, and needs assistance of Gln-501 for proper recognition of COPII coat components.
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
|
P49256 | MAAEGWIWRWGWGRRCLGRPGLPGPGPGPATPLFLLLLLGPVVADITDGNSEHLKREHSLIKPYQGVGSSSMPLWDFQGSTILTSQYVRLTPDERSKEGSIWNHQPCFLKDWEMHVHFKVHGTGKKNLHGDGIALWYTRDRLVPGPVFGSKDNFHGLAIFLDTYPNDETTERVFPYISVMVNNGSLSYDHSKDGRWTELAGCTADFRNRDHDTFLAVRYSRGRLTVMTDLEDKNEWKNCIDITGVRLPTGYYFGASAGTGDLSDNHDIISMKLFQLMVEHTPDEENIDWTKIEPSVNFLKSPKDNVDDPTGNFRSGPLTGWRVFLLLLCALLGIIVCAVVGAVVFQKRQERNKRFY | Cofactor: Binds 2 calcium ions per subunit.
Function: Plays a role as an intracellular lectin in the early secretory pathway. Interacts with N-acetyl-D-galactosamine and high-mannose type glycans and may also bind to O-linked glycans. Involved in the transport and sorting of glycoproteins carrying high mannose-type glycans.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 40214
Sequence Length: 356
Subcellular Location: Golgi apparatus membrane
|
B8NWW2 | MTVTATERIVTVFGTGNQAGAVARALLADKTSQFKVRAISRHPDSASSRTLSALGVQVVKADGWNLEELTRAFADTWAAFVNTNSDDPLFLQKGDGPTEFDLGKNIIDSLVAAKVQHLVYSCFASSVEQTKGKLFIKPMEMKYQALKYARETGHFATTCGIYAAWYYEQFLDKATADVFGGFPTTPDEEGYITFRAPLWGDDEHPSFVSITHDFGDMVHGILLEPEQWDGKSVPAASDVMTFEQLAQTLQNATGRKSRYIPLPSWEDFGRGIPELDDHKLLFAFTQATGGRYFGDVPTETKTALRLKRRAAEAQGKSGNEANLLSMEEWFKTNFA | Function: NmrA-like family domain-containing oxidoreductase; part of the lnb gene cluster that mediates the biosynthesis of diastereomeric piperazines. Lna and lnb clusters encode sets of enzymes that produce overlapping sets of previously undescribed metabolites such as piperazinomycin-like metabolites or morpholine . The lna and lnb biosynthetic pathways appear to be part of a signaling network that controls the formation of sclerotia, a resilient overwintering structure . One primary function of the non-canonical nonribosomal peptide synthetases lnaA and lnbA consists in the reduction of L-tyrosine . The presence in the clusters of tailoring enzymes such as the oxidoreductases lnaB, lnbB, lnaE or lnbE, as well as of the cytochrome P450 monooxygenases lnaC, lnaD, or lnbC, might explain formation of various diastereomeric piperazines .
Sequence Mass (Da): 37067
Sequence Length: 335
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
|
B8NWW3 | MAARLLSSVSLTDVVLLLSSVWIAVHLVLAAYNVYLHPLRRYPGPKLAAASQLLNVYHVLKGDNCKWTAQLHEKYGTVVRIGPNELSYISPSANQTIFGGRPKEDKVFEKNPVAYLQGNGDISNIFFARFHDHNRLRKLMAPAFSETAVREQEATIQGYTNQLIAALRNRSGQAAYPDAKGVVNIIPWLHFILFDVLTRLSFGDPIGCLDRADYHPWVSVIFKAIIHSTYTQAAHRLAPYQWILKHFIPNDMTANYEAHLEFTRKQLDQRQQVKEEPVARADFSSFMLKGMSPDELFDNVNIVITAGGETTASTISSSLYYLVHNPSSYERLTKEIRDTFSAEGEITLAAVAALPYLKAVIQEAMRIHPPVPIGLFRVAPAAGAFIDGQWVPGNTWVSVANLAASRSPTYWRDPERFTPERWLGDAKYESDVREASAPFSIGTRNCIGLNLANANMRIILARLLWNFDFEAQPDNIDPHELDEYGIWETKPLNLKIKERVQTT | Function: Cytochrome P450 monooxygenase; part of the lnb gene cluster that mediates the biosynthesis of diastereomeric piperazines. Lna and lnb clusters encode sets of enzymes that produce overlapping sets of previously undescribed metabolites such as piperazinomycin-like metabolites or morpholine . The lna and lnb biosynthetic pathways appear to be part of a signaling network that controls the formation of sclerotia, a resilient overwintering structure . One primary function of the non-canonical nonribosomal peptide synthetases lnaA and lnbA consists in the reduction of L-tyrosine . The presence in the clusters of tailoring enzymes such as the oxidoreductases lnaB, lnbB, lnaE or lnbE, as well as of the cytochrome P450 monooxygenases lnaC, lnaD, or lnbC, might explain formation of various diastereomeric piperazines .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56609
Sequence Length: 503
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
|
B8NWW6 | MMSKLFTPLQVGFCQLKHRVIMAPLTRFRADDNNVPLPIAKEYYSQRASVPGTLIIAEATYISLAAGGYPNVPGIWSPEQIARWKEITDAVHAQGSYIFLQLWALGRVGDADTLKQDGFDLISSSAVPVDAGEPVPRAMTEEEIKQYIALYAQAARNAVMAGFDGVELHGGNGYLVDQFTQDTCNRRTDSWGGSIPNRSRFAVEVTRAMVQAIGSERVAVKLTPWNDQQGMKMKDMEQQFLHLITSLKELKLAYLHLTNPRVSVDEDVPLQGPPDGHPLEDNAGFVKAWGETSPVFLGGGYTPQSAKHTLDVDYPLNEIGAVFGRLFISNPDLPLRLRDGLPFTPYDRDSFYTPLSPIGYSDYPFSDQAVDLIPVRV | Function: NADP-dependent oxidoreductase; part of the lnb gene cluster that mediates the biosynthesis of diastereomeric piperazines. Lna and lnb clusters encode sets of enzymes that produce overlapping sets of previously undescribed metabolites such as piperazinomycin-like metabolites or morpholine . The lna and lnb biosynthetic pathways appear to be part of a signaling network that controls the formation of sclerotia, a resilient overwintering structure . One primary function of the non-canonical nonribosomal peptide synthetases lnaA and lnbA consists in the reduction of L-tyrosine . The presence in the clusters of tailoring enzymes such as the oxidoreductases lnaB, lnbB, lnaE or lnbE, as well as of the cytochrome P450 monooxygenases lnaC, lnaD, or lnbC, might explain formation of various diastereomeric piperazines .
Sequence Mass (Da): 41706
Sequence Length: 377
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
|
P30639 | MKKILPIIWLINLVSGSLSLEKKAPDLLGKVCAFGDFNADRNTDILVFANGTLTINYQETKLLDVLEASKFTPGTSFAISKPSLNADFVECSVGDFNGDSRLDVLVSIRDKDTEIYNHTLWTSEIEDEKEIFRPFHVAMLQQHAMAIDVSDDGWTDVLGFYPNGSMFCTGFNKEGKYNLLVNGCKHEFVAFPEKLNIYPGMPHLFVDLNSDLIADIVFMTKESDGSLFMSVWQKTKISWQFRDWVPKLTPAQYPFVGAPVVMDVDSDGELDILVPICREDECSHITQMASWSKTKLWGLVACDMQDYTVIKEPFSRVIFRVGEFSLDSFPDMVVIAQATRANTRPVIKVMDNAECTKCEKNGTRRFEIRAQENIQPKNMSLGVIKMGTFFDLLEDGSLDLLVEYEYGGQTRFGFIYCPDKGDTTFLKVQVFTGVCSDRCNPKSNEIGSSISMTGACASFSMTDGWGGSTQSVACQVPASSNRALYLPFLLYGLGRSPNFVDELNIAIPKYADRKEDWKHSLKQIVPNSRIIVLPPSDQYPHWTSRLYVTPSALIVQSLAVIALVCCMLLMVVVFLHYREKKEDRYERQQQSHRFHFDAM | Function: Probable cell adhesion protein involved in gonadal cell migration.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 67593
Sequence Length: 599
Subcellular Location: Apical cell membrane
|
Q9ZI86 | MRWISRPGWPGHLLALAAGALTPLALAPFDYWPLAILSIALLYLGLRGLPGKSALWRGWWYGFGAFGAGTSWIYVSIHDYGAASVPLASLLMLGFTAGVAFFFALPAWLWARCLRRDNAPLGDALAFAALWLALELFRSWFLTGFPWLYAGYSQLQGPLAGLVPVGGVWLSSFVIALSAALLVNLPRLFPHGASLLLGLVLLLGPWAAGLYLKGHAWTHSAGEPLRVVAIQGNIAQELKWDPNQVRAQLDLYRDLSLPQQDVDLIVWPETAVPILQDMASGYLGAMGQVADEKNAALITGVPVRERLADGKSRYFNGITVVGEGAGTYLKQKLVPFGEYVPLQDLLRGLIAFFDLPMSDFARGPADQPLLKAKGYQIAPYICYEVVYPEFAAALAAQSQVLLTVSNDTWFGTSIGPLQHLQMAQMRALESGRWMIRATNNGVTGLIDPYGRIVRQIPQFQQGILRGEVIPMQGLTPYLQYRVWPLAGLAGVLLLWALLGRQLRPQERRLFG | 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): 56017
Sequence Length: 511
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
Q8Y210 | MRALFSSPAADTAGQQEALAVPLARLRFAAPLAALLGVMHTLAFAPNRWWWLQILSLAGLAALVRQAPRLRDVAWVGYAFGLGWFLSGIWWLYISMHVYGDMPAWMAAAAVLLFSAYLALHPALAAWLWQRLARGRQLSGAASALVFGAAWLVSEWLRGTEWTGFPWLNGGYAHTDGPLAGYAPLVGVYGVVAIAATLAGLLCAAAERRLHWLAGLAGVAVLAAGWPLHTIAWTQPVGKPITVRLLQGNVPQDVKFQQTGIDHSLALYTKMVTEQPAQLVVTPETAFPILLQDMPQEIALAIRTYVDTTGSSVLFGAANADSAVDYTNSAFGVGPWFKGVYRYDKHHLVPFGEFIPFGFHWFVHMMNMPLGDFRRGLPVQPPMPVAGQRVAPNICYEDLFGEEIAASLRQAERPATMLANVTNLAWFGDTIALDQHLQISRMRALESGRPMLRATNTGATAVVRPDGSVQARLPVFTLGTLQADVQGMQGLTPFVRTGNAPALGAGVLVLLAALARRRRAGAA | 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): 56513
Sequence Length: 523
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
P58377 | MERLAGRIILLSGVSRTFVGFLAGLLAVLAQPPFGIFAAAFVSFPVLVWLIDGVAPDPGDGLLRRLMPPAAIGWSFGFGYFLGGLWWLGNALLVEADAFAWALPLTVVGLPAVLGLFYALAVVIARSLWSDGWGRIAALALGFGIAEWLRGFLFTGFPWNAIGYAAMPMPLMMQSASVVNLSTINMLAVFVFAAPALIWTGKGARAGLAIAAALFTAHVAFGFYRLAQPAPAPLQPEMTVRVVQPVIDQAKKLDDRERASIFEDHLSLTAAPVQDGAKRPDIVVWPETSIPFILTDNPDALARIADVLQDGQVLVAGAVRVEDAGAGLPPRYYNSVYVIDDRGQIVGAADKVHLVPFGEYLPFEDLLTSWGLSSVAASMPGGFSAASTRPVLTLPGGRRIYPMICYEAIFADEVDGNARLADALLNITNDAWFGDTPGPRQHFHQAQLRAVEAGTPMIRAANTGISAVVDARGVLVVVLGYNYRGVIDTILPGKLPTLTNIATRSQIFWLTTGILFLVAAISRLGFNIRKN | 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): 56822
Sequence Length: 531
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
Q7UGJ8 | MRWLSAASSAFAVVLWLSGPPFAIGPLVFIALVPLLAIAEVSPSSSWKRPLYAASLAYWLLSLQGLRYAHPLMFLPWIALSGYLAIYPVLFIALLRRLRLVDNCDVSQARRDRVPLCLVAAVVWVGLEWIRNYFFTGISVLMLGHALADMPMLIQIADLGGTYAVSFVIVCVNVAMFDALNRWVVQRTSSVSDSPMKSLVTAGGLLIATMVYGAMSMNAETEPTGKTIALLGDNELTVYEQDIVREQEIFATYGQMAIDAVAKSNTRIDAVVWPESMFSGGLPWMTTGADLVVPDFMQNPAAAPLQPEQLRFAVESKQNDFLDRANSIQRAMRASSTVPTEAPPAIIGGCGLVQYADRPSQYSGVVWVNATGNMSGTYSKNHLVLFGETIPLVHSLPWIRDIVPPGLGLDRGTQPERFDLDGISLMPNLCIETAVERIPVNHMHQLNSRANPKLPDAIVTLTNDVWFHDSAVVDHHLRCAQLVAVGCRRPILSAANGGPTVWIDSAGRVVERLAKGQSDVIYAQPRRDSRISLYVRIGSWPAGLMGAATLCGLAWMTFEWLMRRRKRSVIA | 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): 62647
Sequence Length: 571
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
Q9ZDG3 | MYKTKIICLLLGILSGLVFAPIFFIPALFTFSYLCYIVQKSQNWQVAAKFGYLFGFGHFLSGMYWISIGVSVYIADFWWAIPFALFGLPIILAFFISANCTLSFFAKNNKYYQLIFCLLWVLFEWIRSWILTGLPWNLIGYAFSFSEILIQPLSITGIYGLSFIVIYISTSAYPVFTKKFTQLKILLASSMLILTVMVIYGAVRVSTNPTNFTDIKVRLVQPSIPQTAKWDQEEFWHNLMLHINLSENLEPTDLIIWSEAALVVPDDIPQVKLKLLNMLNSTNAILITGGISDNKKHGDQFELYSAMYALDKNNNKLFEYHKSHLVPFGEYMPLKNILPFKKLTHGLIDYKEGDGGLVYIKKYHLKIKPLICYESIFPNFVRTNNEIVDVIINITNDAWYGKSSGPYQHFHISRSRAVENGLPMIRVANNGISAIVDPIGRIVKKLNLNEINYIQGLIPQKLTTPTIFSQFGNFAMLLSIVFIILIHYLLSLIFDE | 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): 56734
Sequence Length: 496
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
|
A0Q491 | MSKLKIDTKRRFSLLIALVLIISLSSCATTQTNVTAITTKTVFNQETTYHNLLKLKKWQANGVIGIIYDNQAESANYTYLQDGDNFSIKLYGPLGIGSIEIKGDTNSVSLANSKGQKLTAKDAKTLMLEQLGWYVPVEGLKYWIKAIAIPNIRQTSELNTNNLLSKLSQNGWSISYSNYQLVDSKYPLPTKIRMSRDNLTLKIVIKSWQI | 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): 23598
Sequence Length: 210
Subcellular Location: Cell outer membrane
|
Q7VL53 | MKKSTLLFSLMAMALSGCNSVLNAPIEVKKLVYQIEHTDPAWQQHLKQLAEIKNYEVKGQFGYISPTERFSAHFDWQYKTPIDFTLALSSNLSTKLLKLQRSHQGLTVSDSEGYSRTEADIHALMQEIIGVSFPIDQFAYWVKGQPAQEGNYIVNEKRQLSQFSYPINQQIWQARYVEYHENRVPYLPKLIVLENGQQTLKIRLDHWNY | 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): 24328
Sequence Length: 209
Subcellular Location: Cell outer membrane
|
P45270 | MNNMKTFKFFTALFATAILTACTLDMERPTNVQYIDKTDAIWQQHLQKIQKIQSYQAKGQIGYISPTERFSSRFEWQYQNPKSYTLKLYSLISKSTLWIQMHQSGMTISDNNGNQQSAANSKLLLQEIIGMDVPLEHLAYWLKGQPAMNADYQVGTNHLLGAFTYHVDGSQWTADYLTYHSNNSMPENILLKNDSTKQTLKIRVDEWIY | 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): 24193
Sequence Length: 209
Subcellular Location: Cell outer membrane
|
A1WVQ5 | MTGRWSPRLLAGLLAALVLSGCALLVPEDEREAQYEAFLEERAELRDWSVAGRAALRAEGEAVSLSLRWEQRGEVYTINLSGPFGAGAVRIEGQPGRVTLRDGAGQSATAQSPEELLAAQTGHQLPVTALRDWIVGRPADGLEVDELSLDRVGRPDRLEQAGWRVDFQGWTDVDGVDLPSRVDLTRGSTQMRVALSGWSRSDD | 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): 22106
Sequence Length: 203
Subcellular Location: Cell outer membrane
|
C4K7Y9 | MLIFKICFYRLLPLSVLLLAACSALKAPESSSVLKNHIASDEWQEYQHQLKQIQQFQIQGSVAYFSDEKKAYARFFWQQYSPKNYHLLLLSPLGQTEFELKVTNGRVDMAKYKDQGEIKGDAEEILFKLTGIPIPLEHLSRWIVGASSDADEIILNRQSRLKTLIHHKKEQTWKVYYQAYNTKITPILPERLELYLISPNHQDQRMTLKINHWILK | 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): 25333
Sequence Length: 216
Subcellular Location: Cell outer membrane
|
O66646 | MAEILRAENIKKVIRGYEILKGISLSVKKGEFVSIIGASGSGKSTLLYILGLLDAPTEGKVFLEGKEVDYTNEKELSLLRNRKLGFVFQFHYLIPELTALENVIVPMLKMGKPKKEAKERGEYLLSELGLGDKLSRKPYELSGGEQQRVAIARALANEPILLFADEPTGNLDSANTKRVMDIFLKINEGGTSIVMVTHERELAELTHRTLEMKDGKVVGEITRV | 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): 24887
Sequence Length: 224
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
|
Q5NZT6 | MSEATNEPVLACEGLSKTFREGADALQVLDGVTLAVARGERIAIVGASGSGKSTLLHLLGGLDVPSAGAVRLHGRDFSRMSDAERGRVRNEALGFVYQFHHLLPEFSALENVAMPLYIRRMEREAANERAVAMLKEVGLGHRLDHAPGELSGGERQRAAIARALVTQPACVLADEPTGNLDRRTAQSVFDLMLSLNERLATSFIIVTHDEQLAGRAQRTLRLDDGRLA | 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): 24674
Sequence Length: 228
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
|
Q5LI72 | MIHLEGITKSFGSLQVLKGIDLEITQGEVVSIVGPSGAGKTTLLQIMGTLDSPDAGMINIDGTNVSRMKEKELSAFRNKHIGFVFQFHQLLPEFTALENVMIPAFIAGVPTKEASMRAMEILDFMGLKERASHKPNELSGGEKQRVAVARALINQPAVILADEPSGSLDSHNKEELHQLFFDLRNRFGQTFVIVTHDEALAKITDRTIHMVDGNII | 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): 23718
Sequence Length: 216
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
|
Q8A1M1 | MIKLEGITKSFGSLQVLKGIDLEINKGEIVSIVGPSGAGKTTLLQIMGTLDEPDAGTVAIDGTVVSRMKEKELSAFRNKNIGFVFQFHQLLPEFTALENVMIPAFIAGVSSKEANERAMEILAFMGLTDRASHKPNELSGGEKQRVAVARALINHPAVILADEPSGSLDTHNKEDLHQLFFDLRDRLGQTFVIVTHDEGLAKITDRTVHMVDGTIKKD | 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): 23762
Sequence Length: 218
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
|
Q6MMY0 | MRAVDIHKSYSQGVGELEILRGVSLDIREGEAFAILGASGAGKSTLLQIMGTLDRPNKGELYCEGRDLLAMSDDELSRFRNSEMGFVFQFHHLLSEFNALENVMIPCRVGGESIKVAKEKALHLLEFMGLADRRDHHPNQLSGGELQRVAIARALVRHPKILFADEPTGNLDSHTSGKIQELFFRLKEEMKLALVIVTHDLTFATRFPKVYRMKDGQWQS | 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): 24735
Sequence Length: 220
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
|
Q492R2 | MANIPLLQCIQLTKYYQRANFLIKVLNCITLSIQSNEMIAVVGASGSGKSTLLHLLGGLDKPTEGEIFFEGHALHKLTDNERSVIRNKRLGFVYQFHHLLSDFDVLENVAMPLLIGGIAFNQAKSRAQCVLELVGLKNHINSFPHELSGGESQRVTVARAIVNNPSLILADEPTGNLDQKNSDSIFQLLKKLNTYYGTTFLIATHDLDFAKKCHKILMISNGKIKLSQNDSFR | 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): 25907
Sequence Length: 233
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
|
Q89KN0 | MEQQQGAEDVPVIYLHEIKRQYLQGEVPLTILDGAKLALWAGQSVALVAPSGSGKSTLLHIAGLLEAPDSGEVYVNGAPTSQLPDIERTQLRRTDIGFVYQSHRLLPEFSALENVMLPQMIRGLKKSESVKRAKEILGYLGLGDRITHRPAELSGGEQQRVAIARAVANAPRVLFADEPTGNLDPHTADHVFQALMQLVKATRVSMLIATHNMELAGRMDRRVSLSDGQVVELE | 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): 25602
Sequence Length: 234
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
|
P57383 | MNNIIIKCINLNKSYKDGDFTYTILKNISFQLNKGDIAGIIGKSGSGKTTFLHLLAGLENPTSGDILFNGRLFSSMSSNKMSKFRNIELGFIYQFHHLMLDFNILENVSMPLLISNKSKKDSEEIAYNMLKKFNLEDKIKKYPSELSGGERQRVAVARAFINKPSLIIADEPTGNLDEDNTNIIFNLITELNSDYNTSFIIATHDPTLIKKIPVLFKIENNQIFNYES | Function: Usually LolD forms an ABC transporter complex with LolC and LolE involved in the translocation of lipoprotein, in an ATP-dependent manner. However, LolE is certainly not functional as it is frameshifted.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25829
Sequence Length: 228
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
|
Q72JM6 | MLPETMPVCPVRGSVIYPTMVMPIDAGRPISIRAIDEALARDRVLLIVSQRDKEVETPRPSDLFEVGTACNILKMRKNPDGSVQVLVQAFARVRVREWLDLGDHLEARGEVLADEPGEPILVKALVREVKDKFQALLKEGKYLAPEVAQFILNLEDPSQLADYVAFHMDFRLEDKQKVLETANVAERLRAVLVLLEAELALIETQRRIQQQVKEEIDRNQREYFLREQMKAIQRELHGEEGEQEVEEFRRKLEALDLPPVVRQEVERELNRFARMHPDSAEASVIRTYLDWIVNLPWNTRTEDNLDLERAKEILERDHYGLEKVKDRVLEYLAVRKLKAERAKRGEIPPDEVNKGPILLFVGPPGVGKTSIAKSIAEALGRKYVRVSLGGVRDESDIRGHRRTYIGAMPGRIIQGLRQAGTKNPVFLLDEVDKLGISYQGDPAAALLEVLDPAQNKEFVDHYLGVPFDLSEVMFICTANFPQNIPAPLYDRMEPIEFTSYTEQEKLEIAKRYLLPRQLKENGLEPEQVVVTEAALTRLITHYTREAGVRQLEREIGALLRKAARRILEEGKKRVRITEKDLEAYLGPPRFLPETEAREPQVGVATGMYYTPVGGDIMFVEVSVMPGKGNLILTGQLGDVMKESARAALSYAKKNALRFGIPLEKFDKSDIHIHVPAGAIPKEGPSAGVALVSALVSALTEVPVRHDIAMTGEITLTGRVLPIGGVKEKVLGARRAGIREVILPKLNEPDLADIPKPLRQNMTFHFVEHLDQVLDLALVGGLKALEERGRRSRSARRKKELVAHA | 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): 90513
Sequence Length: 804
Subcellular Location: Cytoplasm
EC: 3.4.21.53
|
A9GIS9 | MFFKNDSDRGKNAPERGIVPLLPLRDIIVFPHMVSQLFVGRERSIAALDEAMNRGKEIFLAAQRNAKTNDPTPDDIFGVGSVGAIMQLLRLPDGTVKVLIEGKRRARIRRYVQSDAYFLIEYDEIVESSVASVEVEALMRSVQSTFEMYVKLNKKIQPEVLMAVQAIDEASRLADTIIANLPTIKLTDRQALLEMEEPQKRLERLIELMQAEIEILQVEKKIRSRVKKQMEKTQKEYYLNEQMQAIQKELGGGERDEFKNEIQEIEEALKTKRMSKEAAAKVKKELKKLKMMHPTSAEATVVRNYIDWILELPWYDKSEERYDLVEAERILDEDHYGLKKIKERILEYLAVQALTKKLKGPVLCFVGPPGVGKTSLAKSIARATGRKFVRLSLGGVRDEAEIRGHRRTYIGALPGKLIQSLKKVGTNNPVFLLDEVDKMSTDFRGDPAAALLEVLDPEQNHTFNDHYLDLDYDLSDVMFITTANTLSGIPVPLQDRMEVIQLSGYTEFEKLNIAVKYLVPRQRKECGLEDVSLDFTEGALRTIIHHYTKESGVRSLEREIASVCRKVARRVVSDGKEKPIEVVAKSIPKYLGVPKYRLGRREERDEVGLVNGLAVTNVGGDLLPAEATVVPGKGKLVITGLLEKGMEESGHAAMSYVRSRLDRLGLEADVYQKVDVHIHFPDFVRKDGPSAGVTMVTALVSSLMKVPVRRDLAMTGEITLRGRVMPIGGLKEKLLAAHRGGIATVILPKENRKDLRDVPRRVLKALRLVLVEHVDDVLREALILPDAYAIFGPPKGVLEYRDGELVTEAAPVKAPPAAAGEPTPAAPPGA | 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): 92887
Sequence Length: 830
Subcellular Location: Cytoplasm
EC: 3.4.21.53
|
A9F8L0 | MSQLRSGASAPRSPFPLLPLRTGVLFPGTVLTLPVGRPRSVALLNAVHAGDVIGVIAQRDPKREDPRREDLHDIGTFARVVDISRVSNGYRLVIEGLDRFALSALVETEPTWRAEGTLAPEFLGDAEEARLLAASLRERAREVGPKTGTNLAEIAATSRAEPGVFADQVAGALGLPTEKEMEVLSELRVVPRLQRVAGLLAEASALADLKKKIDGDVRRELGKGQREVILREQLRAIQKELAGGEEGEDELSALRRRLDEAGLPEEARAVADRELRRLESVGPQSAEHNVIRTYLEWIADLPWSARAEVKDDLDAVKAKLDEEHRGLDDVKRRILEHMAVLKLTGKARATILCFAGPPGVGKTSLGQSIADATGRPFVRISLGGVHDEAELRGHRRTYVGALPGRIVHALKKAKVKNPIVLLDEVDKLGAGWRGSPEAALLEVLDPEQNRTFVDHYLELPFDLSEVVFLCTVNDLGALSAPLRDRLEVIELSGYTPDEKIAIARSHLVPKQLKEHAIDPGSLSITDEALAAIVRDYTREAGVRQLGREIKKLCRAVALEIARAADGKAPRVVVEASDLGTYLGKVRFFSDVAERTSVAGVATGLAWTPVGGDILFIETSRMPGKGRVEITGQLGDVMKESAKAALTYVRSHAIELGVDTAKLEAEDLHIHVPAGGVPKDGPSAGVTMFTALTSLLSARRVRSDTAMTGECTLRGRVLPVGGIKSKVLAAHRAGIKRVVLPQKNARDAEEIPKEVRAELELIFVEDMSQVIAAALEEAPIEAAGTGGVTGAAAGEPAAAA | 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): 85866
Sequence Length: 799
Subcellular Location: Cytoplasm
EC: 3.4.21.53
|
Q9HSC3 | MSNESTNDAPPDDDPDDPEPSVDHDDTDGLQDDPADSVDDAGEVDDLENLGSDVGVEGDVSIDEDNAEDDLLGGLRIDDTSDITVPDRLVDQVIGQEAAREIVKRAAKQHRHVMMIGSPGTGKSLLAKAMSRLLPKESLQDVLVYHNPDDSNEPKVRTVPAGKGEQIVDAHKEEARKRNQMRSFLMWIMILLAVGYALLIATPARPLLALLSAAGIYLLFRYTNRGSDAMVPKLLINNADRQVAPFEDATGAHAGAMLGDVRHDPFQSGGMATPSHERVEAGSIQKANKGVLFIDEINTLDVRSQQKLMTAIQEGEFSITGQSERSSGAMVQTEAVPCDFIMVAAGNMDAMENMHPALRSRIKGYGYEVYMDDTIEDTPDMRRKYARFVAQEVEKDGNLPHFAPDAIRELILEAKRRAGRKDSLTLKLRDLGGLVRVAGDIARSEGHDLTQRSDVLEAKKRSRSIEQQFVDNYIQRRKDYELGTTSEEAVGRVNGLAVMGGDSGIMLPVMAEITPAQSQEEGRIYATGQLKEMAEEAVENVSAIIKKFSDENMSEKDTHIQFVQAGEGGVDGDSASITVATAVISALEDIPVAQELAMTGSLSVRGDVLPVGGVTHKIEAAAKAGCERVIIPKANEDDVMIEDEYEEQIEIIPVTHISEVLDVALVGEPEKDSLVDRLKSITGKALDSASDSGTTGGNPSPQ | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76017
Sequence Length: 702
Subcellular Location: Cell membrane
EC: 3.4.21.-
|
Q58812 | MFSIKFKTTEELPEPSPRLIDQVIGQEEAVKIVLSAVKNKRNVILLGDPGVGKSMIVKAVGEILSDFGEFTPYYVIAKPNLKNMERPIVEVIDGEYKEDSKDMPKLDFKAPSSTTLLLIMIGAILLSEYLLKYLPQNYLLAAVTITALIVLIFGFVIILTSIMGASRASMPNNLNPMDLKPVLLYECKKRPLVRASAYNVTRLLGDIKHCPLGGRPPLGTPPHKRIILGAIHEAHRGILYVDEIKTMPLEVQDYILTALQDKQLPISGRNPNSSGATVETNPIPCDFILIMSGNMDDVYNLRAPLLDRIDYKIVLKNKMDNTLENRDKLLQFIVQEIKNNNLNPMTYDGCCEVVRIAQYLAGSKDKLTLRLRLLANIIKMANDVAMGKDVEELLGNFDDKGEYHPETQKDKSNKVYITAEHVRKVFDTGIYSMEKQVALNYIKNFKRYKHIVPNDEPKVGVIYGLAVLGAGGIGDVTKIIVQILESKNPGTHLLNISGDIAKHSITLASALSKKLVAEKKLPLPKKDIDLNNKEIYIQFSQSYSKIDGDSATAAVCLAIISALLDIPLKQDFAITGSLDLSGNVLAIGGVNEKIEAAKRYGFKRVIIPEANMIDVIETEGIEIIPVKTLDEIVPLVFDLDNRGGAERFN | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71918
Sequence Length: 649
Subcellular Location: Cell membrane
EC: 3.4.21.-
|
O26878 | MKTTIKNSRTQESVSYEGNETKKGTGETLSYETSKDIEVPERLIDQIIGQEEAVETIKKAAEQRRNVLLIGEPGVGKSMLAKAMAELLPREQLQDILVYPNIEDPNNPLIGAVPAGEGRKIVMNHKNKARSQDEKKNLFMMLIISFILVLGFMMNQFLAAIIAAGIIFLALQQFRPRTTVMVPKLLVNNEGRQVAPFVDATGAHAGALLGDVRHDPYQSGGLGTPAHERVEAGMIHKANKGVLYIDEIGTMKMKTQQELLTAMQEKRYSITGQSETSSGAMVRSQAVPCDFVLVASGNLQVLEGMHPALRSRIRGYGYEVFMKDTMPDTPENRDKLVQFVAQEVEKDGRIPHFSREAVEEIIREAQRRAGKKDSLTLKLRELGGLVRAAGDIAKSRGAELVETEDVIEAKKLSRTLEQQIADRYIVQKKKYSVFKSEGGEVGRVNGLAIIGDRSGIILPIAAEAAPAQSKEEGRIIATGKLGEIAREAVQNVSALIKKYTGTDISNYDIHIQFLQAYDGVEGDSASVSVATAVISALEEIPVDQSVALTGSLSIRGDVLPVGGVTGKIEAAAEAGIRKVLIPASNMGDVMIEKKYEDMVEIVPVETLGDVLEHALIGKGKESLIQRMQKISDIVPSIMKKPAMH | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70212
Sequence Length: 644
Subcellular Location: Cell membrane
EC: 3.4.21.-
|
Q9UYC6 | MLKFYKMGIKRLSGEMTMGEERMDLGIEFETTEEIPVPERLIDQVIGQDHAVEVIKTAAKQRRHVLLIGEPGTGKSMLGQAMAELLPTEDLEDILVFPNPEDENMPRIKTVPAGQGRRIVEEYKRKAKEQENIRFYLLFFVFFIVAMAVFMSRGDPNTLLLGVFVILIALMVTANMRFRTQAMVPKLLVDNSGRKRAPFVDATGAHAGALLGDVRHDPFQCFSGEETVVIRENGEVKVLRLKDFVEKALEKPSGEGLDGDVKVVYHDFRNENVEVLTKDGFTKLLYANKRIGKQKLRRVVNLEKDYWFALTPDHKVYTTDGLKEAGEITEKDELISVPITVFDCEDEDLKKIGLLPLTSDDERLRKIATLMGILFNGGSIDEGLGVLTLKSERSVIEKFVITLKELFGKFEYEIIKEENTILKTRDPRIIKFLVGLGAPIEGKDLKMPWWVKLKPSLFLAFLEGFRAHIVEQLVDDPNKNLPFFQELSWYLGLFGIKADIKVEEVGDKHKIIFDAGRLDVDKQFIETWEDVEVTYNLTTEKGNLLANGLFVKNSGGLGTPAHLRVEPGMIHRAHKGVLFIDEIATLSLKMQQSLLTAMQEKKFPITGQSELSSGAMVRTEPVPCDFILVAAGNLDTIEKMHPALRSRIRGYGYEVYMRTTMPDTVENRRKLVQFVAQEVKKDGRIPHFTRDAVEEIIREAQRRAGRKGHLTLRLRDLGGVVRAAGDIAVRKGKKYVTREDVLEALQMAKPLEKQLADWYIERKKEYQVIRTEGGEIGRVNGLAIIGEQSGIVLPIEAIVAPAASKEEGKIIVTGKLGEIAREAVLNVSAIIKRYKGEDISRYDIHVQFLQTYEGVEGDSASISVATAVISALEEIPVRQDVAMTGSLSVRGEVLPVGGVTPKIEAAIEAGIKKVIIPKANEKDVFLSPDKREKIEIIPVERIDEVLEVALVESEKKKELIKRIRETLPLGVSESAGSETLHEHGRDSGSALSVEESKA | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).
PTM: This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 111704
Sequence Length: 998
Subcellular Location: Cell membrane
EC: 3.4.21.-
|
Q9HJ89 | MEENIESVEEWVNKLDIETTKDIHVPKLLFDQVIGQDQAGEIVKKAALQRRHVILIGEPGTGKSMLAQSMVDFLPKSELEDILVFPNPEDPNKPKIKTVPAGKGKEIVRQYQIKAEREKRDRSRSIMFVIFSVVLLGIIAAIVLRSITLIFFAIMAAAFLYMAMAFNPVIRNERAMVPKLLVSHNPNDKPPFVDSTGAHSGALLGDVRHDPFQSGGLETPAHERVEAGNIHKAHKGVLFIDEINLLRPEDQQAILTALQEKKYPISGQSERSAGAMVQTEPVPCDFVLVAAGNYDAIRNMHPALRSRIRGYGYEVVVNDYMDDNDENRRKLVQFIAQEVEKDKKIPHFDKSAIIEVIKEAQKRSGRRNKLTLRLRELGGLVRVAGDIAVSQKKTVVTAADVIAAKNLAKPLEQQIADRSIEIKKIYKTFRTEGSVVGMVNGLAVVGADTGMSEYTGVVLPIVAEVTPAEHKGAGNIIATGKLGDIAKEAVLNVSAVFKKLTGKDISNMDIHIQFVGTYEGVEGDSASVSIATAVISAIENIPVDQSVAMTGSLSVRGDVLPVGGVTAKVEAAIEAGLNKVIVPELNYSDIILDADHVNKIEIIPAKTIEDVLRVALVNSPEKEKLFDRISNLINAAKIIKPQRPATPATTRAGNNAA | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71601
Sequence Length: 657
Subcellular Location: Cell membrane
EC: 3.4.21.-
|
Q8NKS6 | MDEESTKERLIPREYGESLDLGIDFKTTEEIPVPEKLIDQVIGQEHAVEVIKTAANQRRHVLLIGEPGTGKSMLGQAMAELLPTENLEDILVFPNPEDENMPKIKTVPACQGRRIVENYRRKAKEQEGIKNYLLMFVIFTVILAIIMEPTATTLLMGMFVVLLSMMVLSNMRFRNTVLVPKLLVDNCGRKKAPFVDATGAHAGALLGDVRHDPFQSGGLGTPAHERVEPGMIHRAHKGVLFIDEIATLSLKMQQSLLTAMQEKKFPITGQSEMSSGAMVRTEPVPCDFILVAAGNLDTIDKMHPALRSRIRGYGYEVYMRTTMPDTIENRRKLVQFVAQEVKRDGKIPHFTREAVEEIVREAQKRAGRKGHLTLRLRDLGGIVRAAGDIAIKKGKKYVEREDVLEAMRMAKPLEKQLADWYIENKKEYQVIKTEGGEIGRVNGLAVIGEQSGIVLPIEAVVAPAASKEEGKIIVTGKLGEIAKEAVQNVSAIIKRYKGEDISRYDIHVQFLQTYEGVEGDSASISVATAVISALENIPIRQDVAMTGSLSVRGEVLPIGGATPKIEAAIEAGIKKVIIPKANEKDVFLSPDKAEKIEIYPVETIDQVLEIALQDGPEKDELLRRIREALPLYGSS | Cofactor: Mg(2+). Exhibits no peptide cleavage activity without Mg(2+), regardless of the presence or the absence of ATP. Can also use other divalent cations such as Ni(2+), Ca(2+), Mn(2+) and Co(2+).
Function: Serine protease that displays ATP-independent proteolytic activity towards peptides and unfolded proteins and ATP-dependent activity for the cleavage of folded proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70258
Sequence Length: 635
Domain: Possesses a two-domain structure consisting of an N-terminal ATPase domain belonging to the AAA(+) superfamily and a C-terminal protease domain. The ATPase domain likely acts as a molecular chaperone functioning in the unfolding of protein structures, along with ATP hydrolysis.
Subcellular Location: Cell membrane
EC: 3.4.21.-
|
Q9UN81 | MGKKQNRKTGNSKTQSASPPPKERSSSPATEQSWMENDFDELREEGFRRSNYSELREDIQTKGKEVENFEKNLEECITRITNTEKCLKELMELKTKARELREECRSLRSRCDQLEERVSAMEDEMNEMKREGKFREKRIKRNEQSLQEIWDYVKRPNLRLIGVPESDVENGTKLENTLQDIIQENFPNLARQANVQIQEIQRTPQRYSSRRATPRHIIVRFTKVEMKEKMLRAAREKGRVTLKGKPIRLTADLSAETLQARREWGPIFNILKEKNFQPRISYPAKLSFISEGEIKYFIDKQMLRDFVTTRPALKELLKEALNMERNNRYQPLQNHAKM | Function: Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. Functions as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded.
PTM: Polyubiquitinated, probably by UBR2, which induces its degradation.
Sequence Mass (Da): 40056
Sequence Length: 338
Domain: The coiled coil domain mediates homotrimerization.
Subcellular Location: Nucleus
|
P11260 | MAKGKRKNPTNRNQDHSPSSERSTPTPPSPGHPNTTENLDPDLKTFLMMMIEDIKKDFHKSLKDLQESTAKELQALKEKQENTAKQVMEMNKTILELKGEVDTIKKTQSEATLEIETLGKRSGTIDASISNRIQEMEERISGAEDSIENIDTTVKENTKCKRILTQNIQVIQDTMRRPNLRIIGIDENEDFQLKGPANIFNKIIEENFPNIKKEMPMIIQEAYRTPNRLDQKRNSSRHIIIRTTNALNKDRILKAVREKGQVTYKGRPIRITPDFSPETMKARRAWTDVIQTLREHKCQPRLLYPAKLSITIDGETKVFHDKTKFTQYLSTNPALQRIITEKKQYKDGNHALEQPRK | Function: Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. Functions as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded.
PTM: Polyubiquitinated, probably by UBR2, which induces its degradation.
Sequence Mass (Da): 41226
Sequence Length: 357
Domain: The coiled coil domain mediates homotrimerization.
Subcellular Location: Nucleus
|
P23490 | MSYQKKQPTPQPPVDCVKTSGGGGGGGGSGGGGCGFFGGGGSGGGSSGSGCGYSGGGGYSGGGCGGGSSGGGGGGGIGGCGGGSGGSVKYSGGGGSSGGGSGCFSSGGGGSGCFSSGGGGSSGGGSGCFSSGGGGSSGGGSGCFSSGGGGFSGQAVQCQSYGGVSSGGSSGGGSGCFSSGGGGGSVCGYSGGGSGCGGGSSGGSGSGYVSSQQVTQTSCAPQPSYGGGSSGGGGSGGSGCFSSGGGGGSSGCGGGSSGIGSGCIISGGGSVCGGGSSGGGGGGSSVGGSGSGKGVPICHQTQQKQAPTWPSK | Function: Major keratinocyte cell envelope protein.
PTM: Substrate of transglutaminases. Some glutamines and lysines are cross-linked to other loricrin molecules and to SPRRs proteins.
Sequence Mass (Da): 25761
Sequence Length: 312
Subcellular Location: Cytoplasm
|
A0A142ZC57 | MKYTDFLAHPDEIIPTIRMMYADYRLKNMEIKDPSVRFCYNMLNRVSRSFAMVIQQLPVELRDATCVFYLILRALDTVEDDMAIPKEVKIPMLRTFHEHLSDRSWKIKCGYGPYVDLMDNYPLVTDVYLRFDEGTKAVIKDITRRMGNGMADFIDLDEVLTIPQYDLYCHYVAGLCGIGMCKLFVDSGLEKEDLVAEEDLANQMGLFLQKNNIVRDYLEDINELPAPRMFWPKEIWGNYAKQLDEFKDPKNLDKAMLCLNHMVTDALRHCEVGLRSLSLLHNPNILRAVLIPQVMGVRTLTLVYNNPEVFRGVVKMRRGETAKIFVTTTSKLSFFRTYLQFANEMEQKCLTEAKNDPMVALTLKRVQGVQAACRAAIVKAEIAEGAKGPSTAMVLAGALLIAALAYFAYVYSAGGTSLKALPLFGVVIILAIGLFGRNLALKTV | Function: Converts the C20 geranylgeranyl diphosphate (GGPP) to the C40 lycopaoctaene, the first committed intermediate in the production of lycopadiene . Converts farnesyl diphosphate (FPP) into squalene, a precursor for sterol biosynthesis in eukaryotes . Converts with low efficiency the C20 phytyl diphosphate (PPP) to the C40 lycopadiene in vitro. This reaction may not have biological significance in vivo .
Catalytic Activity: 2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50278
Sequence Length: 444
Subcellular Location: Membrane
EC: 2.5.1.148
|
Q3ZC80 | MQANSSAKSLPTECPDYQPIHHLHLVVYSVVLAAGLPLNALALWVFLRALRVHSVVSVYMCNLAASDLLFTLSLPLRLSYYARHYWPFPDFLCQLAGAVFQMNMYGSCIFLTLINVDRYAAIVHPLRLRHLRRPRVARLLCLGVWALILVFAVPTILAHQPSSCARDGRNVSLCFESFSDKLWKGSLLPLLLLAEALGFLLPLAAVVYSSGRVFWTLARPDATRSQRRRKTVRLLLASLVIFLLCFVPYNATLAVYGLLRGEVVPASSEARKKVRGVLMVMVLLAGANCVLDPLVYYFSAEGFRNTLRGLRAPLRDRTLAANGAQEALAEPLTETAHASTLTTTSQGQLQPSDPRSSFTPSHEDSSF | Function: Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40639
Sequence Length: 367
Subcellular Location: Cell membrane
|
Q9H1C0 | MLANSSSTNSSVLPCPDYRPTHRLHLVVYSLVLAAGLPLNALALWVFLRALRVHSVVSVYMCNLAASDLLFTLSLPVRLSYYALHHWPFPDLLCQTTGAIFQMNMYGSCIFLMLINVDRYAAIVHPLRLRHLRRPRVARLLCLGVWALILVFAVPAARVHRPSRCRYRDLEVRLCFESFSDELWKGRLLPLVLLAEALGFLLPLAAVVYSSGRVFWTLARPDATQSQRRRKTVRLLLANLVIFLLCFVPYNSTLAVYGLLRSKLVAASVPARDRVRGVLMVMVLLAGANCVLDPLVYYFSAEGFRNTLRGLGTPHRARTSATNGTRAALAQSERSAVTTDATRPDAASQGLLRPSDSHSLSSFTQCPQDSAL | Function: Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41347
Sequence Length: 372
Subcellular Location: Cell membrane
|
P32250 | MVSSNCSTEDSFKYTLYGCVFSMVFVLGLIANCVAIYIFTFTLKVRNETTTYMLNLAISDLLFVFTLPFRIYYFVVRNWPFGDVLCKISVTLFYTNMYGSILFLTCISVDRFLAIVHPFRSKTLRTKRNARIVCVAVWITVLAGSTPASFFQSTNRQNNTEQRTCFENFPESTWKTYLSRIVIFIEIVGFFIPLILNVTCSTMVLRTLNKPLTLSRNKLSKKKVLKMIFVHLVIFCFCFVPYNITLILYSLMRTQTWINCSVVTAVRTMYPVTLCIAVSNCCFDPIVYYFTSDTNSELDKKQQVHQNT | Function: Binds to oleoyl-L-alpha-lysophosphatidic acid (LPA). Intracellular cAMP is involved in the receptor activation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35597
Sequence Length: 308
Subcellular Location: Cell membrane
|
P43657 | MVSVNSSHCFYNDSFKYTLYGCMFSMVFVLGLISNCVAIYIFICVLKVRNETTTYMINLAMSDLLFVFTLPFRIFYFTTRNWPFGDLLCKISVMLFYTNMYGSILFLTCISVDRFLAIVYPFKSKTLRTKRNAKIVCTGVWLTVIGGSAPAVFVQSTHSQGNNASEACFENFPEATWKTYLSRIVIFIEIVGFFIPLILNVTCSSMVLKTLTKPVTLSRSKINKTKVLKMIFVHLIIFCFCFVPYNINLILYSLVRTQTFVNCSVVAAVRTMYPITLCIAVSNCCFDPIVYYFTSDTIQNSIKMKNWSVRRSDFRFSEVHGAENFIQHNLQTLKSKIFDNESAA | Function: Binds to oleoyl-L-alpha-lysophosphatidic acid (LPA). Intracellular cAMP is involved in the receptor activation. Important for the maintenance of hair growth and texture.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39392
Sequence Length: 344
Subcellular Location: Cell membrane
|
Q8GXU8 | MDVASARSISSHPSYYGKPICSSQSSLIRISRDKVCCFGRISNGMTSFTTSLHAVPSEKFMGETRRTGIQWSNRSLRHDPYRFLDKKSPRSSQLARDITVRADLSGAATPDSSFPEPEIKLSSRLRGIFFCVVAGISATFLIVLMIIGHPFVLLFDPYRRKFHHFIAKLWASISIYPFYKINIEGLENLPSSDTPAVYVSNHQSFLDIYTLLSLGKSFKFISKTGIFVIPIIGWAMSMMGVVPLKRMDPRSQVDCLKRCMELLKKGASVFFFPEGTRSKDGRLGSFKKGAFTVAAKTGVAVVPITLMGTGKIMPTGSEGILNHGNVRVIIHKPIHGSKADVLCNEARSKIAESMDL | Function: Plastidial enzyme of the prokaryotic glycerol-3-phosphate pathway that converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at position sn-2 . Utilizes palmitoyl-ACP (16:0-ACP) to produce phosphatidic acid containing a saturated group at position sn-2, which is characteristic of lipids synthesized by the prokaryotic pathway . In vitro, can use 16:0-CoA as acyl donor . Essential for embryo development during the transition from the globular to the heart stage when chloroplasts begin to form .
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphate + holo-[ACP]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39395
Sequence Length: 356
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular Location: Plastid
EC: 2.3.1.51
|
Q8LG50 | MVIAAAVIVPLGLLFFISGLAVNLFQAVCYVLIRPLSKNTYRKINRVVAETLWLELVWIVDWWAGVKIQVFADNETFNRMGKEHALVVCNHRSDIDWLVGWILAQRSGCLGSALAVMKKSSKFLPVIGWSMWFSEYLFLERNWAKDESTLKSGLQRLSDFPRPFWLALFVEGTRFTEAKLKAAQEYAASSELPIPRNVLIPRTKGFVSAVSNMRSFVPAIYDMTVTIPKTSPPPTMLRLFKGQPSVVHVHIKCHSMKDLPESDDAIAQWCRDQFVAKDALLDKHIAADTFPGQQEQNIGRPIKSLAVVLSWACVLTLGAIKFLHWAQLFSSWKGITISALGLGIITLCMQILIRSSQSERSTPAKVVPAKPKDNHHPESSSQTETEKEK | Function: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position. Has preference for C-18-CoA substrates compared to C-16-CoA substrates. Required for female but not male gametophyte development.
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43676
Sequence Length: 389
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.51
|
Q9SYC8 | MKIPAALVFIPVGVLFLISGLIVNIIQLVFFIIVRPFSRSLYRRINKNVAELLWLQLIWLFDWWACIKINLYVDAETLELIGKEHALVLSNHRSDIDWLIGWVMAQRVGCLGSSLAIMKKEAKYLPIIGWSMWFSDYIFLERSWAKDENTLKAGFKRLEDFPMTFWLALFVEGTRFTQEKLEAAQEYASIRSLPSPRNVLIPRTKGFVSAVSEIRSFVPAIYDCTLTVHNNQPTPTLLRMFSGQSSEINLQMRRHKMSELPETDDGIAQWCQDLFITKDAQLEKYFTKDVFSDLEVHQINRPIKPLIVVIIWLGFLVFGGFKLLQWLSIVASWKIILLFVFFLVIATITMQILIQSSESQRSTPAKRPLQEQLISA | Function: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position. Has preference for C-18-CoA substrates compared to C-16-CoA substrates.
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43435
Sequence Length: 376
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular Location: Membrane
EC: 2.3.1.51
|
Q8L4Y2 | MEVCGDLKSDNLKNRPLTPLRILRGLMILLVFLSTAFMFLLYFAPIAALGLRLLSVQQSRKVVSLIFGLWLALWPYLFETVNGTTVVFSGDIIPVEKRVLLIANHRTEVDWMYLWNIALRKGCLGYIKYVLKSSLMKLPIFGWGFHVLEFIPVERKREVDEPVLLQMLSSFKDPQEPLWLALFPEGTDFTEEKCKRSQKFAAEVGLPALSNVLLPKTRGFGVCLEVLHNSLDAVYDLTIAYKPRCPSFMDNVFGTDPSEVHIHVRRVLLKEIPANEAESSAWLMDSFKLKDKLLSDFNAQGKFPNQRPEEELSVLKCIATFAGVISLTVVFIYLTLYSHSCFKVYACLSGTYLTFATYYKFQPSPGCFREDSCKVKNH | Function: May convert lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position (By similarity). Has no activity when expressed in bacteria or yeast.
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43064
Sequence Length: 378
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular Location: Membrane
EC: 2.3.1.51
|
A8J0J0 | MARKSSLAQAAIERKPVLLRPQLNVPRMSGITALPMERRPLPVAPSPSAKPELPARSALVCHAAAASVPLPNSDSAPQPNVLLAKIRAIMFFAWSFLLSLPLFVTMMVMAPLVLAFDKYRRLAQHFVNNLWACASTAPFYKVTIIGRENLPPPDKPVVYVANHQSFLDIYSLFHLQRPFKFISKTSNFLIPIIGWSMFLTGHVMINRVDRRSQLKCLQQCRDLLAEGAPVLFFPEGTRSLDCKMAGFKKGAFSVAAKAGVEVVPITLLGTGSLMPSGKESQLRPGQVTIVVHKALPPNKNADQLCDAARQAVASSLPPELVGSATEMAPDEQ | Function: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36241
Sequence Length: 332
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular Location: Membrane
EC: 2.3.1.51
|
Q41745 | MAIPLVLVVLPLGLLFLLSGLIVNAIQAVLFVTIRPFSKSFYRRINRFLAELLWLQLVWVVDWWAGVKVQLHADEETYRSMGKEHALIISNHRSDIDWLIGWILAQRSGCLGSTLAVMKKSSKFLPVIGWSMWFAEYLFLERSWAKDEKTLKWGLQRLKDFPRPFWLALFVEGTRFTPAKLLAAQEYAASQGLPAPRNVLIPRTKGFVSAVSIMRDFVPAIYDTTVIVPKDSPQPTMLRILKGQSSVIHVRMKRHAMSEMPKSDEDVSKWCKDIFVAKDALLDKHLATGTFDEEIRPIGRPVKSLLVTLFWSCLLLFGAIEFFKWTQLLSTWRGVAFTAAGMALVTGVMHVFIMFSQAERSSSARAARNRVKKE | Function: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position.
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42571
Sequence Length: 374
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular Location: Membrane
EC: 2.3.1.51
|
Q8FA49 | MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKTISTSIVLNALNALGVSAEASGRNDLVVKTAEGDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGITHEQVCEAIREAFFAHYGERVEAEIISPDKTPDLPNFAETFARQSSWEWNFGQAPAFSHLLDERFSWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFPEQEKELPELSAWIAGAVR | 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): 37863
Sequence Length: 338
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
|
P47512 | MQTFIITSPVFNPYFNAALEEWLLTEFRKNELVKVIYFWQNANTIVVGRNQNTYAEVNLKELESDKVNLFRRFSGGGAVFHDLGNICFSIILPRTGKVMENAYEQTTRNVVKFLNSLNVPAVFHGRNDLEINNKKFSGLAEYIAKDRLLVHGTLLFDTDFSKLAKYLNVDKTKIASKGVDSVAKRVVNVKEYLPNWTTAKFLEEMINFFTVTEKAETIVLTKDALAKVEKRAKEHFQSWEWNFGKTYEYNFKNKRYFNNAGLFECNVQVEKGTVVDIKFYGDFLSVVDITPVTKKLIGQKYDYKTFEKLFNELDHFSDYFGSLKPEQLLGVIFDNK | 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): 38944
Sequence Length: 336
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
|
C6DKP5 | MSSLRLLISDSYDPWFNLAVEECIFRQMPTTQRVLFLWRNAETVVIGRAQNPWKECNTRRMEEDGIKLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKSVSTQIVLDALSALGLKASASGRNDLVVETADGVRKVSGSAYRETKDRGFHHGTLLLNADLNRLADYLNPDIKKLQAKGITSVRSRVANLVELLPSVDHQVICQAVTQAFFDYFGEQCEPEIISPSAYPDLPGFSEQFARQSSWEWNFGQAPDFSHLLDNRFTWGGIELHFDVERGVIIRAQVYTDSLNPAPLEALACALQGTAYRPENMAATCQALITAFPEQQNELQELAEWLEQSLR | 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): 37858
Sequence Length: 338
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
|
Q1QEC2 | MKLRILKSAVTNPWFNLATEDWIFNTLNPDSHTLFLWRNSETVVIGRSQNPWVECKIDKMEADDVFLARRQSGGGAVFHDLGNTNFTFLSPKDDYDQAANFTIIINALKKLGIDADLSGRNDMQVGDKKISGSAFKHTADRSFHHGTLLVNANMQKLGDYLNPHPLKLKAKGIKSVRARVANLVEFNEDINHETLSDAIIEAFREYYRDTDYGDTAPVEELDEASLAKQPNLNKYYQQMADWDWRFGKTPEFTHHIETRFNWGIIDLHLDVKQAAIREVVIFSDALNVELIDLLKESLADVKYDKHDIKAKFDELNRAHPELAAQIDDVSEWLIGEMEG | 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): 38722
Sequence Length: 339
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
|
Q65T15 | MTILLQRAKFKKRLMPILFPLMLAGCTNLFGSNFQDVLRNDANASSEFYMNKIEQTREVEDQQTYKLLAARVLVTENKTAQAEALLAELTKLTPEQQLDKSILDALIAAVKRDNDSASALLKTIPLAQLSQSQTSRYYEVQARIAENKTDIIEAVKARIQMDMALTDVQRKQDNIDKIWALLRSGNKTLINTTQPEGNVALAGWLDLTKAYNDNLSQPSQLAQALQNWKTTYPNHSAAYLFPTELKSLSNFTQTQVNKIALLLPLSGNASILGSTIKSGFDDSRGADKSVQVDVIDTMAMPVTDAIALAKQNGDGMIVGPLLKDNVDVILSNPTAVQGMNVLALNSTPNARAIDKMCYYGLAPEDEAEAAANRMWNDGVRQPIVAVPQSDLGQRTASAFNVRWQQLAASDADVRYYNQPDDAAYNLTADPAQNQAIYIVVTDSEQLMSIKGALDNSGVKAKIYTNSRNNSSNNAVEYRLAMEGVTFSDIPFFKDLDGEQYKKIEAATGGDYSLMRLYAMGADSWLLAHSFNELRQVPGFSLSGLTGKLTAGPNCNVERDLTWYSYQGGNIVPLN | Function: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a).
Location Topology: Lipid-anchor
Sequence Mass (Da): 63113
Sequence Length: 574
Subcellular Location: Cell outer membrane
|
Q6LME4 | MNSMLNFTHKRKSVSRLLAPVALAVILAGCSSSNQQQASASNITAIATDTSANYLIKAESSDGIESIDWNILALKALIKEGQWTQADNQSKRLSRMSLSPIQMAEWQLARATLRYQQGQLQEALNTLNFQPWWPLPDNQYKRYFMLRAELLGQLGQHSKAARQRTMLDQYLPSNQKNANWQNLWQDLSSYNNSQLQSVSLKEDETVLRGWIQLSILKNTYSQRPVRLKSAVDEWLSMNPYHPAHQYLPTELEAIMSMEVAQLDNVALLLPLTGRFESQGKAVRDGFINAMLDDTSRDTDTELTVFDTEAESMTAIMAKLQANGTQFVIGPLRKEKVTAFQQSNTSQINLLALNQPEQLDVSQTQSCYFSLSPEQEAEQAAQHLFAKGHQYPLVLAPKSKFGQRMTDAFNEQWQQLTGRNADIDTFGSRKQIQQQISRIFGLNDSQARISQMNQLTGVKLESQQRSRRDTDAVYLIANKSELTLLKPFIEVAINPEVKPPKLYASSRGNPNANSDNSELRGIEFSDIPLIINPELSFMERFDSLWPNESNTSIRLHAFGMDAYKMVNELPQLRVVDNYTVQGMTGQLGIDNQCVVQREMDWAVFTSDGITPAAE | Function: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a).
Location Topology: Lipid-anchor
Sequence Mass (Da): 69215
Sequence Length: 613
Subcellular Location: Cell outer membrane
|
Q2NWH5 | MLYSYVLVFKTGRLLPVVLASLILAACTAQGPESQTGHAAIPANANADYYLQQMQQSSNDTKTDYQLLAIRALIKEGRLPQAQQQLAALQQIDSASLDAPQRLRYTQAMINAGQSRPSLDLVRAYIAQAPLLTDPAARQQNIDKTWQTLVSLPSPQSNLVINADENILQGWLDLLRIYQDNRQDPTLLQAAIKDWQTRYPQNPAAKTLPTPLSQVQNYSSSSVGGIALLLPLNGQAQVFSNAIQQGFSAAKNGLTTQQSALEQDASAAGQSTDGVPQNDGTAGTEPAGGSANQNGPVTTPGTRPDPAASGVDGQASAADNAPQATTLSGQSAGGQPSAAPSAASGVPVKVYDTSSQPLPALLAQAQRDGASMIIGPLLKNDVEQLYNDNAVAASAGTLNILALNQPEHLQPRPNICYFALSPEDEARDAANHIHQQGRQQPLLLLPRGALGDRIAKAFSDAWHQAGGATVLEQRFGSSAELKQNINSGSGISLTGTPVAAGAAVTIAGLTIPVPQDNGAVSPSGGAIDAVYIIATPVELALIKPMIDMRVSSRSRLALYASSRSYQADAGPDYSLEMEGLEFSDIPLLTGAHPALLSQISAQFRGDYSLVRLYAMGIDAWALANHFSEMRQIPGFQVAGETGTLSATPDCVINRTLSWLKYQRGQMIAAQ | Function: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a).
Location Topology: Lipid-anchor
Sequence Mass (Da): 70665
Sequence Length: 670
Subcellular Location: Cell outer membrane
|
A5F987 | MAMNHHQRRSVPRLLTPIALSIVLSACSTQPSSPDVVDITAQPLLTAQTYLMRADASQGNQQNDWLIMALKAAIEENNPDQAQLLIMRLAKQPLTPTQQAQWQLLRAQLLANTEQYQEALEQLSFQANWSLPQVQWQQYHQLRADIFTALDRSFDSTRELVALYGLSSNKDKEALADQIWANLNHYSASKIIKLSTEPDEAQLDGWLQLAIYMKTLGSDLPQLKNTLEKWLAENPQHPAAIYTPKAITDILALEIVKPTNTALLLPLTGKFAKQAQFIRDGFVFAMMNDADRQTNATLTIIDTNAETLESVDAILTSKQIDFVVGPLIKGNIEKLQQFQQSRGQMIPTLALNIPDQIDTTAGACYLALSPEQEVAQAAKHLFTQGYRYPLILAPQNAYGERVVEAFNEEWRRYSKNKVAVNLFGDKRQLQRNINSIFGLQDSQQNIAQMESLLGMGLESQPRSRRDIDAVYIVANSSELTLIKPFIEVAINPDTRPPKLFSNSNSNTGGRQYEDLSGVTYSDIPLLIQPAPSIKEQLTQIWPESSNAERRLQALGMDAYRLMVELPQMKIVEGYTIDGQTGVLSIDEQCVVQREISWAEHGVR | Function: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a).
Location Topology: Lipid-anchor
Sequence Mass (Da): 67670
Sequence Length: 603
Subcellular Location: Cell outer membrane
|
G7CES0 | MDGRQVVRARRWCATAAVALMTASTVAACGSDSGEIVISYYTPANEAATFTAVAQRCNAELGGRFRIEQRSLPREADAQRLQLARRLTGNDRSLDVMALDVVWTAEFAEAGWALPLSEDPAGLAEADATTNTLPGPLETAKWNGELYAAPITTNTQLLWYRADLMDEPPATWDEMLSEAARLHAQGGPSWIAVQGKQYEGLVVWFNTLLESAGGQVLSDDGQRVTLTDTPEHRAATVKALEIIKAVATAPGADPSITQTDENTARLALEQGRAALEVNWPYVLPSLLENAIKGGVGFLPLNENPALRGSINDVGTFAPTDEQFDLALNASKEVFGFARYPGVRPDEPARVTLGGLNLAVASTTRHKAEAFEAVRCLRNEENQRLTSIEGGLPAVRTSLYDDPQFQAKYPQYEIIRDQLINAAVRPATPVYQAMSTRMSATLAPISQIDPERTADELAEQVQQAIDGKGLIP | Function: Part of the ABC transporter complex LpqY-SugA-SugB-SugC, which is highly specific for uptake of trehalose. Involved in the recycling of extracellular trehalose released from trehalose-containing molecules synthesized by M.thermoresistibile. Trehalose uptake is essential for virulence (By similarity). Binds deuterated trehalose with similar high affinity to trehalose, trehalose analogs including galactotrehalose, 4-azido-4-deoxy-trehalose, 6-azido-6-deoxy-trehalose, 3-azido-3-deoxy-trehalose and mannotrehalose in the order of decreasing affinity, respectively, and 2-azido-2-deoxy-trehalose and kojibiose (alpha1,2-glycosidic bond) with very low affinity. Does not recognize single glucose, 6-amino-6-deoxy-trehalose, trehalose-6-phosphate, nigerose (alpha1,3-glycosidic bond), maltose (alpha1,4-glycosidic bond), isomaltose (alpha1,6-glycosidic bond) or glycerophosphocholine. Decreased recognition of alpha,beta-trehalose and almost no recognition of beta,beta-trehalose. Substrate specificity indicates a strict requirement for an alpha1,1-linked disaccharide .
Location Topology: Lipid-anchor
Sequence Mass (Da): 50958
Sequence Length: 471
Subcellular Location: Cell inner membrane
|
F4I4K5 | MESLLCRRRIKRVMVLIIALTWLRSTCGELEDQLFEVGKLKMFVDDLPDMPRLYGFNSVHGIIKPASLQIGMFSTKWKFHRDLPATPVFAYGTSRSKATVPGPTIETVYGVDTYVTWRNHLPKSHILPWDPTISPATPKHGGIPTVVHLHGGIHEPTSDGNADAWFTAGFRETGPKWTKTTLHYENKQQPGNMWYHDHAMGLTRVNLLAGLVGAYILRHHAVESPFQLPTGDEFDRPLIIFDRSFRKDGSIYMNATGNNPSIHPQWQPEYFGDVIIVNGKAWPRLNVRRRKYRFRIINASNARFFKFFFSNGLDFIVVGSDSAYLSKPVMTKSILLSPSEIVDVVVDFYKSPSRTVVLANDAPYPYPSGDPVNEENGKVMKFIINNESEDDTCTIPKKLINYPNADVSNAVLTRYISMYEYVSNSDEPTHLLVNGLPYEAPVTETPKSGTTEVWEVINLTEDNHPLHIHLGLFKVVEQTALLAAGLEEFKECMTKQNDAVKCQISKYARGKKTAVTAHERGWKNVFKMMPGHVTRILVRFSYIHTNASYPFDPTQEPGYVYHCHILDHEDNMMMRPLKVII | Cofactor: Binds 4 Cu cations per monomer. The Cu cations are bound as 3 distinct Cu centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear.
Function: Multicopper oxidase that may be involved in copper homeostasis and oxidative stress response, and that is necessary for root growth inhibition by low phosphate conditions. Functions together with LPR2 and PDR2 in a common pathway that adjusts root meristem activity to phosphate availability. Oxidizes the substrate 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulphonate) in vitro.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65998
Sequence Length: 581
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.-.-.-
|
Q949X9 | MEPSRRRMTRDMLLLIVTMAWLVTGDEGGIKQEERLFNLGKLEMFVDKLPHIPTLHGYHFVNGFLKPKSLHIGMFFKKWKFHRDLPATPVFAYGTSKRSATVPGPTIEAVYGVDTYVTWRNHLPLHHILPWDPTISPAIPKHGGIPTVVHLHGGIHEPTSDGNADSWFTAGFKETGSKWTKKTTHYVNKQQPGNMWYHDHAAGLTRVNLLAGLLGSYILRHSSVESPLRLPTGREFDRPLVIFDRSFRKDGSIYMNATGNNPTIHPQWQPEYFGDAIIVNGKAWPRLTVRRRKYRFRITNASNARFFRFFFSNGLDFIVVGSDSAYLAKPVSTKSVLLAPSEIVDVLVDFSKSTSKTAILANNAPYPYPSGDPVTEENSKVMKFIINYKSEVDTSIIPKKLIEYPPAHVSTSTRTRYIAMFEYVSSIDEPTHLYINGLPYNAPVTETPKIGTSEVWEVINLTEDNHPLHIHLGLFKVLEQTALVKSEEFIECMTKRNDAVKCEISKYARGNKTAVTVHERGWKNVFKMMPGHVTKILVRFSYIHSNESYSFDATQEPGYVYHCHILDHEDNMMMRPFAMVL | Cofactor: Binds 4 Cu cations per monomer. The Cu cations are bound as 3 distinct Cu centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear.
Function: Multicopper oxidase that may be involved in copper homeostasis and oxidative stress response, and that is necessary for root growth inhibition by low phosphate conditions. Functions together with LPR1 and PDR2 in a common pathway that adjusts root meristem activity to phosphate availability.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 66165
Sequence Length: 581
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.-.-.-
|
Q5ZE07 | MEKRRFLGVCLLVAVLVLRAAVLGRGDDGGGGGRLLDPGKLEMFVDELPDMPRMRGYGVAEGGKLVAGNLTIGMYETMWKFHRDLPATRVFAYGTSKETATVPGPTIEAMQGVPTYVTWTNHLPPRHFLPWDPTLTAAAPGSGVPAVVHLHGGVQHSGSDGHSLAWFTAGFAATGPRFSSPAAYEYPNQQPPGNLWYHDHAMGLTRVNILAGLLGAYRVASPAEEAALNLPSGEAFDRNLVLFDRDFLADGSLFMNRTGNNPSVHPQWQPEYFGAVVVANGKAWPYLRVRRRRYRLRILNASNARFFRLSLSGGLRFVHVASDSVYLARPVPTRAFLLAPSEIADVVVDFVESGNATAIVLRSDAPAPYPGDPGDKAETVPVMKFVIDDDDDALSTEPDTSSVPARLTSPSQYAKPDAREAVLMRRIAMYEYTKEGTDEPTHLYLNARSYMDPVTETPREGTSELWDVINLTDDNHPLHVHLALFVALEQRSLRDVDDLKECMMARGSGGGGADACGLERHLAGGRKHVVPKQERGWKNVFKVRPGTVTRLLVRFRPLSPPDSRRFPFDVAAGPGYVYHCHILDHEDNEMMRPMKIVR | Cofactor: Binds 4 Cu cations per monomer. The Cu cations are bound as 3 distinct Cu centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear.
Function: Multicopper oxidase that may play a role in the maintenance of inorganic phosphate homeostasis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65839
Sequence Length: 598
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.-.-.-
|
A2ZNT5 | MSPRIQQLAAVLLAAVVVVAAARDEPAAAKNYQTQWDTVMSILNCKSDSLIPSYICSVISKSRWGWASDDPNDDEYTPPDHPLPAPAAGRRRWPVMTSLNLTKYVDSLPRIAKIRGYGIRHGRPVPIKLTIGMYSKTWQFHRDMPPTPVFVYGQSLQTATFPGPTIVARQGVPLAVEWQNHLPDAHILPWDPKVPTAIPKKGGVPTVVHLHGGAHPPEFDGHAFAWFTRDFAENGSTWTRKTYTYPNVQAPGNLWYHDHALGLTRVSLLAGLLAAYVIEKPELEDPMNLPCGDHDLHLVIADREFYTNGSISIDREWKPEYFGLVITVNGKAWPYLSVQRRRYRLRILNASNARYFNVTLSNGALPFTVIGSDSSYLSRPVTVSNLVLSPAEIFDVIVDFSRLPAAMTEIEMLNTAPYPFPNGPNVTDPNLDGKVMLFKVAGKGKVDDMPDKSKVPEHGVPYASVAALPPPTTTRYIVLYENQTAPGNLYINGLRLEDPVTETPKSGTTELWQVINLTGDNHPLHLHIATFQAIKMTKIEGFQVFKDCMIKNNNTATCNLDQHAVGPVVPVPEEEKTWKNAVKIPPEFMTSVVVAFRLVEANQPYPFDATTEPGFVYHCHILDHEDNAMIRPLKLLP | Cofactor: Binds 4 Cu cations per monomer. The Cu cations are bound as 3 distinct Cu centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear.
Function: Multicopper oxidase that may play a role in the maintenance of inorganic phosphate homeostasis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 70919
Sequence Length: 637
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.-.-.-
|
P0AFA0 | MIIIRYLVRETLKSQLAILFILLLIFFCQKLVRILGAAVDGDIPANLVLSLLGLGVPEMAQLILPLSLFLGLLMTLGKLYTESEITVMHACGLSKAVLVKAAMILAVFTAIVAAVNVMWAGPWSSRHQDEVLAEAKANPGMAALAQGQFQQATNGSSVLFIESVDGSDFKDVFLAQIRPKGNARPSVVVADSGHLTQLRDGSQVVTLNQGTRFEGTALLRDFRITDFQDYQAIIGHQAVALDPNDTDQMDMRTLWNTDTDRARAELNWRITLVFTVFMMALMVVPLSVVNPRQGRVLSMLPAMLLYLLFFLIQTSLKSNGGKGKLDPTLWMWTVNLIYLALAIVLNLWDTVPVRRLRASFSRKGAV | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40358
Sequence Length: 366
Subcellular Location: Cell inner membrane
|
P45333 | MILIRYLIKEVFKSQIAILLILLLIFFSQQFVRVLGAAANGNVPADLVFSLLGLGMPTMAQLMLPLCLFIAILLTFGRLYAESEITVMRACGVGQRILVKVALIMSLLTAGIAAYNALWLSPWAIQKQVNMVEDAKANPTVGVLSSGQFISTNNNNVVLFIDKIKDNQIRNVYLFQMTPQKQTKPSVITAEKGELIALPNGDQVLNLKNTKRVEGTSALPDFRITHFDEYHAYLGYQSAENTNDEVAELTLSQLIDLDSSSAKAELHWRITLILAVPLMALIAVPLSRVNPRQGRFAKILPALLLYLIYFLLQSSFKSAGSAGKLEAELLMPLVNIGFFLLAVVLNSWDSEIMYKFRYLFSKKGSAKDDKYP | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41337
Sequence Length: 372
Subcellular Location: Cell inner membrane
|
P0ADC7 | MQPFGVLDRYIGKTIFTTIMMTLFMLVSLSGIIKFVDQLKKAGQGSYDALGAGMYTLLSVPKDVQIFFPMAALLGALLGLGMLAQRSELVVMQASGFTRMQVALSVMKTAIPLVLLTMAIGEWVAPQGEQMARNYRAQAMYGGSLLSTQQGLWAKDGNNFVYIERVKGDEELGGISIYAFNENRRLQSVRYAATAKFDPEHKVWRLSQVDESDLTNPKQITGSQTVSGTWKTNLTPDKLGVVALDPDALSISGLHNYVKYLKSSGQDAGRYQLNMWSKIFQPLSVAVMMLMALSFIFGPLRSVPMGVRVVTGISFGFVFYVLDQIFGPLTLVYGIPPIIGALLPSASFFLISLWLLMRKS | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39619
Sequence Length: 360
Subcellular Location: Cell inner membrane
|
Q886N1 | MSLIDPRAIIDPTAILADSVEVGPWSIIGPGVEIGEGTVVGPHVVLRGPTKIGKHNRIYQFSSVGEDTPDLKYKGEETRLVIGDHNVIREGVTIHRGTVQDRAETTLGDHNLIMAYAHIGHDSVIGNHVILVNNTALAGHVHVDDWAILSGFTLVHQFCHIGAHSFSGMGTAIGKDVPAFVTVFGNPAEARSMNFEGMRRRGFSEEAIHALRRAYKTVYRQGLTIAQALSDLAEPAAQFPEVAVFLQSIQTSTRGIIR | 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): 27954
Sequence Length: 258
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
|
Q4ZWR6 | MSLIDPRAIIDPTAVLADNVEVGPWSIIGPGVEIGEGTVVGPHVVLKGPTRIGKHNRIYQFSSVGEDTPDLKYKGEETRLVIGDHNVIREGVTIHRGTVQDRAETTLGDHNLIMAYAHIGHDSVIGNHVILVNNTALAGHVHVDDWAILSGFTLVHQFCHIGAHSFSGMGTAIGKDVPAFVTVFGNPAEARSMNFEGMRRRGFSEEAIHALRRAYKTVYRQGLTIGQALADLAEPAAQFPEVAVFLQSIQTSTRGIIR | 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): 27937
Sequence Length: 258
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
|
Q4FRI4 | MSQIHPTALISPSATIDETATIGPYCIVGDEVTIGAHTVLHRHVVVTRLTRIGEHNQFYQFSSIGEDPQDLKYAGERTWLEIGDHNTIREACSLHRGTEQDGGLTKIGSHNLLMVNTHVAHDCLIGDHNVLANNVGVAGHVTIGNHIIVGGNSGIHQFCTIDDYSLVGGATLVLKDVAAFTMVSGNPAKAHGLNVEGMRRKGWSKDSIDVLRQAYRVVFRSGLTTVQALEVLKQDLLPKEQKIEFLIDSLQKSRRGVVR | 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): 28267
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 1/6.
Subcellular Location: Cytoplasm
EC: 2.3.1.129
|
A1SYV1 | MTKKIAMIHPTAIVHENAIIGKDVEIGPYTIIGDRVEIGDNCWIAPHVVIKGPTKMGKGNKIYQFASIGEDCQDLKYNGEETFLEIGDNNVFRESCTVHRGTAQDQGTTRIGNNNLLMAYVHVAHDCVLGNNIILSNNATLAGHTKLANNVIIGGLSALHQFTRVGEFAMIGGCSAVNKDIPPYFMATGNYVEAQGVNSVGLKRSGFNSKAIMEIKRAYKILCREGNSLEQAKIKIAEKLEGCPELQVLYDFICEESRGIVR | 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): 28641
Sequence Length: 262
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
|
Q6ALW0 | MDKQKRETGSEIMVVTGEASGDIHGANLVRALKEKDSSLSFSGMGGPELASLGVEILYDAKKISVVGLVEVFSHLPSIFAAKKILQRRLKNKPPALLIIIDLPDFNLMLAKKAKALGIPVFYYITPQVWAWRSGRIKTIGERTDQLGVILPFEEEFFRQRGQAASYVGHPLLDNVSIKLSREEFLTKHRIGPAAKYVGLLPGSREKEISALLPDFLRAAKRLQDECSEKISFLLPIAATIDREQLLENGLAEYQDLLDIHVISEDRYELMACCDAVVAASGTVTLELAILEVPMLVVYRTSPISYWVGRKLVKIEFFSLVNLIAGREVVTELLQDEVTPERISIEIKELLYGAKGVAVGKGLREVHGLLGEAGASAKAADLALSMI | 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): 42466
Sequence Length: 386
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.4.1.182
|
F4IAT8 | MRLPVTVKATKPSFLVIWIRYSSAASSPTVSLNPSGRLQQTLAGSVEVKGKSLHSGKFSTVKLNPEIAGAGRFFEFRSRFIPASIEFAQESPLCTTLLKDELKIRTVEHLLSALEAKGVDNCRIQIESESSDDREVEVPIFDGSAKEWVDAIQGVGINAAQNHDGESVEKMVAHVNKPVYVCKNDTFVAAFPALETRITCGIDFPQVPAIGCQWFSWRPIHESSFAKDIASSRTFCVYEEVERMREAGLIKGGSLDNAIVCSAEHGWMNPPLRFDDEACRHKILDLIGDLSLVSRGGNGGLPVAHIVAYKAGHALHTDLARHLTMD | 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 (Potential).
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): 35717
Sequence Length: 326
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.
Subcellular Location: Mitochondrion
EC: 3.5.1.108
|
B7J3W7 | MIRQRTLKNMIWGTGIGLHSGKKVYIGLRPAPVNTGIVFHRSDIEGGAWIKADPLHVVDTRLSTNIGDGHIRVGTVEHLMSALAGLGIDNAYVDLDGPEVPIMDGSAAPFVFLIQCAGIEEQNAPKRFIRITKPLKAEDGDRWVQLEPFEGFKVSFAIDFDHPVMKNGGQEVTVDFARTSYLKEVARARTFGFMREVEALRRMGLALGGNLDNAIVVDDYRVLNEEGLRYTNEFVRHKVLDSIGDLYLLGHPLVGHFSGHKAGHALNNSLLRALLLRQDAWEFVDYAERRAPFSFADTLVTASA | 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): 33693
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 2/6.
EC: 3.5.1.108
|
Q029X9 | MRFETTVQRPVEASGVGLHSGVPVKIRILPAPVSTGVVFVRTDLDGFQIPASWRHVARVSYATSLMRQGVLISTTEHLLSVFYSMGIDNVYVEIDNLEVPILDGSGLPFVKLIAQAGIRQYRRKRRYLRIRRPISVEDKGKRISILPDEAFRLTCDTEYPAPVGRQSLELVVTPEHYASELAFARTFGWENDLDQMRNMGLIRGASLANAVCFTSEGPLNPDGLRAVDECCRHKALDLIGDLALLGRPLLGHVIAERAGHAMHAALVARIMGDPSIYEIITFDQLASRVTQALVS | 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): 32615
Sequence Length: 295
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
|
Q30ST0 | MYQTTIKKSVELVGIGLHKGSAVKLRLEPLESNSGLIFYRSDVDVAIPLLPANVVDTKMATVIGKDGYVISTIEHMLSAIYAYGIDNLKIIVNADEVPVMDGSSASFCMLLDEAGVVQLDVPKKIMRIKKEIIVQEGEKYVKLSPSTDLKYGFTIKFPHPVIQQQEYVLNFTKQNYKDEIARARTFGFLHEVQYLRSKGLALGGSLENAIVLDDKKVLNPEGLRFDDEFVRHKILDAIGDMALIGMNFVGNYEALAGSHDLNHKLTLELLKDAENYEVIELVDEKTKELEKAYA | 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): 32854
Sequence Length: 294
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
|
Q2LVE4 | MYFQRTLKSDLSCQSVGLHSGRKVNMRIRPASSDEGIILVRTDTRYRQMIRVCLENVTDTTLATTIGSSGAAISTVEHILSALSGMGVDNAIIEVDAPEIPIMDGSALPFVNMLKLVGIRTQEKLKKYLVVKKPVSVSEGESFAMLAPSSSFEITYKIEFDHPLIKEQSYHLKLSDETYEKEICSSRTFGFLKDVEYLQAKGLALGGSLKNAVILDEKRIINKEGLRSHNEFVKHKILDAIGDLSLIGMPIVGHFIAYKSGHKLNSMLVKALLEQQENWTTASFLNCQDAHGQNTREKFSIRDIPARKILGAIHA | 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): 34980
Sequence Length: 315
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
|
Q3A225 | MIYQSTLNKPLTISGIGLHTGRQITMILRPAEPDNGIIFHCTDGERRVSIPAVSANVVDTRLATVIGKDGLSVSTIEHLMAALSACGIDNLHIDIDGPEVPVMDGSAAPFVALLQETGNRVQEKRRKYLAIRKPITLVDGEKRVSIIPSRFFRITFDIAFDHPCIGLQHRAIKVNTETFRKEIAPARTFGFLHEVEYLKANGLALGGSLDNAVVIGEEGVLNPDGVRFEDECVRHKILDAVGDFSLLGHRVLGHVKAYKAGHDINHQMVEKILANADCWQLVESGEAASHGSLSMTGCAAMAMAGVAEA | 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): 33433
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
|
P72988 | MGHTIKAPLTVQGVGLHSGVETTVTLCPVAAGKGRYFQRVDLPKKPIIPADLTWVREAMLSTELGEPGATIRTVEHLLATLVALDIGDLRIEVNGPEVPLLDGSALSWLTAIAKVGTRPRSKKSQDQPIVITDPLTCQLEDAFVAAFPCATTRFSYGVDYPYLPIGKQWYTWEPDQENFATAIAPARTFGFADQIEKLRQAGLIKGGSLENALVCDKEKWLNPPLRFPDEPVRHKLLDLLGDLSLLGKIPQAHFVAYKASHKLHTQLAQKIADTYR | 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): 30326
Sequence Length: 276
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
|
B5YKK1 | MPFQKTIKSEISLTGIGIHTGKKINLNLIPAQRDTGIVFYRKDRNFPIKAKLPFVVDTSFATTLGVDGIKIRTVEHLLATLHVFGITNVFIEIDSSEIPVMDGSAIDFTKAILKAGIAKQGKTVSLFKITKPVYYEESHSKIFAKPYRGFKITYKIFYEHPLIMEQSLSIEINEQNFLNDIAPARTFGFLKDINYLLKNGFAKGGSLDNALVLDEKGVVGGNLRFKDEFVRHKILDAIGDLSLIGYPIQGHFIIEKGGHTSHINFLRKLIETGCYELAEEPYFNFQLSAQAV | 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): 32732
Sequence Length: 292
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
|
A5CWY8 | MIKQRTIKKEVKARGIGIHSGSVVNMTLIPAKEDHGVVFRRMDVGDKLVRAHSAFVNEVVLSTGLENKGVKVSTVEHLMSAFSALGIDNVLVELDSFEVPIMDGSSAPFIFLVQSAGIEEQSTHKKFFVIKDTIRVENGDSWAQVSKYEGFKVSLEIDFDHKKVKESGEKLSINFSKQSYLKEISRARTFGYMKDVEMMQRQNLALGASMDNAIALSDDDVLNEDGMRYQNEFVKHKILDIVGDLYLLGSNLIGHYEGYKTGHLLNDQLLSTILAKPDTWSIETFEEDNSPIQFYSEDWQNSL | 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): 34092
Sequence Length: 303
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
|
A0M2A1 | MKFTATQIAEILDGKVEGNPEAEVSELAKIEEGSEGSLTFLSNPKYTSFLYTTNASVTIVNDDFEVEQPVNTTLIKVKDAYKAFSTLLEYYNQIKLNKSGIEQPSHISESAKYGEGLYLGAFAYIGENVSIGENVKIYPNVYIGDNVKIGNNVTLFPGVKVYSESLIGSEVTIHSGVVIGADGFGFSPGDTGEYSKVPQIGNVIIEDYVDIGAGTTIDRATLGSTIIRKGAKLDNHIQIAHNVEIGENTAIAAQTGIAGSTKIGKNCLIGGQVGIAGHLTIGNRVKIQAQSGIGRDIKDDEMLQGSPAIGYSDYNKSYIHFKNLPKTMNIIHQLEKKINNG | 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): 36631
Sequence Length: 341
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q1R023 | MKTLTPCAFTLGELAERLKARLVGDSDRRVTGLATLLDAGPNDITFLANKTYLKYLPDTRAAAVLVHPAHGTDAPCARLELENPYLGYAELSRLFDPLAGQAPEGVHPSAVVAESARIGEHVSVGPQCVIEAGAVIGDGCVIGAGSIVGADSEIGADSRLHANVTVYHGVSVGRRAILHSGCVIGADGFGFAHDGQGWHKIAQLGGVIVGDDVEIGSCSSIDRGALGDTVIGNDVKIDSQVQIAHNVQIGDHSALAGCVGIAGSTRVGSHCMLGGGVGLSGHLTLCDGVQVTGMSLVTNSIHEPGVYSSGTGAMPNGLWRKNAVRFKQLDELAKRLSRLERGASDTP | 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): 35762
Sequence Length: 347
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q7NVY4 | MSYTLEHIVKQLGGALRGPNREVSRLAPLELAGAGEIAFVASAKFRRQMLESAADALIVTEALAAELPDRSLIVAADPYLYFARLATLFHPPKAPRAGIHPRAVVGVGCRIGESSEIAANATIGDNVVIGERCRLMPGVVVGDGCEIGDDVTLYPNVTIYHDCVIGNRVGVHSGSVIGGDGFGLAWDKDHWFKIPQTGRVVLEDDVEIGANTTVDRGALVDTVIRKGAKIDNLVQIAHNVEIGEHTAIAGCVGIAGSTKIGARCTVGGAAMFVGHIEVADRTHIGGGTLVSKSIKEAGNYASSYPLQSMKDWLSNAVHVRHLDDFAKRVKQLERELETLKKSKEEPHE | 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): 37120
Sequence Length: 348
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q485G0 | MTYTLAEIAIKLDAKLIVPAALDEQNEALTQISGLATLAKAGTGQVAFLANSKYQQQLSSTNASAVIVSPDAVEACQVSALVMDNPYMGYAMLASLLDSTPKVSCGIHPNAVIADDVLIGENVSVGANTVIESGVQLADNVSIGAGCFIGHGAKIGESTILWANITIYHRVEIGHHCLIQASTVIGSDGFGYAPVKGQYKWHKIPQLGSVIIGDHVEIGASTTIDRGALDNTEIRDGVILDNQIQIAHNVIVGENTAIAGCTVIAGSTVIGKNCTIAGLVGVNGHITIADNCVFTGMSMVTKNISQAGVYSSGMPVVQNKEWNKTNARVKRLDSLTKRVKELEKLLAKN | 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): 36606
Sequence Length: 349
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q1LNE8 | MKTPTLGQLATENGAQVVGDPDLAVVGLAPLDQAGPGDLSFLSNPLYLPQALASAAGAVIVSPADLERIRADGQAEGRNWLVARNPYVCFARVAQRFDRAANADSRTGIDPRASVAPDAVVPASCFIGPNVVIESGARLGERVRILANAFIGASAEIGEDTLIYANVSVYHRCVIGARNILHSGAVIGADGFGFAPDIGPTGVEYVKIPQVGRAVLGNDVEIGANTAVDRGAMADTVIEDGCKIDNQVQIAHNVHVGAHTVIAGTAAVSGSTKIGRFCVIGGAANFSGHLNIADRTTVSGGTSITKSITKPGGHYTSVFPFTSHGEWERNAAIVRGLSKLRERVVQLERRQRGENNAPAQNKQDEEKSS | 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): 38502
Sequence Length: 369
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q11WA1 | MEFTLEEIAHLLGGEVKGDGKAKVSSIAKIEEASSGSISFLSNPKYESFIYSTNASAVIVKKDFQPRESLKTSLILVDDPYTSFTTILEAYQQALNASKMGKEEPSFIGKNAVIGSNHYIGAFAYIGSNCKIGNNVKIYPQAYIGDNVTIGDNTTIYAGVKIYANCELGNQVTIHSGCVIGSDGFGFAPQADGTYKTIPQIGNVVIGNHVDIGANTVIDCATMGSTIIYDGVKIDNLIQIAHNVKIGKNTVIAAQAGISGSTTIGENCIIAGQVGIIGHIKIANKTTIAAQAGIGRTISEEGLTLLGSPAIEKLDFLKSFAIYRKLPTLQKRIEELEEKTLNLSGIKES | 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): 37062
Sequence Length: 349
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
A8ZYC0 | MKRSLEQIARLVSGRVVGDAAKKVSGAAPFEQAGPEEITLAGSAGFLKRIDQTGAGALVVPTDFTDSRRNLVAVENPAAAFARIRQMFDTGCRQPVGIDPRAVIGGGFACGEDVSIGPGVVIGDHVTLGDRVLLYPGVFLGNHVRIGNDGIIHANTSILRECVLGNRVIIHAGSVIGSDGFGFAPDGEMYVKIPHSGMVQIDDDVEIGAGNAIDRATFGRTWIRQGVKTDNLVHIAHNVTVGENTIIVAQVGIAGSTTVGRHVILAGQAGISGHLDIGDNAVVGPQAGIVKSIKPGETVSGTPGMPHKLWLRAQSIVAGLPGMRKKIAELEKRLAVLEKG | 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): 35407
Sequence Length: 340
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q6AJ06 | MKENITVAMLAELVDGEVIGDGEVLVGNFVSLETAGEGDITFLVKAGDQDLLTSTKAGAVIVHRKVEVESPATLIKVDDAYLAAAKIHTFLLEDEFSPEGIHRSAFVGEGCQISSEVTIKALVSIGNRVVIGPRTRIESGVAIGDDVTIGEDCLLKANVTIADGSQLGNGVTIHSGTVIGSDGYGYATDKMGFHYKRPQVGTVRVDDNVEIGANSCVDRATYGLTWIKSGAKIDNLVQIAHNVVVGENSLIVSQVGISGSTSLGRNVVMGGKAAAVGHLQIGDGVMIAGGSGVLSNLSAGAVVGGIPARPIKQWRKSVVLTTKLPEMQKDIRALKKSVEELAGKN | 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): 35912
Sequence Length: 345
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q2LVL5 | MKKSINEIADFLGGKVVGDGGILIKAVRGIDEAGPGDITFVANPQYEKKLNETGASAVLVTRDTERPGENVTLIQVDDPYVSLGKLLTIFYPEEREKPGISAQAIVEEGAEISPSATVYPGVYISSGAGIGAGVVLYPGVFVGRDAVIGENSILYPNVCVYRRCLIGKRVILHAGAVVGSDGFGFANPGRDNIKIPQIGIVQIDDDVEIGANTTIDRATLGRTWIQRGVKIDNLVQIAHNVVIGEKSIIVSQVGISGSTRLGRSVILGGQAGLVGHLQIGDFAMVGAQSGVHEDVPANSVVSGSPCQPHRNWLRSMSCLPRLPDMRHLLNDLRKRIETLEKLSEMKKEVEKEKESSREKEETK | 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): 38941
Sequence Length: 363
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q3A555 | MATLNELAELIGGEVVGDGSVVLNRMAPIESAGPGDITFVANPKYLAKLKDTTASAVIVKAGIECPGVNLLICANPYLAFAKVLTALHAQRPAPQGVMDGAWVDPSAELGADVTVHPGCVVGKNVRVGRGTILYPGVVLYDDVQVGEDCLVHAGVLVREQCRLGNRVVVQPGAVIGSDGFGFAPDGKSYYKIPQVGIVAIEDDVEVGANVCIDRAAMGVTLIKRGTKIDNLVQIAHNVSIGEDTILVAQVGIAGSSKVGDHCTLGGQVGVSGHLKIGDNTMVGAQSGIISDLPAGQVFSGTPTMPHREWLKASASMRSLPAMRKTVSNLQKRIEELEKLIKER | 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): 35827
Sequence Length: 343
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q31N90 | MRWSEFLQHLEAKTGPCTAKAIAGDPELHGVAAINEAQSGQVSFLDQESGLQDWIEQTAASALILPPDPALQARAEARNLPWMTTAQPRLAFAAAIAVFYQPFRPVAGIHPSAVIDPSAQLGDRVSVGAHVVIGANCVIGNDVILHANVVLYPGVSLGDRCQIHANSTIHERSQIGQDCVIHSGAVIGAEGFGFVPTASGWFKMEQSGIVVLEDGVEVGCNSAIDRPAVGETRIGAQTKLDNLVHIGHGCQIGKACAMAAQVGLAGGVEVGDRVILAGQVGVANRVKIGDRAIASSKSGIHGEIEAGAIVSGYPAIPNRQWLKTSAVYNRLPELYRSLRNLIRRVEVLEQDRPSS | 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): 37469
Sequence Length: 355
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
A0LPR5 | MESCFQGDSRKSYSLSELAEILGAAVRGDPAIRIRGVNSLEDALPDELSFITDVRYKPLLSKCRAAAIIVSPALAELEFPLLVAERPYVVFARAAQLFAEPPFLAPGVHPGAYIGPNVHLGEGVSVGPQAHIGEDCVVGPGTRIYGSAYLGPGVRVGENCMLYPGAVILDRCLLGNRVTVHSGTVVGSDGFGYAQDEKGRHVKIPQTGIVQIDDDVEIGANCTVDRATFGRTWVRRGAKIDNQVQIAHNVVIGEHAILVAQVGISGSTTLGSHVVLAGQVGVAGHIEIGDRARVGAKSGVHHSVGAGEDILGIPGVPAREWKRTYANIQRLARFREELRLLVEKVQRIEKALDGE | 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): 37808
Sequence Length: 355
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q2JLY8 | MQLQEIAQKLGCAYEGDPTLEIHSVASLAEARPGELSFLSEARYLPLLEQTQASAVIVEEGLALPCSIACLRGRDPRLLFAQAIELFYQPYRLPVGIHPTAVIDPSVELGEGVAIGPHAVVMEGVKIGDHTQIHPNVTIYPHVRIGSRCQLFANCVIHERTEIGDDCLIHSGAVIGDDGFGHIPLADGSWRRMLQAGRVVLEDNVEVGSNTTIDRAAVGETRIGRGTKIDNLVQIGHGVRTGSHCLIVAQVGIAGSTQLGHHVILAGQCGLAGHLHIGDGVRVAAQTGVTSDVPAGQTVAGYPHQPIAEWRKSMAVQRHLPELQRTLRKLEARVAKLEQNSTDRAPNAKMLEVGVDPETTCSS | 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): 38862
Sequence Length: 363
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.