ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q6LMF5 | MLSQAKNGASIVGEWLTKPPAPCLYDRQLVWITLSLMITGLVIVTSASVPVATRLTGIPFYFALRHAFFLVCSLVIIAGVVQVPLSRWKQFSVPMLFLSIVLLIIVLLIGRSVNGAARWIPLGIFNLQPAEVAKLSLFIFLAGYLVRQYSQVRASFIGFIKPLAVLGVLAFLLLMQPDLGSFVVMFVTTVGMLFIAGAKLWQFLVMISGALLGIGLLIVFEPYRLRRVTSFLDPWEDPFGSGYQLTQSLMAFGRGELMGQGLGNSIQKLEYLPEAHTDFVFAVLGEELGLIGVTVVLLLIFALVFKALFIGRKCLQSGQL... | Function: Peptidoglycan polymerase that is essential for cell division.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [G... |
Q15Q16 | MNTSTFATPLRAMFAQRHDAAPAVVRPYDVSLILLALSLMAIGLVIVTSASMPVASRLFDNPFHFAIRHGIYIVLAIGAALTVMQIPMQWWRTSNAWLLLLGLVLLIAVLLVGRSVNGSTRWLAIGPITIQAAEPAKLFFFCYLAGYLVRRYEEVTENIKGFAKPLVVFFAFAVLLLLQPDLGTVVVMLCTTIGLLFLAGAKLWQFFGLAFTGGAAVTFLIMFEEYRMKRITSFLDPWADPFGSGYQLTQSLMAYGRGDVFGQGLGNSLQKLEYLPEAHTDFIMAILAEELGFAGVLTVLALMLCIVLKAMKMGSKALQN... | Function: Peptidoglycan polymerase that is essential for cell division.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [G... |
C3KCS9 | MSIDFRNIIKPYPSPIITGRGIDLDFPMLAGCLALLGLGLVMITSASSEVAAVQSGNTLYMMIRHLVYLVIGLGACIVTMMIPIATWQRLGWLMLIGAFGLLIMVILPGIGREVNGSMRWIGFGAFNVQPSEIAKVFVVIYLAGYLVRRQKEVRESWMGFFKPFIVLLPMAGLLLMEPDFGATVVMMGAAAAMLFLGGVGLFRFTLMVVLAVAAVTVLVQAQPYRMARLITFTDPWSDQFGSGYQLTQALIAFGRGEWLGVGLGNSVQKQFYLPEAHTDFVFSVLAEELGVVGSLCTVALFVFVCVRGMYIGMWAEKAKQ... | Function: Peptidoglycan polymerase that is essential for cell division.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [G... |
D4G8R2 | MKKSHLYNRSLLSVTIILLIFSIIMVGSSSVSVGNRIRTDYLSFLKKNFIHSIISILCMIFVFNVPIYKWKKNKNKLILCSIILLLTLNYFGISNHGAKRWINIKIAFIQPSELVKISFSCYLSSYLSEKNKKTSTIQLISIILIVSKLLLSQPDFGTLVILYSSLLFMLFLIGKNFLFLSASSAIFTTIVLSLIYFRSYRAKRLISFLNPWSNYLGDGYQLVHSMLSFGRGKMFGQGIGNSIQKINFLPEPHTDFIISIIGEELGYLGIAMIVISLFFIFFQGMNIGRNALKDFQYFSGFLAYSISLLIIIQSIINIGS... | Function: Peptidoglycan polymerase that is essential for cell division.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [G... |
Q21MH0 | MIVNIASPLYGSVQGFRRLDFSLYATVAILISVGIVMVASSSLDFAAERYHDTWFFVRKQITFLAMGLVGGLVILAVPMSVWNKYSGLLLILAFFLLMAVLIPGIGKVVNGSRRWLSLGPFSMQASEIAKFCLIVYFASYLARRNEELRTQWSGFLKLTAVLLIIVLLLLLEPDFGSSVVISATLGCMMFVAGVPLARFLLLAVSGVAGLALMAVASPYRWERLVAFMDPWATQFDSGYQLVQSLIAFGRGGWFGVGLGNSLQKLFFLPEAHTDFIFAIFTEEFGFIGAIALIGVFGFFLYRLVILFRRASEQEQFFSSY... | Function: Peptidoglycan polymerase that is essential for cell division.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [G... |
A8FQ99 | MRSEERQLNLFGTSVNWSWPNLFKEREAPGMQLYDRALLFAVLSLICFGFVMVMSASMPEAQSLTGNPYHFAIRHFAYLVGCAVIAAVVLRIEMSRWQQFSPLLLLIVGIMLVAVLLVGTSVNGATRWLSVGPIRIQVAELAKFAFTIYMAGYLVRRHQEIRENAKGFYKPIAVFAVYAFLILMQPDLGTVVVLFVGTVGLLFLAGARLLDFFALILTGVMAFVALVLLEPYRMRRVTSFMDPWQDPFGSGYQLTQSLMAYGRGDWFGQGLGNSIQKLEYLPEAHTDFIFAVIGEELGFIGIVVVLSVLLFVALRAIKLG... | Function: Peptidoglycan polymerase that is essential for cell division.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [G... |
P74180 | MITAANLLRIIFPFYDPEVLRWSGEARLMRTLFFAWMAMGVVVLFSASYAESLDTSGTGLSIILKQIAYLWLGLNIFNFLVRLPLQVCLKLVPWFLIVVLLLIFLTKSGLGVEVNGARRWISLGPILIQPSEFMKPCLVLQAANLFGNWHRFPWRSRLIWLGIFALTLGSILLQPNLSTTALCGMGLWLIALASGLPWIYLISTALLGITTAVTSISIRDYQRARVTSFLDPFADPRGDGYQLVQSLYAIASGGVLGRGFGMSQQKLFYLPIQTTDFIFAVFAEEFGLVGCITFLAFLGLFTTMGLRVAMRCRHRVKRLI... | Function: Peptidoglycan polymerase that is essential for cell division.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [G... |
E8UEF9 | MGLIMVFSSSIALGDGPKYVNAGRYYFFSRQLIFILIGLFAMAFTFLMPMKFWDSKAFWGYCICFLLLALVLVPGIGREVNYAYRWIPIGPFNFQPSEFAKLTMIVFTSAYTVRKQKSIHGLKGFLPIIIYLGIICFLLINEPDLGATMVVVAIVMSILLLGGLGFALFSLLFLSAVLLVIAAILTAPWRMQRFFAYLDPFSQEHAQNTGYQLTHSLIAVGRGGFFGEGLGLSIEKLHYLPEAHTDFIMAVVGEELGFVGIFFVILLFVLLVRKGLNVGRQAIAMDRLFNGLVAQGVVVWFGVQAIVNLGVCFGVFPTKG... | Function: Peptidoglycan polymerase that is essential for cell division.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [G... |
D5X4H4 | MLERMLPFLGRKRDKAAADLPVRVGHSAPRNSRMLEYDQNLVWVTLLLLAYGLVMVYSATISFHDSPRYAQWSPYHYFIRDLFSIAAALLASWIVVQIPMAELQKWSMRFFFLSLIGLVLVLLPHIGKDVNGSKRWVVFPGGLNFQPSELVKLTALIYAADFMVRKQEVKQSLLKTFLPMMAVMMIVGVLLLAEPDMGAFLVIASITLAILFLGGANGKLFSVFSVAVIGAFVLMIVLSPWRRDRIFAYLNPWSESNALGSAYQLSHALIAMGRGEWFGVGLGGSIEKLHYLPEAHTDFLLAIIGEELGLVGVGVVIFAF... | Function: Peptidoglycan polymerase that is essential for cell division.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [G... |
D3SD93 | MSTGSLPLGLPSRDSLDGLRNSVDLPLLAAAALLLGLGLIMVASASMDLGERYYGNTWHFFQRQVLFAAIGLALATVMWAIPLERWERAGPWLLILVMVLLIAVLLPGVGRTVNGATRWIPIGMFNLQVAEPVKLLVVMYLAGYIVRHYSALRLHLRGFVRPLVVLGFGTVLLLLQPDFGGAAIMLAIGMGMLFLAGAKLWQFAALGATIAVGMAFVAVAAPYRVARLTAFLDPWQDPFATGFQLTQSLIAIGSGGWFGTGLGNSVQKLFYLPEAHNDFLFAVFAEEFGFIGVLALIALFAVVVWRCVKIGLWAERAGHA... | Function: Peptidoglycan polymerase that is essential for cell division.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [G... |
E6UUM7 | MNSAAAGATPNTRTSRFGGWFRRARSGIDSLPVHLPVRLGGAGIAQTKATPMRVLGFDQALVWVTVALLTWGLVMVYSASIALPDNPRFARAGYGASFFLTRHAASVAFAFIAALLAFQIPMKTWERAAPWLFVVSLLLLVAVLIPHIGISVNGARRWLPMGFMRFQPSELAKVAMVLYAASYMVRKMEIKERFFRAVLPMGIAVVVVGMLVMAEPDMGAFMVIAVIAMGILFLGGVNARMFFVIAALVVVAFGTIVASSPWRRERIFAYLDPWSEEHALGKGYQLSHSLIAIGRGEIFGVGLGGSVEKLHWLPEAHTDF... | Function: Peptidoglycan polymerase that is essential for cell division.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [G... |
Q8D2Z5 | MNNKKKIVKIFFYDKILFFLLISLSIIGIIIVSSASISFGIRLHNDYFYFAKRNLLYFFLSFFLFFQIIRIPINQLEKYNKIALLINLFLLIIVFIIGNSINGAIRWIKIGFFSIQPSECSKLILFFYISDYIVKKNKELKNKLWGFLKPIIIMLIFVILLLMQPDLGNSLILFLTTLLLFFLAGINLWKCCFMFLFGLLTIFILIIFKPYRIRRILSFLDPWEDPFNSGYQLTQSLMALGRGKIIGTGLGNSIQKLEYLPEAYTDFIFSILGEELGYIGSIIILIMLFFVIFRIFLIGKNSFIQKKFFSGYFSFSVGIW... | Function: Peptidoglycan polymerase that is essential for cell division.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [G... |
Q8P3K2 | MRTIIALETHDVRFPTSRELDGSDAMNPDPDYSAAYVVLRTDGAEDLAGYGLVFTIGRGNDVQTAAVAALAEHVVGLSVDKVIADLGAFARRLTNDSQLRWLGPEKGVMHMAIGAVINAAWDLAARAANKPLWRFIAELTPEQLVDTIDFRYLSDALTRDEALAILRDAQPQRAARTATLIEQGYPAYTTSPGWLGYSDEKLVRLAKEAVADGFRTIKLKVGANVQDDIRRCRLARAAIGPDIAMAVDANQRWDVGPAIDWMRQLAEFDIAWIEEPTSPDDVLGHAAIRQGITPVPVSTGEHTQNRVVFKQLLQAGAVDL... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays a role in the catabolism of L-fucose. Catalyzes the dehydration of L-fuconate to 2-keto-3-deoxy-L-fuconate by the abstraction of the 2-proton to generate an enediolate intermediate that is stabilized by the magnesium ion. L-fuconate is the preferred substrate wi... |
Q8XNL5 | MKTYPKIGIRPTIDGRQGGVRESLEEKAMKMAQAAKKLIENSLYYADGTPVQCVLASRTIGGSGDAGIVQQEFTGKNIVATLSVTPSWCYGTETMDLDPNTIKAIWGFNGTERPGAVYLAAAMSGYAQKGIPAFKIYGHDVQELDDDTIPVDVQEKILSFARGAIAVGQMKGKSYVNIGASSMGIAGSQVDISFFEDYLGMLVEFVDMTEILRRIHLEIFDPIEYDKALNWIKENCREGIDINEGKDLPDIVKKSKVIPADKDWEFIAKQAIIIRDILYRNEKLGDLGWEEEARGRNAIAGGFQGQRQWTDWLPNGDFTE... | Function: Converts the aldose L-fucose into the corresponding ketose L-fuculose.
Catalytic Activity: L-fucose = L-fuculose
Sequence Mass (Da): 65929
Sequence Length: 595
Pathway: Carbohydrate degradation; L-fucose degradation; L-lactaldehyde and glycerone phosphate from L-fucose: step 1/3.
Subcellular Location: Cytopla... |
Q8ZMC4 | MLKTISPLISPTLLKVLAEMGHGDEIIFSDAHFPAHSLGPQVIRADGLSVSDLLRAIIPLFELDSYAPPLVMMAAVEGDTLDPNVEARYRDALSLEAPCPDIVRIDRYAFYERAQKAFAIVITGECAKYGNILLKKGVTP | Function: Involved in the anomeric conversion of L-fucose.
Catalytic Activity: alpha-L-fucose = beta-L-fucose
Sequence Mass (Da): 15281
Sequence Length: 140
Pathway: Carbohydrate metabolism; L-fucose metabolism.
Subcellular Location: Cytoplasm
EC: 5.1.3.29
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Q8P3K1 | MSMQRLCYVLDLHDDAALIAQYERWHRPSEVWPEVVASLQQAGIAELEIFRSGDRLVMLMTVGEDYDPAAKAARDAGDPRIQAWEALMWRFQKALPGSAPGEKWREAGRIFALSEAVSVQQGSAA | Function: Plays a role in the catabolism of L-fucose. Involved in the anomeric conversion of L-fucose.
Catalytic Activity: alpha-L-fucose = beta-L-fucose
Sequence Mass (Da): 13959
Sequence Length: 125
EC: 5.1.3.29
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Q8GW72 | MNSQITLFFFFFSILSLSQISNSSSLLKPHPCPILPLPSSQQLQWQLGSMAMFLHFGPNTFTDSEWGTGKANPSIFNPTHLNASQWVQIAKDSGFSRVILTAKHHDGFCLWPSEYTDYSVKSSQWRNGAGDVVAELASAAKEAGIGLGLYLSPWDRHEQCYGKTLEYNEFYLSQMTELLTKYGEIKEVWLDGAKGDGEKDMEYFFDTWFSLIHQLQPKAVIFSDAGPDVRWIGDEAGLAGSTCWSLFNRTNAKIGDTEPSYSQEGDGYGQDWVPAECDVSIRPGWFWHASESPKPAVQLLDIYYNSVGRNCLFLLNVPPN... | Function: Hydrolyzes both 3- and 4-linked fucoses in Lewis determinants. Not active on neither 2-linked fucose nor on fucose in alpha-1,3-linkage to the innermost GlcNAc.
Catalytic Activity: an alpha-L-fucoside + H2O = an alcohol + L-fucose
Sequence Mass (Da): 57186
Sequence Length: 506
Subcellular Location: Secreted
E... |
Q7XUR3 | MATILLLLLGLLVGLPLLRAHGVTGSAAPTPPPLPVLPVPSYAQLQWQLSEMALFLHFGPNTFTDSEWGSVRADPAVFAPSALDAGQWARAAAAGGFGRVVLTAKHHDGFCLWPSALTNYSVAASPWKGGAGDVVGELAAAARAEGIGLGLYLSPWDRHEPVYGDTVAYNEHYLGQMTELLTRYGDVEEVWLDGAKGEGKDMDYMFDAWFALIHQLQQRVVIFSDAGPDTRWVGDEAGVAGYTCWSPFNKSTVTIGHIIPEYSRCGDPFGQDWVPAECDVSIRPGWFWHASEKPKNATTLLDIYYKSVGRNCLLILNVPP... | Function: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Active only against 2'-fucosyl-lactitol when heterologously expressed.
Catalytic Activity: an alpha-L-fucoside + H2O = an alcohol + L-fuco... |
Q8L7W8 | MAEKSSFFVHFSCLLLLLTIIITCGEGVRNPVRPRSSERRALMDGQDLSRPLKLTFGGPSRNWTDAIPIGNGRLGATIWGGVSSEILNINEDTIWTGVPADYTNQKAPEALAEVRRLVDERNYAEATSEAVKLSGQPSDVYQIVGDLNLEFDSSHRKYTQASYRRELDLETAVAKVSYSVGAVDFSREFFASNPDQVIIAKIYASKPGSLSFKVSFDSELHHHSETNPKANQILMRGSCRPKRLPVNLKKSINATNIPYDDHKGLQFASILEVRVSNGGSVSSLGGKKLSVEKADWAVLLLAASSNFDGPFTMPVDSKID... | Function: Hydrolyzes alpha-1,2-linked fucose. Also active on fucosylated xyloglucan oligosaccharides. No activity with 3-fucosyllactose, p-nitrophenyl-alpha-I-fucopyranoside, lacto-N-fucopentaose II, lacto-N-fucopentaose III or alpha 1,6-fucosylated chitopentaose. Involved in apoplastic xyloglucan metabolism.
Catalytic... |
Q9BTY2 | MRPQELPRLAFPLLLLLLLLLPPPPCPAHSATRFDPTWESLDARQLPAWFDQAKFGIFIHWGVFSVPSFGSEWFWWYWQKEKIPKYVEFMKDNYPPSFKYEDFGPLFTAKFFNANQWADIFQASGAKYIVLTSKHHEGFTLWGSEYSWNWNAIDEGPKRDIVKELEVAIRNRTDLRFGLYYSLFEWFHPLFLEDESSSFHKRQFPVSKTLPELYELVNNYQPEVLWSDGDGGAPDQYWNSTGFLAWLYNESPVRGTVVTNDRWGAGSICKHGGFYTCSDRYNPGHLLPHKWENCMTIDKLSWGYRREAGISDYLTIEELV... | Function: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.
Catalytic Activity: an alpha-L-fucoside + H2O = an alcohol + L-fucose
Sequence Mass (Da): 54067
Sequence Length: 467
Subcellular Location:... |
Q10279 | MESVDNNSFFSRIRNSNAYRKVKDFVILDHRPGMTMAERMLTNKDLYPVPPSKRLWGPWNFISFWLADAVNINTWMISATAIELGLNWWEAWICVWVGYLICGILVATTGRPGAVYHISFPVLSRSSFGTWGSLWPILNRSVLACVWYGVQAWIGGECVVLMIRSIWPSFSHIPNTMAKSGTETYQWVGFFIFWLLSNIAIWFPVHQIRHLFTFKAIVAPPAAIAFLIWALVKAHGAGPVIHEPTKLGQYEHAWVVINGIVTCIDGFATLIVNNPDFARFATTPGAVHWPQIITVPLAFGVTSLIGVLVSSASKAIYGTT... | Function: Transport of uracil.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64177
Sequence Length: 581
Subcellular Location: Membrane
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P05316 | MPDNLSLHLSGSSKRLNSRQLMESSNETFAPNNVDLEKEYKSSQSNITTEVYEASSFEEKVSSEKPQYSSFWKKIYYEYVVVDKSILGVSILDSFMYNQDLKPVEKERRVWSWYNYCYFWLAECFNINTWQIAATGLQLGLNWWQCWITIWIGYGFVGAFVVLASRVGSAYHLSFPISSRASFGIFFSLWPVINRVVMAIVWYSVQAYIAATPVSLMLKSIFGKDLQDKIPDHFGSPNATTYEFMCFFIFWAASLPFLLVPPHKIRHLFTVKAVLVPFASFGFLIWAIRRAHGRIALGSLTDVQPHGSAFSWAFLRSLMG... | Function: Transport of uracil.
PTM: Glycosylated (possible); but there is not yet direct biochemical evidence for it.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71736
Sequence Length: 633
Subcellular Location: Membrane
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Q2L6E3 | MPGTDDVAVDVASVYSAIEKSAGLLDVTAAREVVWPVLTAFEDVLEQAVIAFRVATNARHEGDFDVRFTVPEEVDPYAVALSRSLIAKTDHPVGSLLSDIQQLCSVDTYGVDLGVKSGFKKVWVYFPAGEHETLARLTGLTSMPGSLAGNVDFFTRYGLADKVDVIGIDYRSRTMNVYFAAPSECFERETVLAMHRDIGLPSPSEQMFKFCENSFGLYTTLNWDTMEIERISYGVKTENPMTFFARLGTKVEHFVKNVPYGVDTQKMVYAAVTSSGEEYYKLQSYYRWRSVSRLNAAYIAARDKEST | Function: Involved in the biosynthesis of furaquinocin. Catalyzes the transfer of a geranyl group to 2-methoxy-3-methyl-flaviolin to yield 6-prenyl-2-methoxy-3-methyl-flaviolin and 7-O-geranyl-2-methoxy-3-methyl-flaviolin in a 10:1 ratio. Can also use other substrates such as flaviolin or 1,3-dihydroxy naphthalene, and... |
Q75W17 | MATITTLASSVPLFRPYSFPGGSSRKPKKDNLSIKPPATSSLKVNAKLASADDTSSNFNKDNWLASADELSRSFPPGFLFGGGSASYQYEGAVKEGGRTPSIWDTFAHEFPDKIADGSNGDVAVDFYHRYKDDVKLMKKIGVNGFRFSISWTRILPSGKLCGGVNKEGVAFYNSLINELLANGIEPFVTIFHWDLPQGLENEYDGFLSGQIVNDYRDYAEVCFQEFGDRVKFWTTLNEPWTFCYNGYVNGSFAPGRCSTCTAGNSGTEPYLVAHNLLLSHAAVAQLYKNKYQASQKGQIGIVLVCFWMVPYSDCPYDCEA... | Function: Disaccharide-specific acuminosidase, hydrolyzes the beta-glycosidic bond between p-allylphenol and acuminose with retention of anomeric configuration. Has highest activity towards furcatin, and lower activity towards beta-primeverosides and beta-vicianoside. Has very low activity towards beta-gentobiosides.
C... |
P09958 | MELRPWLLWVVAATGTLVLLAADAQGQKVFTNTWAVRIPGGPAVANSVARKHGFLNLGQIFGDYYHFWHRGVTKRSLSPHRPRHSRLQREPQVQWLEQQVAKRRTKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSA... | Cofactor: Binds 3 calcium ions per subunit.
Function: Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif . Mediates processing of TGFB1, an essential step in TGF-beta-1 activation . Converts through proteolytic cleavage the non-functional Brain natriuretic... |
P61154 | MVKVVRNVVCPFCGTLCDDLEILVEDNHIVGTRHACRIGNAKFMHFEGAVRYTEPLMRENKKDDFKKVDYETAIEETARLLTEATLPLIYGWSATECHAHMYGVELAELVGAVIDNTASVUHGPSLLAVQDVGYPVCTLGEVKNRADVIIFWGSNPMHAHPRHMSRYSVFARGFFRERGREDRTLIVVDPRETDTAKLADIHLQVEPHKDYELVSAMRAVLKGFELQVDKVAGVPADLIYEAVEVCKNAQFGELFFAMGVTMTRGKHRNIDNAIQLVIDLNAYTKFGLMPMRGHYNVNGFNQVLTWVTGYPFGVDFSRGY... | Function: Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). This enzyme is oxygen-labile.
Catalytic Activity: H2O + N-formylmethanofuran + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + H(+) + methanofuran + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 48718
Sequence... |
Q58571 | MKELILTLQKEIIVPVEMDKVLPEVIENMSLEEIKNIELVQGRKRIKVADIFDVELNDIEGEPRIVIKNSSPKLKYIGSKMTKGEIVVEGDAGMYVGAEMKGGKIVVNGNAESWAGQNMKGGELLIKGNAGDYVGSAYRGDWRGMSGGTIIVEGNAGNEIGEFMSKGLIHIKGNVGIMAGIHQNGGIIIIDGDVDVRVGGEMKAGAIVVYGKVEEILPSFKFEGIVENPVIKLSKKDAGTPIAGTFYKFSGDYVYNKPKGQLYISVDSNPDLI | Function: Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). This enzyme is oxygen-labile.
Catalytic Activity: H2O + N-formylmethanofuran + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + H(+) + methanofuran + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 29461
Sequence... |
O27600 | MSEIILTPKEQPEVPLEAPNIKPDVFAGKSIDEIRNIQIMHGNEVVKLGDFFEVSGEPADSAADIKIIIDGDVYNTKRIGQDMTAGEILVKGNVNMYVGAGMKGGKITVEGNAKSWAGQDMRGGELEIFGDAGDYVGSSYRGDWRGMSGGVITVHGNAGNEIGEYMNGGKIIIKGDVNIMPGIHMNNGLIIIEGNAVARVGGEMAGGTIVVKGMIEEFLPGFKYLGVEKDIEVNGETFPGAYYKFEGDHAIKGAKGMVYAAVGCNGHIEP | Function: Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). Can only oxidize formylmethanofuran. This enzyme is oxygen-labile.
Catalytic Activity: H2O + N-formylmethanofuran + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + H(+) + methanofuran + 2 reduced [2Fe-2S]-[ferredoxi... |
Q49611 | MVKIVIHEERCHGCGNCVIACPVNACNSPNVWGGKGPEDGEDVVIKVVNGTVSVINEDLCEACMTCELACPVDAIEIKT | Cofactor: Binds 2 [4Fe-4S] clusters.
Function: Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). This enzyme is oxygen-labile. May function as an electron transfer protein.
Catalytic Activity: H2O + N-formylmethanofuran + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + H(+) ... |
P0DM17 | MQRGAVLLGVVALLVLWPQAGAELYDVNDPDVRAMVIDGQKLMHDCAIANDYIDDPWWTLNLGAFEEKRVYHSMLSELVFCLNAFLQRRQQAP | PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 10575
Sequence Length: 93
Domain: The cysteine framework is C-C.
Subcellular Location: Secreted
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P37147 | MRWLPFIAIFLYVYIEISIFIQVAHVLGVLLTLVLVIFTSVIGMSLVRNQGFKNFVLMQQKMAAGENPAAEMIKSVSLIIAGLLLLLPGFFTDFLGLLLLLPPVQKHLTVKLMPHLRFSRMPGGGFSAGTGGGNTFDGEYQRKDDERDRLDHKDDRQD | Function: Overexpression alleviates the exclusion of phage T7 in cells harboring the F plasmid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17692
Sequence Length: 158
Subcellular Location: Cell inner membrane
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C0HJJ0 | MSQLTELVLLTVFLALFSRAEANPFVYNYEALRIGGLVFTCVLVAGAVTALCWGQCKPKRKHDDDASKI | Function: May modulate the activity of a sodium/potassium-transporting ATPase.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 7604
Sequence Length: 69
Subcellular Location: Cell membrane
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Q14802 | MQKVTLGLLVFLAGFPVLDANDLEDKNSPFYYDWHSLQVGGLICAGVLCAMGIIIVMSAKCKCKFGQKSGHHPGETPPLITPGSAQS | Function: Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell . Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated inhibition of ATP1B1 . Induces a hyperpolarization-... |
Q61835 | MQEVVLSLLVLLAGLPTLDANDPENKNDPFYYDWYSLRVGGLICAGILCALGIIVLMSGKCKCKFRQKPSHRPGEGPPLITPGSAHNC | Function: Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell . Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated inhibition of ATP1B1 (By similarity). Induces a hyp... |
P59645 | MQEFALSLLVLLAGLPTLDANDPEDKDSPFYYDWHSLRVGGLICAGILCALGIIVLMSGKCKCKFSQKPSHRPGDGPPLITPGSAHNC | Function: Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell. Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated inhibition of ATP1B1. Induces a hyperpolarization-ac... |
Q63113 | MEGITCAFLLVLAGLPVLEANGPVDKGSPFYYDWESLQLGGMIFGGLLCIAGIAMALSGKCKCRRNHTPSSLPEKVTPLITPGSAST | Function: Induces a potassium channel when expressed in Xenopus oocytes.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 9084
Sequence Length: 87
Subcellular Location: Membrane
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Q96DB9 | MSPSGRLCLLTIVGLILPTRGQTLKDTTSSSSADSTIMDIQVPTRAPDAVYTELQPTSPTPTWPADETPQPQTQTQQLEGTDGPLVTDPETHKSTKAAHPTDDTTTLSERPSPSTDVQTDPQTLKPSGFHEDDPFFYDEHTLRKRGLLVAAVLFITGIIILTSGKCRQLSRLCRNRCR | Function: Involved in down-regulation of E-cadherin which results in reduced cell adhesion. Promotes metastasis.
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 19472
Sequence Length: 178
Subcellular Location: Membrane
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P97808 | MSLSSRLCLLTIVALILPSRGQTPKKPTSIFTADQTSATTRDNVPDPDQTSPGVQTTPLIWTREEATGSQTAAQTETQQLTKMATSNPVSDPGPHTSSKKGTPAVSRIEPLSPSKNFMPPSYIEHPLDSNENNPFYYDDTTLRKRGLLVAAVLFITGIIILTSGKCRQLSQFCLNRHR | Function: Involved in down-regulation of E-cadherin which results in reduced cell adhesion. Promotes metastasis (By similarity).
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 19454
Sequence Length: 178
Subcellular Location: Membrane
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B1L7K1 | MTRAVAEDLASSLEPDYRILHVLTTGGLEDLMDAIKTARKSEVDLLIGVGGGKPLDITKILAAELGVRYVVVPTSASHDGIASPSVSFTLSREIEERFGRVIRVEAPTAILADTTIINRASPITFKSGFGDLVAKITAVRDWELAYKLRDEPYSEYAASMSLLSAKIAMDHAHEIRTRLEESTRILVKALIGSGVAMSIAGSSRPASGSEHMFSHALDILSSEAGVKPAPHGIQVAIGTIMMAYLQGQDWKMIKEKLIEAGVPTTAEEAGISPDMIVKALTIAHKIRERYTILGSSGLTLSAAEKLARVTGVIK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea.
Catalytic Activity:... |
Q2FPC7 | MSTDPVQVLQPDGFNKSRWTQLPRDVLIGHQAIMQLPDIIADIKPGRSVLLISGGTTREVAGNTVADILKDQYEVRRFVAGKLDADTLEACSQASSSADFLIGVGGGRVIDCAKIVSYKQGKPFISVPTAASHDGIISGRATLPTETGSVSVGAHPPIAVVADTGIISQAPHRLMASGCADVISNYTAILDWELAHRLRGEQISEYAIALSKMTAEILVKDANLIKPGQEEAAWIVVKALVSSGVSMAIAGSSRPASGGEHKFGHALERLMPGAALHGEACGIGSIMTMYLHGGDWREIRSSLARIGAPTTPRELNIPDE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea.
Catalytic Activity:... |
Q58122 | MIIVTPRYTIIEDGAINKIEEILKKLNLKNPLVITGKNTKKYCRFFYDIVYYDEILNNLEIELKKYTAYDCVIGIGGGRSIDTGKYLAYKLGIPFISVPTTASNDGIASPIVSIRQPSFMVDAPIAIIADTEIIKKSPRRLLSAGMGDIVSNITAVLDWKLAYKEKGEKYSESSAIFSKTIAKELISYVLNSDLSEYHNKLVKALVGSGIAIAIANSSRPASGSEHLFSHALDKLKEEYNLNINSLHGEQCGIGTIMMSYLHEKENKKLSGLHEKIKMSLKKVDAPTTAKELGFDEDIIIEALTMAHKIRNRWTILRDGL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea.
Catalytic Activity:... |
Q8TW08 | MSVPKKRMQLPREVVVGSNVLPEVPKLLRSVGVPDGVVAVFSGRTTMKIAGNEVADHLEEAGYQTSPVIVKGSTGDDVKKALEALDEIDADVVAAVGGGKVIDVAKVASYRRGIPFISVPTSASHDGIASPFASIRREGRPYSEPAQAPLAILADIEVIREAPERLIRAGVGDVVSNVTAVKDWRLAHRLRNEPYSEYASSLSLMAARIVMKNAKPIGKLLPEGIKKLVQALISGGVAMSIAGSSRPCSGSEHLFSHALDVIAERPALHGEQCGVGTIIMEYLHGGNWREIRETLETAGAPTTAEDLGVSDEEIIEALCR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea.
Catalytic Activity:... |
Q5HF86 | MSTNIAINGMGRIGRMVLRIALQNKNLNVVAINASYPPETIAHLINYDTTHGKYNLKVEPIENGLQVGDHKIKLVADRNPENLPWKELDIDIAIDATGKFNHGDKAIAHIKAGAKKVLLTGPSKGGHVQMVVKGVNDNQLDIEAFDIFSNASCTTNCIGPVAKVLNNQFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPELEGKLHGMALRVPTKNVSLVDLVVDLEKEVTAEEVNQAFENAGLEGIIEVEHQPLVSVDFNTNPNSAIIDAKSTMVMSGNKVKVIAWYDNEWGYSNR... | Function: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester,... |
Q8CNY0 | MATNIAINGMGRIGRMVLRIALNNKNLNVKAINASYPPETIAHLLNYDTTHGVYDKKVEPIESGIKVNGHEIKLLSDRNPENLPWNEMDIDVVIEATGKFNHGDKAVAHINAGAKKVLLTGPSKGGDVQMIVKGVNDNQLDIDTYDIFSNASCTTNCIGPVAKVLNDKFGIINGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTKNVSLVDLVVDLEQNVTVTQVNDAFKNADLSGVLDVEEAPLVSVDFNTNPHSAIIDSQSTMVMGQNKVKVIAWYDNEWGYSNR... | Function: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester,... |
Q829W3 | MTIRVGINGFGRIGRNYFRALLEQGADIEIVAVNDLGDTATTAHLLKYDTILGRLKAEVTHTADTITVDGKTIKVFSERNPADIPWGELNVDIVIESTGIFTKKADAEKHIAGGAKKVLISAPASDEDITIVLGVNEDKYDPAKHNVISNASCTTNCVAPMAKVLDENFGIVKGLMTTIHAYTNDQRILDFPHKDLRRARAAAENIIPTTTGAAKATALVLPQLKGKMDGISMRVPVPTGSATDLVVEVSREVTKDEVNAAFKKAAEGELQGYLSYTEDPIVSSDIVGDPSSCTFDSAMTMVMEGTSVKILGWYDNEWGY... | Function: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester,... |
P00358 | MVRVAINGFGRIGRLVMRIALQRKNVEVVALNDPFISNDYSAYMFKYDSTHGRYAGEVSHDDKHIIVDGHKIATFQERDPANLPWASLNIDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAPLAKVINDAFGIEEGLMTTVHSMTATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSNSSIFDAAAGIQLSPKFVKLVSWYDNEYGYST... | Catalytic Activity: D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH
Sequence Mass (Da): 35847
Sequence Length: 332
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subcellular Location: Cytoplasm
EC: 1.2.1.12
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Q2NEN0 | MKSIGINGYGTIGKRVADAVSAQDDMKIVGVTKRTPDYEAKAAVEKGYDLYISVPERESQFEEAGIEVAGTADELFEKLDLVVDCTPGGIGAQNKTDIYEKIGLKAIFEGGEDHDAIGSSFNAEANYADNIGEDYVRVVSCNTTGLCRTLKPIYDISGIKKVRAVMVRRGADPSDVKKGPINSIVPTTEVPSHHGPDVQTIIDDINVMTMALLVPTTLMHTHNIMVELEDKITTDDVLDAFENAHRVLPVQKSLKLGSTAEIMEYAKDLGRSRGDMYEIPVWKESVNIENGELFYMQAVHQESDVVPENVDAIRAMLELE... | Catalytic Activity: D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADPH
Sequence Mass (Da): 36910
Sequence Length: 337
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subcellular Location: Cytoplasm
EC: 1.2.1.59
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P47543 | MAAKNRTIKVAINGFGRIGRLVFRSLLSKANVEVVAINDLTQPEVLAHLLKYDSAHGELKRKITVKQNILQIDRKKVYVFSEKDPQNLPWDEHDIDVVIESTGRFVSEEGASLHLKAGAKRVIISAPAKEKTIRTVVYNVNHKTISSDDKIISAASCTTNCLAPLVHVLEKNFGIVYGTMLTVHAYTADQRLQDAPHNDLRRARAAAVNIVPTTTGAAKAIGLVVPEANGKLNGMSLRVPVLTGSIVELSVVLEKSPSVEQVNQAMKRFASASFKYCEDPIVSSDVVSSEYGSIFDSKLTNIVEVDGMKLYKVYAWYDNE... | Function: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester,... |
Q43727 | MATHSMIIPSPSSSSSSLATAASPFKETLPLFSRSLTFPRKSLFSQVRLRFFAEKHSQLDTSNGCATNFASLQDSGDQLTEEHVTKGESTLSITVVGASGDLAKKKIFPALFALFYEGCLPQDFSVFGYARTKLTHEELRDMISSTLTCRIDQREKCGDKMEQFLKRCFYHSGQYNSEEDFAELNKKLKEKEAGKISNRLYYLSIPPNIFVDVVRCASLRASSENGWTRVIVEKPFGRDSESSGELTRCLKQYLTEEQIFRIDHYLGKELVENLSVLRFSNLVFEPLWSRNYIRNVQLIFSEDFGTEGRGGYFDQYGIIR... | Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis . The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis which are inv... |
P9WN70 | MVDGGGGASDLLVIFGITGDLARKMTFRALYRLERHQLLDCPILGVASDDMSVGQLVKWARESIGRTEKIDDAVFDRLAGRLSYLHGDVTDSQLYDSLAELIGSACRPLYYLEMPPALFAPIVENLANVRLLERARVAVEKPFGHDLASALELNARLRAVLGEDQILRVDHFLGKQPVVELEYLRFANQALAELWDRNSISEIHITMAEDFGVEDRGKFYDAVGALRDVVQNHLLQVLALVTMEPPVGSSADDLNDKKAEVFRAMAPLDPDRCVRGQYLGYTEVAGVASDSATETYVALRTEIDNWRWAGVPIFVRSGKE... | Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 52189
Sequence Length: 466
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate fr... |
Q9FY99 | MAALSSSVTTRSYHSGYLASFSPVNGDRHRSLSFLSASPQGLNPLDLCVRFQRKSGRASVFMQDGAIVTNSNSSESKTSLKGLKDEVLSALSQEAAKVGVESDGQSQSTVSITVVGASGDLAKKKIFPALFALYYEGCLPEHFTIFGYSRSKMTDVELRNMVSKTLTCRIDKRANCGEKMEEFLKRCFYHSGQYDSQEHFTELDKKLKEHEAGRISNRLFYLSIPPNIFVDAVKCASTSASSVNGWTRVIVEKPFGRDSETSAALTKSLKQYLEEDQIFRIDHYLGKELVENLSVLRFSNLIFEPLWSRQYIRNVQFIFS... | Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis . The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis which are inv... |
P0A585 | MKPAHAAASWRNPLRDKRDKRLPRIAGPCGMVIFGVTGDLARKKVMPAVYDLANRGLLPPTFSLVGFARRDWSTQDFGQVVYNAVQEHCRTPFRQQNWDRLAEGFRFVPGTFDDDDAFAQLAETLEKLDAERGTGGNHAFYLAIPPKSFPVVCEQLHKSGLARPQGDRWSRVVIEKPFGHDLASARELNKAVNAVFPEEAVFRIDHYLGKETVQNILALRFANQLFDPIWNAHYVDHVQITMAEDIGLGGRAGYYDGIGAARDVIQNHLMQLLALTAMEEPVSFHPAALQAEKIKVLSATRLAEPLDQTTSRGQYAAGWQ... | Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 57343
Sequence Length: 514
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate fr... |
O59812 | MLSIIVFGASGDLATKMTFPALFALYVRKIIPEDFQIIGYARSKLSQEAANKIVTAHIPIDDTVGASQKALNTFVEHYKYVPGTYDKPESFEMLNSIIAEKETAPASECTRIFYLVLPPHLFAPVSELIKSKAHPNGMVTRLIVEKPIGFDYKSADAILSDLSKHWSAKDTFKVDHFLGEDMIDGFTAIRFANSMFEPIWNREHIESVRVDFREDFGCEGRGGYFEGAGILRDVVQNHLLQLLTLLCIEEPKSQDAEDIIKCKVDFLKSLHPVSKEDIVYGQYTKSANGKVPGYRELDGVADDSEVSTFCALQLRSEAPR... | Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis (By similarity... |
Q8L743 | MSSLSCPTYRSRTSSSSPFLSNHHHSSLINVVDPRRSLSFHYASPQGLNLAELCVVRSQRRSVQSSVVVQDGSVATESSSSEEAKDVGVLTIPSLEADKVVAESDGGEQLSTVSITVVGASGDLAKKKIFPALFALYYEGCLPEHFTIFGYARSKMTDAELRVMVSKTLTCRIDKRANCGEKMEEFLKRCFYHSGQYDSQEHFVALDEKLKEHEGGRLSNRLFYLSIPPNIFVDAVKCASSSASSVNGWTRVIVEKPFGRDSKTSAALTKSLKQYLEEDQIFRIDHYLGKELVENLSVLRFSNLIFEPLWSRQYIRNVQF... | Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis . The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis which are inv... |
O14137 | MVTFMVFGASGNLANKKTFPALFHLFKRNLVDRSSFYVLGYARSKIPIGEFRESIRESVKPDTESKQVFQDFIDRVSYFSGQYDQSSSYVEFRKHLESVEKKADSSKALRIFYIALPPSVYVTVSSHIYENLYLPGKSRLVIEKPFGKNYQSAVKLKEEVHKHWKEEEIYRIDHYTAKDMVNNFFTLRFANSSSIDAVLNRHSIQSVEIHMYETGGCEGRIGYYDANGVVRDVVQNHLTQIFCIAAMNEPKSASASDVRAEKVNLLKATRPASLKESMLGQYTTSEDGKIPGYLDLEGVPKDSKATTFAASTLHVDNDRW... | Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis (By similarity... |
Q9LK23 | MGSGQWHMEKRSTLKNDSFVKEYNPVTETGSLSIIVLGASGDLAKKKTFPALFNLFHQGFLNPDEVHIFGYARSKITDEELRDKIRGYLVDEKNASKKTEALSKFLKLIKYVSGPYDSEEGFKRLDKAILEHEISKKTAEGSSRRLFYLALPPSVYPPVSKMIKAWCTNKSDLGGWTRIVVEKPFGKDLESAEQLSSQIGALFEEPQIYRIDHYLGKELVQNMLVLRFANRLFLPLWNRDNIANVQIVFREDFGTEGRGGYFDEYGIIRDIIQNHLLQVLCLVAMEKPISLKPEHIRDEKVKVLQSVIPIKDEEVVLGQY... | Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis . The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis which are inv... |
Q9FJI5 | MGSGQWHVEKRSTFRNDSFVREYGIVPETGCLSIIVLGASGDLAKKKTFPALFNLYRQGFLNPDEVHIFGYARTKISDEELRDRIRGYLVDEKNAEQAEALSKFLQLIKYVSGPYDAEEGFQRLDKAISEHEISKNSTEGSSRRLFYLALPPSVYPSVCKMIKTCCMNKSDLGGWTRIVVEKPFGKDLESAEQLSSQIGELFDESQIYRIDHYLGKELVQNMLVLRFANRFFLPLWNRDNIENVQIVFREDFGTEGRGGYFDEYGIIRDIIQNHLLQVLCLVAMEKPISLKPEHIRDEKVKVLQSVVPISDDEVVLGQYE... | Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis . The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis which are inv... |
Q43839 | MGVQLRLNPCSSSSAATSPSTFHNGTPYFCKKFNFLPFRTQPLNWVSGIYSRIQPRKHFEVFSSNGFPLNAVSVQDVQVPLTELGSGDTTVSITVIGASGDLAKKKILPALFALFYEDCLPENFVVFGYSRTKLSDEELRNMISTTLTCRIDKRENCDAKMEHFLERCFYHSGQYNSEDDFAELDYKLKEKEGCRVSNRLFYLSIPPNIFVDVVRCASLKASSTSGWTRVIVEKPFGRDLESSSELTRSLKKYLTEEQIFRIDHYLGKELVENLSVLRFSNLVFEPLWSRNYIRNVQFIFSEDFGTEGRGGYFDHYGIIR... | Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis which are invo... |
B5EBB8 | MQKQQLWERYKNLLYHDAELELSVDTSRIDFPEGFLEKMDPRLQQAYQEMEALEQGAVANPDEHRMVGHYWLRAPELAPEATLAEEITSTLAAIEAFASSVHGGNIAAPDGHRFTDLLIIGIGGSALGPQFLADSLGGPKDLLRIWFFDNTDPDGMDKVLSGIGAALKQTLVVVISKSGGTKETRNGMLEACQAFERAGLHFAGHAVAVTGSGSELDRTASRENWLGVFPMWDWVGGRTSVTSAVGLLPAALQGIDVDRLLAGARACDQKTRSRVTRENPAALLALSWFHATQGKGTRDMVLLPYKDRLLLFSRYLQQLI... | Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 58161
Sequence Length: 530
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
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Q8FR39 | MANDITTTAAWQSLTERYEAFQGTTLRELFQDGGRAEKLSFDAAGLRVDLSKNLLDDAILTDLVALAEQAGLTDRIEAMFRGEHINNTEDRAVLHTALRLPVEESLEVDGQDVAADVHEVLGRMRDFATALRSGAWLGYTGRTIKKVVNIGIGGSDLGPAMATKALRAYATAGITAEFVSNVDPADMVSVLEDLDAESTLFVIASKTFTTQETLANANAAKNWLIEQLGSEEAVSKHFVAVSTNAEKVTAFGINPENMFGFWDWVGGRYSVDSAVGLSLMAVIGPRDFMRFLGGFRAMDEHFRYTDFGQNVPVLMALLSV... | Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 59230
Sequence Length: 542
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
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Q4A5S9 | MSSSYLKLDFKLKNQVVPFESYQKQVSQIHNAVKSKSVEEKDWLGWLNLASDYNKEEYAKMEEKVAQWLKDKVEVVVVIGIGGSYLGAKTGYEFIFGKYSIKKPQMELVFAGNDISAETLVAKLNYVKDKKFAINVISKSGTTLEPSIAFREFRNLLEQKEVNSWEYIVATTDKQKGVLFELATAKKYTKFVIPDDVGGRFSVLTAVGLFPFLCAGIDAKKVLEGARQMNKELFSENVMENAAYKYAVARHYLHKEKKYAVEIFVSYEPKLRYFAEWWKQLFAESEGKDGKGLWPSSAIFSTDLHSLGQMIQDGPKILFE... | Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 48990
Sequence Length: 430
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
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A1TEQ0 | MGSDITATPAWQALSRHHDEIRAKDLRGLFADDPTRGTGFALTVGDLYIDYSKHRVTRETLDLLLDLARTAGLPAKRDAMFSGAHINTSEDRAVLHTALRLPRDASLTVDGQDVVADVHEVLDRMGDFTDRLRSGEWRGATGERITTVVNIGIGGSDLGPVMVDQALRHYADAGISARFVSNVDPADLVAKLNGLDPATTLFIIASKTFSTLETLTNATAARRWLVDGLGGSAGQDAVSKHFVAVSTNAKLVDDFGIDTANMFGFWDWVGGRYSVDSAIGLSVMAVIGRERFAEFLAGFHLVDEHFRSAPLEANAPVLLG... | Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 59595
Sequence Length: 553
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
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Q1CX51 | MTERELWERYQRYLCVVPALDFTLDVSRMRFPADYLERMRPRLEEAFGAMEALEKGAVANPDEKRKVGHYWLRAPELAPEPALQKEITDTVAAIHAFAKNVHEGRVKPQKAQRFTHMLIVGIGGSALGPQLVADALGTAKDPMQVSFFDNTDPDGFDRVLAQLGERLSETLTLVISKSGGTKETRNGMLEAERGYSARGLDFSKHAVAVTGAGSELDNHAKKQGWLRAFPMWDWVGGRTSVTSAVGLLPARLQGLDIDALLKGARDMDAATRERDALKNPAALLALMWHYAGDGRGHKDMVILPYKDRLLLMSRYLQQLV... | Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 58323
Sequence Length: 529
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
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Q2YBU4 | MITPLTQRPAWKALEAHYQTIKGMHLRQLFADDPKRGERFTAEAVGLYLDYSKNRITDETLHLLVQLAEECGLRERIEAMFRGDAINVTEQRAVLHIALRAPRNEKILVDGNDVVPGVHAVLDRMADFSDKIRSGDWQGHTGKRIRNIINIGIGGSDLGPVMAYEALRHYSLHNLSFRFISNVDGTDFVEATRGLDPEETLFIICSKTFTTTETLANAHTARRWMLRQIKDLEGVRKHFVAVSTNAEEVARFGIDTANMFEFWDWVGGRYSMDSAIGLSTMIAVGPENFREMLAGFHAMDQHFYSAPFDRNLPVLMGLLS... | Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 61372
Sequence Length: 542
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
|
Q3JCN1 | MKPYLAQARSWASLLQHYGCIKKQHMRDLFAADPQRFDKFSLIFNGILFDFSKNRITEETLKLLLDLARERELQQGISRMFAGEPINNTENRPVLHVALRNRANRPIMVKGKDVMPQVNVVLERMGKFCDRVHRGQWRGFSGERLTDIVNIGIGGSDLGPAMVTEALQPYAKSGFRVHFVSNIDGTQLAETLKTIRPETALFVISSKTFTTQETLTNAHSARNWFLRAAPDDKAIAKHFIAVSTNRSEVEKFGIDPCNMFEFWDWVGGRYSLWSAIGLSIALYLGMENFEQLLEGAHEMDKHFQETPLKQNIPVIAALVG... | Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 61868
Sequence Length: 549
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
|
Q2JX86 | MDSLQLWQRYCDWLYYHPELEIFVDISRIRFTPAQVEALRPLFARAFAEMQALEAGAIANPDEGRQVGHYWLRAPELAPTAEIRQAIQDCVEQVESFAKKIHCGTIPASGGGRFTELLWIGIGGSALGPQFVAEALAPLQPPLNIHFIDNTDPDGFDRVLGRLAGKLGQTLVVVTSKSGNTPEPRNALVEVELAYRKAGIPFSAHAVAITGPGSQLEQQARQEGWLAVFPIFDWVGGRTSETSAVGLLPAALQGIDIRALLAGAATMDKATRVPHLERNPAALLAMAWYIVGEGRGRKDMVVLPYKDRLALFSRYLQQLV... | Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Mass (Da): 58462
Sequence Length: 532
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.9
|
P22256 | MNSNKELMQRRSQAIPRGVGQIHPIFADRAENCRVWDVEGREYLDFAGGIAVLNTGHLHPKVVAAVEAQLKKLSHTCFQVLAYEPYLELCEIMNQKVPGDFAKKTLLVTTGSEAVENAVKIARAATKRSGTIAFSGAYHGRTHYTLALTGKVNPYSAGMGLMPGHVYRALYPCPLHGISEDDAIASIHRIFKNDAAPEDIAAIVIEPVQGEGGFYASSPAFMQRLRALCDEHGIMLIADEVQSGAGRTGTLFAMEQMGVAPDLTTFAKSIAGGFPLAGVTGRAEVMDAVAPGGLGGTYAGNPIACVAALEVLKVFEQENL... | Function: Pyridoxal phosphate-dependent enzyme that catalyzes transamination between primary amines and alpha-keto acids. Catalyzes the transfer of the amino group from gamma-aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA) and glutamate . Thereby functions in a GABA degradation pat... |
P80404 | MASMLLAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGPLMKTEVPGPRSQELMKQLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPALLKLIQQPQNASMFVNRPALGILPPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENALKTIFMWYRSKERGQRGFSQEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPSFDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGGDNHASDDFFRKLRDIARKHG... | Cofactor: Binds 1 [2Fe-2S] cluster per homodimer.
Function: Catalyzes the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively . Can also convert delta-aminovalerate and beta-alanine (By similarity).
Catalytic Activity: 2-oxoglutarate + 4-... |
P40829 | MTSVEQSRQLVTEIPGPVSLELAKRLNAAVPRGVGVTLPVFVTRAAGGVIEDVDGNRLIDLGSGIAVTTIGNSSPRVVDAVRAQVADFTHTCFIITPYEEYVAVTEQLNRITPGSGEKRSVLFNSGAEAVENSIKVARSYTRKPAVVAFDHAYHGRTNLTMALTAKSMPYKSGFGPFAPEIYRAPLSYPYRDGLLNKDLATDGKLAGARAINVIEKQVGADDLAAVIIEPIQGEGGFIVPAEGFLATLLDWCRKNNVMFIADEVQTGFARTGAMFACEHDGIVPDLICTAKGIADGLPLAAVTGRAEIMNAPHVSGLGGT... | Catalytic Activity: 2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate semialdehyde
Sequence Mass (Da): 47215
Sequence Length: 446
Pathway: Amino-acid degradation; 4-aminobutanoate degradation.
EC: 2.6.1.19
|
P50554 | MAFLLTTRRLVCSSQKNLHLFTPGSRYISQAAAKVDFEFDYDGPLMKTEVPGPRSQELMKQLNTIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYNHPALAKLVQQPQNASTFINRPALGILPPENFVDKLRESLMSVAPKGMCQLITMACGSCSNENAFKTIFMWYRSKERGQRGFSKEELETCMVNQSPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPSFDWPIAPFPRLKYPLEEFVTDNQQEEARCLEEVEDLIVKYRKKKRTVAGIIVEPIQSEGGDNHASDDFFRKLRDIARKHG... | Cofactor: Binds 1 [2Fe-2S] cluster per homodimer.
Function: Catalyzes the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively . Can also convert delta-aminovalerate and beta-alanine .
Catalytic Activity: 2-oxoglutarate + 4-aminobutanoate ... |
P32503 | MLRFVTKNSQDKSSDLFSICSDRGTFVAHNRVRTDFKFDNLVFNRVYGVSQKFTLVGNPTVCFNEGSSYLEGIAKKYLTLDGGLAIDNVLNELRSTCGIPGNAVASHAYNITSWRWYDNHVALLMNMLRAYHLQVLTEQGQYSAGDIPMYHDGHVKIKLPVTIDDTAGPTQFAWPSDRSTDSYPDWAQFSESFPSIDVPYLDVRPLTVTEVNFVLMMMSKWHRRTNLAIDYEAPQLADKFAYRHALTVQDADEWIEGDRTDDQFRPPSSKVMLSALRKYVNHNRLYNQFYTAAQLLAQIMMKPVPNCAEGYAWLMHDALV... | Function: Capsid protein self-assembles to form an icosahedral capsid with a T=2 symmetry, 40 nm in diameter, and consisting of 60 capsid proteins asymmetric dimers. The capsid encapsulates the genomic dsRNA and the polymerase and remains intact following cell entry to protect the dsRNA from degradation and to prevent ... |
P27400 | MGDHNLNVQELLNLFQNLGIPRQPNHREVIGLRMLGGWWGPGTRYILVSIFLQDDSGQPLQQPRWRPEGRPVNPLVHNTIEAPWGELRQAFEDLDVAEGTLRFGPLANGNWIPGDEYSMEFQPPLAQEIAQMQRDELEEILDITGQICAQVIDLVDMQDAQIRGLERRIQDRLGLRDNLPVAGIQAPPSSPIGQPIASSSLQPIPGSSSSPADLDGIWTPRQIDPRLSRVAYNPFLPGSSDGSGGSIPVQPSAPPAVLPSLPSLPAPVSQPIIQYVAQPPVPAPQAIPIQHIRAVTGNTPTNPRDIPMWLGRHSAAIEGV... | Function: Involved in capsid formation and genome binding. Shortly after infection, interaction between incoming particle-associated Gag proteins and host dynein allows centrosomal targeting of the viral genome (associated to Gag), prior to nucleus translocation and integration into host genome (By similarity).
PTM: Sp... |
Q87039 | MASGSNVEEYELDVEALVVILRDRNIGRNPLHGEIIGLRLTEGWWGQLERFQMVRLILQDEDNEPLQRPRHEIIPRAVNPHTMFVLSGPLAELQLAFQDLDLPEGPLRFGPLANGHYVEGDPYSRSYRPVTMAETAQMTRDELEDTLNTQSEIEIQMINLLELYEVETRALRRQLAERSSIGQGGISPGASHSRPPVSSFSGLPSLPAIPGIHTRAPSPPRATSTPGNIPRSLGDDNMPSSSFAGPSQPRVSFHPGNPFAEAEGHRPRSQSRERRRDIPSAPVISAPVPSAPPMIQYIPVPPPPPVGAVIPIQHIRSVTG... | Function: Involved in capsid formation and genome binding. Shortly after infection, interaction between incoming particle-associated Gag proteins and host dynein allows centrosomal targeting of the viral genome (associated to Gag), prior to nucleus translocation and integration into host genome (By similarity).
PTM: Sp... |
Q02843 | MGGGHSALSGRSLDTFEKIRLRPNGKKKYQIKHLIWAGKEMERFGLHEKLLETKEGCQKIIEVLTPLEPTGSEGLKALFNLCCVIWCIHAEQKVKDTEEAVVTVKQHYHLVDKNEKAAKKKNETTAPPGGESRNYPVVNQNNAWVHQPLSPRTLNAWVKCVEEKRWGAEVVPMFQALSEGCLSYDVNQMLNVIGDHQGALQILKEVINEEAAEWDRTHRPPAGPLPAGQLRDPTGSDIAGTTSSIQEQIEWTFNANPRIDVGAQYRKWVILGLQKVVQMYNPQKVLDIRQGPKEPFQDYVDRFYKALRAEQAPQDVKNWM... | Function: Matrix protein p17 targets Gag and Gag-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex. Implicated in the release from host cell mediated by Vpu (By similarity).
PTM... |
P22381 | MGNGNSALLGTDLDKFEKIRLKRGGKKCYRLKHLCWCKGELDRFGLSDKLLETQQGCEKILSVCWPLYDQGSDNLKALVGTVCVVACIHAGIEIKSTQDALKKLKVITRKEEKQEDESKNFPVQRDAAGQYQYTPISPRIIQTWVKTVEEKKWKPEVIPLFSALTEGAISHDLNIMLNAVGDHQGAMQVLKDVINEQAAEWDLTHPQQQPAQPGGGLRTPSGSDIAGTTSTVEEQLAWMNMQQNAINVGTIYKSWIILGMNRLVKSHCPISITDVRQGPKEAFKDYVDRFYNVMRAEQASGEVKMWMQQHLLIENANPEC... | Function: Matrix protein p17 targets Gag and Gag-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex. Implicated in the release from host cell mediated by Vpu (By similarity).
PTM... |
O81884 | MTKIELRALGNTGLKVSAVGFGASPLGSVFGPVAEDDAVATVREAFRLGINFFDTSPYYGGTLSEKMLGKGLKALQVPRSDYIVATKCGRYKEGFDFSAERVRKSIDESLERLQLDYVDILHCHDIEFGSLDQIVSETIPALQKLKQEGKTRFIGITGLPLDIFTYVLDRVPPGTVDVILSYCHYGVNDSTLLDLLPYLKSKGVGVISASPLAMGLLTEQGPPEWHPASPELKSASKAAVAHCKSKGKKITKLALQYSLANKEISSVLVGMSSVSQVEENVAAVTELESLGMDQETLSEVEAILEPVKNLTWPSGIHQN | Function: Catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). Uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Catalytic Activity: L-galactose + NAD(+) = H(+) + L-galactono-1,4-lactone + NADH
Sequence Mass (Da): 34532
Sequence Length: 319
EC: 1.1.1.316
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Q88JY0 | MGQTRIPCLLMRGGTSKGAYFLHDDLPAPGPLRDRVLLAVMGSPDARQIDGIGGADSLTSKVAIIRASQRDDADVDYLFAQVVVDEARVDYGQNCGNILAGVGPFALERGLVAASGASTPVRIFMENTGQIAVAQVPTADGQVEYAGDTRIDGVPGRAAALVVTFADVAGASCGALLPTGNSRDCVEGVEVTCIDNGMPVVLLCAEDLGVTGYEPCETLEADSALKTRLEAIRLQLGPRMNLGDVSQRNVPKMCLLSAPRNGGTVNTRSFIPHRCHASIGVFGAVSVATACLIEGSVAQGLASTSGGDRQRLAVEHPSGE... | Function: Catalyzes the tautomerization of the 4-oxalomesaconic acid keto (OMAketo) generated by GalA dioxygenase to 4-oxalomesaconic acid enol (OMAenol). Mediates the second step in gallate degradation pathway.
Catalytic Activity: (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate = 4-carboxy-2-hydroxy-cis,cis-muconate
Sequence... |
P55180 | MAILVTGGAGYIGSHTCVELLNSGYEIVVLDNLSNSSAEALNRVKEITGKDLTFYEADLLDREAVDSVFAENEIEAVIHFAGLKAVGESVAIPLKYYHNNLTGTFILCEAMEKYGVKKIVFSSSATVYGVPETSPITEDFPLGATNPYGQTKLMLEQILRDLHTADNEWSVALLRYFNPFGAHPSGRIGEDPNGIPNNLMPYVAQVAVGKLEQLSVFGNDYPTKDGTGVRDYIHVVDLAEGHVKALEKVLNSTGADAYNLGTGTGYSVLEMVKAFEKVSGKEVPYRFADRRPGDIATCFADPAKAKRELGWEAKRGLEEM... | Function: Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD (By similarity).
Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Mass (Da): 37009
Sequence Length: 339
Pat... |
E8MF10 | MTTVLVTGGAGFIATHTDIELLNKGYDVISVDNYGNSSPVALERVEQITGKPVKRYDGDVRDEALMERVFAENNIDWVIHFAGLKAVGESVAKPIEYYDNNLYSTLVLLKVMKKHNVKKIIFSSSATVYGTPKELPITEETPTGGTTNPYGTSKLFQEQILRDVHVADPSWTIVLLRYFNPVGAHESGLLGEDPKGIPANLTPYVAKVAVGELKEVQVYGDDYDTPDGTGVRDYIHVVDLAKGHVAVIDHIDKEGVFVYNLGTGHGYSVLEVIKAYEKAAGHPIPYAIKPRRPGDIAACYADASKAEKELGWKAELTIDD... | Function: Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD. Can also epimerize UDP-GalNAc to UDP-GlcNAc. Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which ... |
Q3T105 | MAEKVLVTGGAGYIGSHTVLELLEAGYSPMVIDNFHNAIRGGGSMPESLRRVQDLTGRSVEFEEMDILDQAALQRLFKKHSFMAVIHFAGLKAVGESVQKPLDYYRVNLTGTIQLLEIMRAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGCTNPYGKSKFFIEEMIRDLCQADKAWNAVLLRYFNPIGAHASGCIGEDPQGIPNNLMPYVSQVAIGRREVLNVFGNDYDTEDGTGVRDYIHVVDLAKGHIAALRKLKEQCGCRIYNLGTGTGYSVLQMVQAMEKASGKKIPYKVVARREGDVAACYANPSLALKELGW... | Function: Catalyzes two distinct but analogous reactions: the reversible epimerization of UDP-glucose to UDP-galactose and the reversible epimerization of UDP-N-acetylglucosamine to UDP-N-acetylgalactosamine. The reaction with UDP-Gal plays a critical role in the Leloir pathway of galactose catabolism in which galactos... |
Q564Q1 | MHILVTGAAGFIGSHTVLELLNSGYTVLCIDNFANAISVTDEHGNAISLKRVAQLTGKDVPFQNVDVCDEAALEKVFSENKFDGIIHLAALKAVGESVAKPLQYYSNNLVASLNLIQMCLKYNVKNFVFSSSATVYGPPSELPITEKSQTGQGITNPYGQTKYMMEQILIDVGKANPEWNVVLLRYFNPVGAHKSGLIGEDPKGVPNNLMPYVSQVAIGKLPVLTIYGDQFDTVDGTGVRDYIHVVDLAKGHVKAFDRIKTVGNIGTEIYNLGTGVGYSVRQMVDALKKVSGRDIPVKIGVPRPGDVASVYCDPSLAQEK... | Function: Catalyzes two distinct but analogous reactions: the reversible epimerization of UDP-glucose to UDP-galactose and the reversible epimerization of UDP-N-acetylglucosamine to UDP-N-acetylgalactosamine. The reaction with UDP-Gal plays a critical role in the Leloir pathway of galactose catabolism in which galactos... |
Q45291 | MKLLVTGGAGYVGSVAAAVLLEHGHDVTIIDNFSTGNREAVPADARLIEGDVNDVVEEVLSEGGFEGVVHFAARSLVGESVEKPNEYWHDNVVTALTLLDAMRAHGVNNLVFSSTAATYGEPDVVPITEDMPTQPTNAYGATKLSIDYAITSYAAAFGLAATSLRYFNVAGAYGNIGENREVETHLIPLVLQVATGHREKTFMFGDDWPTPDGTAVRDYIHILDLAKAHVLALESNEAGKHRIFNLGSGDGYSVKQVVEMCREVTGHPIPAEVAPRRAGDPATLIASSEKAKQELGWTPEHTDLRTIVEDAWAFTSALGD... | Function: Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD (Probable).
Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Mass (Da): 35263
Sequence Length: 329
Pathway:... |
Q8I136 | MLPRMLKMKTVGTVLAVIWLFGLAFIYVQSTSSSLRPPGRHPPPLPQLDPLIPQNPPQNDEIRPKKSAPPIPTINLAEDTTIHERTEKDVTWKTFDVEKFLNKGKWHQGEDKYKANSFNQEASDALNPTRKIPDSREPQCRDVDYSKVGMQPTTVIITYHNEARSSLLRTVFSVFNQSPEELLLEIVLVDDNSQDVEIGKELAQIQRITVLRNNQREGLIRSRVKGAQVARAPVLTFLDSHIECNQKWLEPLLARIAENPKAVVAPIIDVINVDNFNYVGASADLRGGFDWTLVFRWEFMNEQLRKERHAHPTAPIRSPT... | Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.
Catalytic Activity: L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[pro... |
Q8IA42 | MAIKKRYVKRLLRKVVLLLVVIVTVSLVTTLVVERRMKNAAELTEQLDPNGDPITPVFRAANIHPTRKAPRPPFQDRNSVVDIPRSDKLQGFRLPEPKGERKDWHDYAAMEADRKRSGFGEHGVAVKIENPDEKQLEKEHYEMNGFNGLISDRISVNRSVPDLRLEACKTRKYLAKLPNISVIFIFFNEHFNTLLRSIYSVINRTPPELLKQIVLVDDGSEWDVLKQPLDDYVQQHFPHLVTIVRNPERQGLIGARIAGAKVAVGQVMVFFDSHIEVNYNWLPPLIEPIAINPKISTCPMVDTISHEDFSYFSGNKDGAR... | Function: Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threoni... |
Q8N4A0 | MAVRWTWAGKSCLLLAFLTVAYIFVELLVSTFHASAGAGRARELGSRRLSDLQKNTEDLSRPLYKKPPADSRALGEWGKASKLQLNEDELKQQEELIERYAINIYLSDRISLHRHIEDKRMYECKSQKFNYRTLPTTSVIIAFYNEAWSTLLRTIHSVLETSPAVLLKEIILVDDLSDRVYLKTQLETYISNLDRVRLIRTNKREGLVRARLIGATFATGDVLTFLDCHCECNSGWLEPLLERIGRDETAVVCPVIDTIDWNTFEFYMQIGEPMIGGFDWRLTFQWHSVPKQERDRRISRIDPIRSPTMAGGLFAVSKKY... | Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a highest activity toward Muc7, EA2 and Muc2, with a lowest activity than GALNT2. Glycosylates 'Thr-57' of SELPLG.
Catalyti... |
Q95ZJ1 | MIIFKKKAILKVLLLVPVFWICSLIFFAATSNDSSQIGSNNDLANKIAEANFHPKAAKQDVIQGFGPPIEPEPVVENNKVEEEEQPGGNLAKPKFMVDPNDPIYKKGDAAQAGELGKAVVVDKTKLSTEEKAKYDKGMLNNAFNQYASDMISVHRTLPTNIDAECKTEKYNENLPRTSVIICFHNEAWSVLLRTVHSVLERTPDHLLEEVVLVDDFSDMDHTKRPLEEYMSQFGGKVKILRMEKREGLIRARLRGAAVATGEVLTYLDSHCECMEGWMEPLLDRIKRDPTTVVCPVIDVIDDNTFEYHHSKAYFTSVGGF... | Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.
Catalytic Activity: L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[pro... |
Q6WV17 | MTFSTFTRKMRGRMRSNTCRIVLLTSLVWVIFDFVLIARYSDCIGKDGWRCKRSGEYDVELPNAERLVDDNQLVDDNEINTEKSLDGESGGALIMGQGFASGGISMTYPSVVLKKWFLAPSVQEAKGKPGEMGKPVKIPADMKDLMKEKFKENQFNLLASDMISLNRSLTDVRHEGCRRKHYASKLPTTSIVIVFHNEAWTTLLRTVWSVINRSPRALLKEIILVDDASERDFLGKQLEEYVAKLPVKTFVLRTEKRSGLIRARLLGAEHVSGEVITFLDAHCECTEGWLEPLLARIVQNRRTVVCPIIDVISDETFEYI... | Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor . It can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide trans... |
Q7Z7M9 | MNRIRKFFRGSGRVLAFIFVASVIWLLFDMAALRLSFSEINTRVIKEDIVRRERIGFRVQPDQGKIFYSSIKEMKPPLRGHGKGAWGKENVRKTEESVLKVEVDLDQTQRERKMQNALGRGKVVPLWHPAHLQTLPVTPNKQKTDGRGTKPEASSHQGTPKQTTAQGAPKTSFIAAKGTQVVKISVHMGRVSLKQEPRKSHSPSSDTSKLAAERDLNVTISLSTDRPKQRSQAVANERAHPASTAVPKSGEAMALNKTKTQSKEVNANKHKANTSLPFPKFTVNSNRLRKQSINETPLGSLSKDDGARGAHGKKLNFSES... | Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward EA2 peptide substrate, but has a weak activity toward Muc2 or Muc1b substrates (By similarity).
Catalytic A... |
O61394 | MIASLIRSRRRSRRCVVYSVFLFGFLALWGSFALALVFLSDMYIGEDQISTQKAIKPIARSNYHVVVGHYNGNLPEDKKRNLTSEELNANLYAPHDDWGEGGAGVSHLTPEQQKLADSTFAVNQFNLLVSDGISVRRSLPEIRKPSCRNMTYPDNLPTTSVIIVYHNEAYSTLLRTVWSVIDRSPKELLKEIILVDDFSDREFLRYPTLDTTLKPLPTDIKIIRSKERVGLIRARMMGAQEAQGDVLTFLDSHCECTKGWLEPLLTRIKLNRKAVPCPVIDIINDNTFQYQKGIEMFRGGFNWNLQFRWYGMPTAMAKQH... | Function: Probable glycopeptide transferase involved in O-linked oligosaccharide biosynthesis. Glycopeptide transferases catalyze the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide (By similarity). In contrast to other members of the family, it does not act as a peptide transferase t... |
Q6WV16 | MRRPNLKWIVKASLLLLISLTLFVLITSWISSTPYTNKPVHHGVEPVPEKAGLSGDVKVKVPAIKQPEPQKPQEPDFEEDPELQKIDEPEPVEEEVDNPHPADDEPQQQPQEELQMAAPADASVKKDWHDYTFMEKDAKRVGLGEGGKASTLDDESQRDLEKRMSLENGFNALLSDSISVNRSVPDIRHPLCRKKEYVAKLPTVSVIIIFYNEYLSVLMRSVHSLINRSPPELMKEIILVDDHSDREYLGKELETYIAEHFKWVRVVRLPRRTGLIGARAAGARNATAEVLIFLDSHVEANYNWLPPLLEPIALNKRTAV... | Function: Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide . In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threon... |
O61397 | MIIARKKLQLQRLWRQRGCRVATYICLGVLVLFGFVYNSKGNSMSSIKSDSAAQQFDDLDDLTNKELPGGPDPNTIFRGSELGNYEPKEPEIPSNQPGEHGKPVPVTDEEGMAAGRAAEKEFGFNTYVSDMISMNRTIPDIRPEECKHWDYPEKLPTVSVVVVFHNEGWTPLLRTVHSVLLRSPPELIEQVVMVDDDSDKPHLKEKLDKYVTRFNGKVIVVRTEQREGLINARSIGAKHSTGEVVLFLDAHCEVNTNWLPPLLAPIKRNRKVMTVPVIDGIDSNSWEYRSVYGSPNAHHSGIFEWGLLYKETQITERETA... | Function: Probable glycopeptide transferase involved in O-linked oligosaccharide biosynthesis. Glycopeptide transferases catalyze the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide (By similarity). In contrast to other members of the family, it does not act as a peptide transferase t... |
Q8MV48 | MRVSTIRSGRICRLALCLLVLLPLLYLLANWSDHHKRVQEAYHTRFGGPKFAHQRLEGRPREVPKLVDGLGNFEPKDVKPRSGPGENGEAHSLSPDKKHMSDASEMEYGMNIACSDEISMHRSVRDTRLEECRHWDYPFDLPRTSVIIVFHNEGFSVLMRTVHSVIDRSPTHMLHEIILVDDFSDKENLRSQLDEYVLQFKGLVKVIRNKEREGLIRTRSRGAMEATGEVIVFLDAHCEVNTNWLPPLLAPIYRDRTVMTVPIIDGIDHKNFEYRPVYGTDNHFRGIFEWGMLYKENEVPRREQRRRAHNSEPYRSPTHA... | Function: Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide . In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threon... |
Q86SF2 | MRLKIGFILRSLLVVGSFLGLVVLWSSLTPRPDDPSPLSRMREDRDVNDPMPNRGGNGLAPGEDRFKPVVPWPHVEGVEVDLESIRRINKAKNEQEHHAGGDSQKDIMQRQYLTFKPQTFTYHDPVLRPGILGNFEPKEPEPPGVVGGPGEKAKPLVLGPEFKQAIQASIKEFGFNMVASDMISLDRSVNDLRQEECKYWHYDENLLTSSVVIVFHNEGWSTLMRTVHSVIKRTPRKYLAEIVLIDDFSNKEHLKEKLDEYIKLWNGLVKVFRNERREGLIQARSIGAQKAKLGQVLIYLDAHCEVAVNWYAPLVAPISK... | Function: Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threoni... |
P11862 | MMCTALSPKVRSGPGLSDMHQYSQWLASRHEANLLPMKEDLALWLTNLLGKEITAETFMEKLDNGALLCQLAATVQEKFKESMDANKPAKTLPLKKIPCKASAPSGSFFARDNTANFLSWCRDLGVDETCLFESEGLVLHKQPREVCLCLLELGRIAARYGVEPPGLIKLEKEIEQEETLSAPSPSPSPSSKSSGKKSTGNLLDDAVKRISEDPPCKCPTKFCVERLSQGRYRVGEKILFIRMLHNKHVMVRVGGGWETFAGYLLKHDPCRMLQISRVDGKTSPVQSKSPTLKDMNPDNYLVVSATYKAKKEIK | Function: May play a role in apoptosis by acting as a cell death substrate for caspases. Is cleaved during apoptosis and the cleaved form induces dramatic rearrangements of the actin cytoskeleton and potent changes in the shape of the affected cells. May play a role in chondrocyte proliferation and differentiation, and... |
Q9USU5 | MVSFTKFTLQLLSASAAFAYFEPLTIKGRKFFKNDTQFYIKGVAYQPAVDAEETSTIVDPLAEVNYKNCTEDAKIISNLGANVIRVYAVNASLNHDKCMEAFRNESIYVFLDLANPKTGIDRDTPTWNTDQFSSYQSVIDTFQKYNNTGAFFAGNEVVNNASNAPAVAYVRAAVRDSKNYIKSKKYRTIPVGYAGADIPVVRTELAAYLSCNATKLNNDTNSETDFLGYNMYEWCGHSDFYTSGYAARTQELENFTIPIFLSEFGCNKVTPRVFTEVQAIYSDNMTNVWSGGIVYEYSQEVNDYGLVNVSSTGERVLTTD... | Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall.
Sequence Mass (Da): 50614
Seque... |
Q06135 | MNKKQNFYAAIIVAIFLCLQLSHGSSGVSFEKTPAIKIVGNKFFDSESGEQFFIKGIAYQLQRSEEELSNANGAFETSYIDALADPKICLRDIPFLKMLGVNTLRVYAIDPTKSHDICMEALSAEGMYVLLDLSEPDISINRENPSWDVHIFERYKSVIDAMSSFPNLLGYFAGNEVTNDHTNTFASPFVKAAIRDAKEYISHSNHRKIPVGYSTNDDAMTRDNLARYFVCGDVKADFYGINMYEWCGYSTYGTSGYRERTKEFEGYPIPVFFSEFGCNLVRPRPFTEVSALYGNKMSSVWSGGLAYMYFEEENEYGVVK... | Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in spore wall assembly... |
Q03655 | MQLSKSILLAALAATPSLVNAMLPIHIKNYRFIKPSSATNSESDNEVFFVKGVDYQPGGSSGYDADSDTDILSDPEVCARDAYAFQQLGVNTVRIYSLNPDLNHDKCMTIFNNAGIYAILDVNSGNYGESLNRADPSGTYDSLYLSRVFKFIDAFKNYPNVLGFFSGNEVINDQSDYAKIDPPYIRAVQRDMKQYISKHANRSIPVGYSAADNTDLRLATFKYLQCNSLDGNKVNDDLDISKSDFFGLNTYEWCSGTSSWESSGYDKLNSTFEDAVIPLIFSEYGCNKNTPRTFDEVSEGLYGGLKNVFSGGLVYEYTEE... | Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall biosynthe... |
Q9Y7Y7 | MGVANIIYALFLLGPSIFLKATAQTHPIVIKGNAFFDSKTNERFYIRGVDYQPGGSSSLVDPLASRSCKKDVEIFKKLGINTVRVYQVDNSADHDKCMNALSEAGIYVILDLNTYRHSISRAHPALSYNKVYLQHLFATIDAFKGYDNVLGFFSGNEVVNDEDTTAITWVKAVTRDVKAYIKKHSDRHIPVGYSAADVAENRLQLAHYFNCGDESERADFYAFNMYEWCGYSSMTVSGYYDRIKEFSNYSIPLFLSEFGCNTVEINDDTTPNRPFTEIEAIYSHDMTPVFSGGLVYEYSAEPNHYGLVVIDKDDERRVSR... | Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in spore wall assembly... |
Q08271 | MMVFSSTFIFLILELVVLCEASVHTIQIKDKHFVDTVTGKPFFIKGVDYQPGGSSDVSEKQDPLSNPDACARDILLFQELGINTVRIYSINPDLNHDACMTMLAMAGIYLILDVNSPLQNQHLNRYEPWTTYNEVYLEHVFKVVEQFSHYNNTLGFFAGNEIVNDKRSAQYSPAYVKELIGTMKNYISAHSPRTIPVGYSAADDLNYRVSLSEYLECKDDDKPENSVDFYGVNSYQWCGQQTMQTSGYDTLVDAYRSYSKPVFFSEFGCNKVLPRQFQEIGYLFSEEMYSVFCGGLVYEFSQEDNNYGLVEYQEDDSVQL... | Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in spore wall assembly... |
O13692 | MNFLHFLTTSLLLLGGSRLALADSASSAIKIKGNAFFNSDTNERFYVRGVDYQPGGSSTLVDPLADTSICKRDLPYLQGLNINTIRVYQVDNSANHDECMSALQDAGIYVILDLATSSNSISRLDAASSYNAVFLQGIFATIDAFKNYTNVLGFFAGNEVANTAENSATTTWVKAALRDAKEYISKNSDRDIPVGYSAADVAEIRVQCADFFACGNSSVRADFYGMNMYEWCGADSSFTISGYDQRMEEFANYSIPLFLSEYGCNDVTKESDGTPDRPFDEVDAIFSSEMSSVFSGGLVYQYSEEGNNYGLVVIDGDNVT... | Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall.
PTM: The GPI-anchor is attached... |
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