ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q6LMF5 | MLSQAKNGASIVGEWLTKPPAPCLYDRQLVWITLSLMITGLVIVTSASVPVATRLTGIPFYFALRHAFFLVCSLVIIAGVVQVPLSRWKQFSVPMLFLSIVLLIIVLLIGRSVNGAARWIPLGIFNLQPAEVAKLSLFIFLAGYLVRQYSQVRASFIGFIKPLAVLGVLAFLLLMQPDLGSFVVMFVTTVGMLFIAGAKLWQFLVMISGALLGIGLLIVFEPYRLRRVTSFLDPWEDPFGSGYQLTQSLMAFGRGELMGQGLGNSIQKLEYLPEAHTDFVFAVLGEELGLIGVTVVLLLIFALVFKALFIGRKCLQSGQLFGGFLACGFSFWFAFQTLVNVGAAIGMVPTKGLTLPLISYGGSSLFIMATAVGILLRIDHEQRLFAKYGPAESEELDDSGLNDSNNNDEQE | 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 = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44892
Sequence Length: 411
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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Q15Q16 | MNTSTFATPLRAMFAQRHDAAPAVVRPYDVSLILLALSLMAIGLVIVTSASMPVASRLFDNPFHFAIRHGIYIVLAIGAALTVMQIPMQWWRTSNAWLLLLGLVLLIAVLLVGRSVNGSTRWLAIGPITIQAAEPAKLFFFCYLAGYLVRRYEEVTENIKGFAKPLVVFFAFAVLLLLQPDLGTVVVMLCTTIGLLFLAGAKLWQFFGLAFTGGAAVTFLIMFEEYRMKRITSFLDPWADPFGSGYQLTQSLMAYGRGDVFGQGLGNSLQKLEYLPEAHTDFIMAILAEELGFAGVLTVLALMLCIVLKAMKMGSKALQNERPFDAYLAYSIGIWFSFQTAVNVGASAGILPTKGLTFPLLSYGGSSLIIMAAAVGLLVRIDFEMRVEGIQAIDRSGKAKASTSSSRKNKPKTASSAGKKKVSTVLDDVAYAVVDDVQDEEQDIDSIMDDFAQDESAQTVSHQTKRASKSTSKTPRGKDEEQEDGYV | 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 = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53074
Sequence Length: 487
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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C3KCS9 | MSIDFRNIIKPYPSPIITGRGIDLDFPMLAGCLALLGLGLVMITSASSEVAAVQSGNTLYMMIRHLVYLVIGLGACIVTMMIPIATWQRLGWLMLIGAFGLLIMVILPGIGREVNGSMRWIGFGAFNVQPSEIAKVFVVIYLAGYLVRRQKEVRESWMGFFKPFIVLLPMAGLLLMEPDFGATVVMMGAAAAMLFLGGVGLFRFTLMVVLAVAAVTVLVQAQPYRMARLITFTDPWSDQFGSGYQLTQALIAFGRGEWLGVGLGNSVQKQFYLPEAHTDFVFSVLAEELGVVGSLCTVALFVFVCVRGMYIGMWAEKAKQYFAAYVAYGLSFLWIGQFLINIGVNVGLLPTKGLTLPFLSYGGSSLVICCACLGLLLRIEWESRTHLGSEEMEFSESDFAEEPTHGR | 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 = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44552
Sequence Length: 407
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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D4G8R2 | MKKSHLYNRSLLSVTIILLIFSIIMVGSSSVSVGNRIRTDYLSFLKKNFIHSIISILCMIFVFNVPIYKWKKNKNKLILCSIILLLTLNYFGISNHGAKRWINIKIAFIQPSELVKISFSCYLSSYLSEKNKKTSTIQLISIILIVSKLLLSQPDFGTLVILYSSLLFMLFLIGKNFLFLSASSAIFTTIVLSLIYFRSYRAKRLISFLNPWSNYLGDGYQLVHSMLSFGRGKMFGQGIGNSIQKINFLPEPHTDFIISIIGEELGYLGIAMIVISLFFIFFQGMNIGRNALKDFQYFSGFLAYSISLLIIIQSIINIGSSIGILPIKGTTLPIISYGGSSKLITCIKIAILLRIDFETKMNKIQAFRR | 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 = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41733
Sequence Length: 369
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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Q21MH0 | MIVNIASPLYGSVQGFRRLDFSLYATVAILISVGIVMVASSSLDFAAERYHDTWFFVRKQITFLAMGLVGGLVILAVPMSVWNKYSGLLLILAFFLLMAVLIPGIGKVVNGSRRWLSLGPFSMQASEIAKFCLIVYFASYLARRNEELRTQWSGFLKLTAVLLIIVLLLLLEPDFGSSVVISATLGCMMFVAGVPLARFLLLAVSGVAGLALMAVASPYRWERLVAFMDPWATQFDSGYQLVQSLIAFGRGGWFGVGLGNSLQKLFFLPEAHTDFIFAIFTEEFGFIGAIALIGVFGFFLYRLVILFRRASEQEQFFSSYVVFGIGVMLAMQAFINMGVASGFLPTKGLTLPFISYGGSSLLITCGLMALVFRVNLELNRENQEGKP | 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 = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42562
Sequence Length: 387
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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A8FQ99 | MRSEERQLNLFGTSVNWSWPNLFKEREAPGMQLYDRALLFAVLSLICFGFVMVMSASMPEAQSLTGNPYHFAIRHFAYLVGCAVIAAVVLRIEMSRWQQFSPLLLLIVGIMLVAVLLVGTSVNGATRWLSVGPIRIQVAELAKFAFTIYMAGYLVRRHQEIRENAKGFYKPIAVFAVYAFLILMQPDLGTVVVLFVGTVGLLFLAGARLLDFFALILTGVMAFVALVLLEPYRMRRVTSFMDPWQDPFGSGYQLTQSLMAYGRGDWFGQGLGNSIQKLEYLPEAHTDFIFAVIGEELGFIGIVVVLSVLLFVALRAIKLGNLCIEIDKPFEGYLAYAIGIWFCFQTVVNVGASIGMLPTKGLTLPFISYGGSSLWVMTAAAMILIRIDHERRLSSIQAVQGKKVNDNREY | 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 = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45693
Sequence Length: 410
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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P74180 | MITAANLLRIIFPFYDPEVLRWSGEARLMRTLFFAWMAMGVVVLFSASYAESLDTSGTGLSIILKQIAYLWLGLNIFNFLVRLPLQVCLKLVPWFLIVVLLLIFLTKSGLGVEVNGARRWISLGPILIQPSEFMKPCLVLQAANLFGNWHRFPWRSRLIWLGIFALTLGSILLQPNLSTTALCGMGLWLIALASGLPWIYLISTALLGITTAVTSISIRDYQRARVTSFLDPFADPRGDGYQLVQSLYAIASGGVLGRGFGMSQQKLFYLPIQTTDFIFAVFAEEFGLVGCITFLAFLGLFTTMGLRVAMRCRHRVKRLIGLGVVIFLVGQSLLNIGVASGALPTTGLPLPFFSYGGSSCLSSLVLAGLLVRVARESNEAEVIPLGTKTAPAV | 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 = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43038
Sequence Length: 393
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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E8UEF9 | MGLIMVFSSSIALGDGPKYVNAGRYYFFSRQLIFILIGLFAMAFTFLMPMKFWDSKAFWGYCICFLLLALVLVPGIGREVNYAYRWIPIGPFNFQPSEFAKLTMIVFTSAYTVRKQKSIHGLKGFLPIIIYLGIICFLLINEPDLGATMVVVAIVMSILLLGGLGFALFSLLFLSAVLLVIAAILTAPWRMQRFFAYLDPFSQEHAQNTGYQLTHSLIAVGRGGFFGEGLGLSIEKLHYLPEAHTDFIMAVVGEELGFVGIFFVILLFVLLVRKGLNVGRQAIAMDRLFNGLVAQGVVVWFGVQAIVNLGVCFGVFPTKGLTLPFISYGGSSIVISLMAFGLLLRVDYENRCLMRGQKPLGIGASYA | 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 = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40512
Sequence Length: 367
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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D5X4H4 | MLERMLPFLGRKRDKAAADLPVRVGHSAPRNSRMLEYDQNLVWVTLLLLAYGLVMVYSATISFHDSPRYAQWSPYHYFIRDLFSIAAALLASWIVVQIPMAELQKWSMRFFFLSLIGLVLVLLPHIGKDVNGSKRWVVFPGGLNFQPSELVKLTALIYAADFMVRKQEVKQSLLKTFLPMMAVMMIVGVLLLAEPDMGAFLVIASITLAILFLGGANGKLFSVFSVAVIGAFVLMIVLSPWRRDRIFAYLNPWSESNALGSAYQLSHALIAMGRGEWFGVGLGGSIEKLHYLPEAHTDFLLAIIGEELGLVGVGVVIFAFYWIVRRAFDIGRQALVLDRMYSALVAQGIGVWIGGQAFINIGVNLGLLPTKGLTLPLMSYGGSALLLNCMAIAVLLRVDFENRILMRGGHV | 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 = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45509
Sequence Length: 411
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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D3SD93 | MSTGSLPLGLPSRDSLDGLRNSVDLPLLAAAALLLGLGLIMVASASMDLGERYYGNTWHFFQRQVLFAAIGLALATVMWAIPLERWERAGPWLLILVMVLLIAVLLPGVGRTVNGATRWIPIGMFNLQVAEPVKLLVVMYLAGYIVRHYSALRLHLRGFVRPLVVLGFGTVLLLLQPDFGGAAIMLAIGMGMLFLAGAKLWQFAALGATIAVGMAFVAVAAPYRVARLTAFLDPWQDPFATGFQLTQSLIAIGSGGWFGTGLGNSVQKLFYLPEAHNDFLFAVFAEEFGFIGVLALIALFAVVVWRCVKIGLWAERAGHAFGSHLAFGVAIWLALQSALNLAVNMGLLPTKGMTLPFLSYGGSSLIVTLMAIGLVMRVYREAQIPAPRQSTPPRRKRGQA | 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 = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43131
Sequence Length: 400
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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E6UUM7 | MNSAAAGATPNTRTSRFGGWFRRARSGIDSLPVHLPVRLGGAGIAQTKATPMRVLGFDQALVWVTVALLTWGLVMVYSASIALPDNPRFARAGYGASFFLTRHAASVAFAFIAALLAFQIPMKTWERAAPWLFVVSLLLLVAVLIPHIGISVNGARRWLPMGFMRFQPSELAKVAMVLYAASYMVRKMEIKERFFRAVLPMGIAVVVVGMLVMAEPDMGAFMVIAVIAMGILFLGGVNARMFFVIAALVVVAFGTIVASSPWRRERIFAYLDPWSEEHALGKGYQLSHSLIAIGRGEIFGVGLGGSVEKLHWLPEAHTDFLLAVIGEEFGLVGVLLIIGLFLWLTRRVMHIGRQAIALDRVFSGLVAQGVGVWLGFQTFINMGVNLGALPTKGLTLPLMSFGGSAILMNMIALAIVLRIDYENRVLMRGGRV | 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 = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46972
Sequence Length: 432
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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Q8D2Z5 | MNNKKKIVKIFFYDKILFFLLISLSIIGIIIVSSASISFGIRLHNDYFYFAKRNLLYFFLSFFLFFQIIRIPINQLEKYNKIALLINLFLLIIVFIIGNSINGAIRWIKIGFFSIQPSECSKLILFFYISDYIVKKNKELKNKLWGFLKPIIIMLIFVILLLMQPDLGNSLILFLTTLLLFFLAGINLWKCCFMFLFGLLTIFILIIFKPYRIRRILSFLDPWEDPFNSGYQLTQSLMALGRGKIIGTGLGNSIQKLEYLPEAYTDFIFSILGEELGYIGSIIILIMLFFVIFRIFLIGKNSFIQKKFFSGYFSFSVGIWISLQTIMNVGGVIGILPIKGLTLPFISYGGSSLITIFSAIAIVIRSDFELRINKYQAYLKQ | 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 = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44051
Sequence Length: 381
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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Q8P3K2 | MRTIIALETHDVRFPTSRELDGSDAMNPDPDYSAAYVVLRTDGAEDLAGYGLVFTIGRGNDVQTAAVAALAEHVVGLSVDKVIADLGAFARRLTNDSQLRWLGPEKGVMHMAIGAVINAAWDLAARAANKPLWRFIAELTPEQLVDTIDFRYLSDALTRDEALAILRDAQPQRAARTATLIEQGYPAYTTSPGWLGYSDEKLVRLAKEAVADGFRTIKLKVGANVQDDIRRCRLARAAIGPDIAMAVDANQRWDVGPAIDWMRQLAEFDIAWIEEPTSPDDVLGHAAIRQGITPVPVSTGEHTQNRVVFKQLLQAGAVDLIQIDAARVGGVNENLAILLLAAKFGVRVFPHAGGVGLCELVQHLAMADFVAITGKMEDRAIEFVDHLHQHFLDPVRIQHGRYLAPEVPGFSAEMHPASIAEFSYPDGRFWVEDLAASKAKA | 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 with 15-fold lower activity observed for L-galactonate and 8-fold lower activity with D-arabinonate. No activity detected with D-fuconate. Can also catalyze the epimerization of L-talonate and D-ribonate, but at slow rates.
Catalytic Activity: L-fuconate = 2-dehydro-3-deoxy-L-fuconate + H2O
Sequence Mass (Da): 48124
Sequence Length: 441
EC: 4.2.1.68
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Q8XNL5 | MKTYPKIGIRPTIDGRQGGVRESLEEKAMKMAQAAKKLIENSLYYADGTPVQCVLASRTIGGSGDAGIVQQEFTGKNIVATLSVTPSWCYGTETMDLDPNTIKAIWGFNGTERPGAVYLAAAMSGYAQKGIPAFKIYGHDVQELDDDTIPVDVQEKILSFARGAIAVGQMKGKSYVNIGASSMGIAGSQVDISFFEDYLGMLVEFVDMTEILRRIHLEIFDPIEYDKALNWIKENCREGIDINEGKDLPDIVKKSKVIPADKDWEFIAKQAIIIRDILYRNEKLGDLGWEEEARGRNAIAGGFQGQRQWTDWLPNGDFTEAIMASTFDWNGPRQVTAFATENDTLNGVSMLLGTLLTNKAPIFSDVRTYWSPESVKRVTGKELTGKAKNGIIHLINSGASALDGTAAAKDKDGNKTMKEFWNMTNEDVQSCLKATDWCRANYEYFRGGGFSSHFKTEAELPVTLIRVNLIKGIGPTLQIAEGYTCVIDEDIHQILDERTDKTWPTTWFAPNLGECGFETVYDVMNHWGANHGAFVHGHIGSDLITLASMLRIPVTLHNVPRERIFRPNIFEGAGTKALETADFEICRLLGPLYKK | 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: Cytoplasm
EC: 5.3.1.25
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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 | MNSQITLFFFFFSILSLSQISNSSSLLKPHPCPILPLPSSQQLQWQLGSMAMFLHFGPNTFTDSEWGTGKANPSIFNPTHLNASQWVQIAKDSGFSRVILTAKHHDGFCLWPSEYTDYSVKSSQWRNGAGDVVAELASAAKEAGIGLGLYLSPWDRHEQCYGKTLEYNEFYLSQMTELLTKYGEIKEVWLDGAKGDGEKDMEYFFDTWFSLIHQLQPKAVIFSDAGPDVRWIGDEAGLAGSTCWSLFNRTNAKIGDTEPSYSQEGDGYGQDWVPAECDVSIRPGWFWHASESPKPAVQLLDIYYNSVGRNCLFLLNVPPNSSGLISEQDIKVLEEFSEMKNSIFSNNLARKAFVNSSSIRGDQSSQFGPKNVLEEGLDKYWAPEENQNEWVLYLEFKDLVSFNVLEIREPIHMGQRIASFHLETRKTGSGEWERVVSGTTVGNKRLLRFLNVVESRSLKLVVDKARTDPLISYLGLYMDKFSGSSRNTTKITITRTLKEEQQLHDL | 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
EC: 3.2.1.51
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Q7XUR3 | MATILLLLLGLLVGLPLLRAHGVTGSAAPTPPPLPVLPVPSYAQLQWQLSEMALFLHFGPNTFTDSEWGSVRADPAVFAPSALDAGQWARAAAAGGFGRVVLTAKHHDGFCLWPSALTNYSVAASPWKGGAGDVVGELAAAARAEGIGLGLYLSPWDRHEPVYGDTVAYNEHYLGQMTELLTRYGDVEEVWLDGAKGEGKDMDYMFDAWFALIHQLQQRVVIFSDAGPDTRWVGDEAGVAGYTCWSPFNKSTVTIGHIIPEYSRCGDPFGQDWVPAECDVSIRPGWFWHASEKPKNATTLLDIYYKSVGRNCLLILNVPPNSSGLISTEDMQVLQEFTEIRQTIFSQNFAANATVTASTVRGGLGNQQFAPSNVLQESIYSYWAPEEGQSSWEMLFDLGQSASFNVIQLQEPIQMGQRVIKFRVEILVDELWQTIVEGTTIGYKRLFQFPVVEGQFLKLSIDGARADPLISFFGVFTDSFSVTYSLENHEKPSVVNSSEVIMLRTDHSFGNKSIATM | 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-fucose
Sequence Mass (Da): 56792
Sequence Length: 517
Subcellular Location: Secreted
EC: 3.2.1.51
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Q8L7W8 | MAEKSSFFVHFSCLLLLLTIIITCGEGVRNPVRPRSSERRALMDGQDLSRPLKLTFGGPSRNWTDAIPIGNGRLGATIWGGVSSEILNINEDTIWTGVPADYTNQKAPEALAEVRRLVDERNYAEATSEAVKLSGQPSDVYQIVGDLNLEFDSSHRKYTQASYRRELDLETAVAKVSYSVGAVDFSREFFASNPDQVIIAKIYASKPGSLSFKVSFDSELHHHSETNPKANQILMRGSCRPKRLPVNLKKSINATNIPYDDHKGLQFASILEVRVSNGGSVSSLGGKKLSVEKADWAVLLLAASSNFDGPFTMPVDSKIDPAKECVNRISSVQKYSYSDLYARHLGDYQKLFNRVSLHLSGSSTNETVQQATSTAERVRSFKTDQDPSLVELLFQYGRYLLISSSRPGTQVANLQGIWNRDIQPPWDGAPHLNINLQMNYWHSLPGNIRECQEPLFDYMSALAINGRKTAQVNYGASGWVAHQVSDIWAKTSPDRGEAVWALWPMGGAWLCTHAWEHYTYTMDKEFLKKKGYPLLEGCTSFLLDWLIKGKDGFLQTNPSTSPEHMFTAPIGKPASVSYSSTMDIAIIKEVFADIVSASEILGKTNDTLIGKVIAAQAKLPPTRISKDGSIREWAEDFEDPEVHHRHVSHLFGLFPGHTITVEKSPELAKAVEATLKKRGEEGPGWSTTWKAALWARLHNSEHAYRMVTHIFDLVDPLNERNYEGGLYSNMFTAHPPFQIDANFGFAAAVAEMLVQSTTKDLYLLPALPADKWPNGIVNGLRARGGVTVSIKWMEGNLVEFGLWSEQIVSTRIVYRGISAAAELLPGKVFTFDKDLRCIRTDKL | 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 Activity: an alpha-L-fucoside + H2O = an alcohol + L-fucose
Sequence Mass (Da): 93725
Sequence Length: 843
Subcellular Location: Secreted
EC: 3.2.1.51
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Q9BTY2 | MRPQELPRLAFPLLLLLLLLLPPPPCPAHSATRFDPTWESLDARQLPAWFDQAKFGIFIHWGVFSVPSFGSEWFWWYWQKEKIPKYVEFMKDNYPPSFKYEDFGPLFTAKFFNANQWADIFQASGAKYIVLTSKHHEGFTLWGSEYSWNWNAIDEGPKRDIVKELEVAIRNRTDLRFGLYYSLFEWFHPLFLEDESSSFHKRQFPVSKTLPELYELVNNYQPEVLWSDGDGGAPDQYWNSTGFLAWLYNESPVRGTVVTNDRWGAGSICKHGGFYTCSDRYNPGHLLPHKWENCMTIDKLSWGYRREAGISDYLTIEELVKQLVETVSCGGNLLMNIGPTLDGTISVVFEERLRQMGSWLKVNGEAIYETHTWRSQNDTVTPDVWYTSKPKEKLVYAIFLKWPTSGQLFLGHPKAILGATEVKLLGHGQPLNWISLEQNGIMVELPQLTIHQMPCKWGWALALTNVI | 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: Secreted
EC: 3.2.1.51
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Q10279 | MESVDNNSFFSRIRNSNAYRKVKDFVILDHRPGMTMAERMLTNKDLYPVPPSKRLWGPWNFISFWLADAVNINTWMISATAIELGLNWWEAWICVWVGYLICGILVATTGRPGAVYHISFPVLSRSSFGTWGSLWPILNRSVLACVWYGVQAWIGGECVVLMIRSIWPSFSHIPNTMAKSGTETYQWVGFFIFWLLSNIAIWFPVHQIRHLFTFKAIVAPPAAIAFLIWALVKAHGAGPVIHEPTKLGQYEHAWVVINGIVTCIDGFATLIVNNPDFARFATTPGAVHWPQIITVPLAFGVTSLIGVLVSSASKAIYGTTLWDPTQLLASFLDHSNAHGVRAGVFFIAFGLCIAQLGVNIAANSVSAGNDLSALLPTVINVRRGGYIASIIALCMCPWNLLSSNNNFTTYLSSYSVFLSSFAGVIIADYYFVRKGLIRVAPLYSSSSSSPYYFWKGINFRAFASYICGMLINIVGMAGSTGQKVPKVANTMFNLNYFLGITVACLSHIIICKIFPVTECGEKMLSEVPEEADDYLLTLASEDSIDKDSTSEIYIDGLPTEKEVEKDDVLSITSKKLSGCFP | 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 | MPDNLSLHLSGSSKRLNSRQLMESSNETFAPNNVDLEKEYKSSQSNITTEVYEASSFEEKVSSEKPQYSSFWKKIYYEYVVVDKSILGVSILDSFMYNQDLKPVEKERRVWSWYNYCYFWLAECFNINTWQIAATGLQLGLNWWQCWITIWIGYGFVGAFVVLASRVGSAYHLSFPISSRASFGIFFSLWPVINRVVMAIVWYSVQAYIAATPVSLMLKSIFGKDLQDKIPDHFGSPNATTYEFMCFFIFWAASLPFLLVPPHKIRHLFTVKAVLVPFASFGFLIWAIRRAHGRIALGSLTDVQPHGSAFSWAFLRSLMGCMANFSTMVINAPDFSRFSKNPNSALWSQLVCIPFLFSITCLIGILVTAAGYEIYGINYWSPLDVLEKFLQTTYNKGTRAGVFLISFVFAVAQLGTNISANSLSCGTDMSAIFPKFINIKRGSLFCAAMALCICPWNLMATSSKFTMALSAYAIFLSSIAGVVCSDYFVVRRGYIKLTHIYSHQKGSFYMYGNRFGINWRALAAYLCGVAPCLPGFIAEVGAPAIKVSDGAMKLYYLSYWVGYGLSFSSYTALCYFFPVPGCPVNNIIKDKGWFQRWANVDDFEEEWKDTIERDDLVDDNISVYEHEHEKTFI | 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 can also use DMAPP as prenyl donor.
Catalytic Activity: (2E)-geranyl diphosphate + 2-O,3-dimethylflaviolin = 6-linalyl-2-O,3-dimethylflaviolin + diphosphate
Sequence Mass (Da): 34248
Sequence Length: 307
EC: 2.5.1.124
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Q75W17 | MATITTLASSVPLFRPYSFPGGSSRKPKKDNLSIKPPATSSLKVNAKLASADDTSSNFNKDNWLASADELSRSFPPGFLFGGGSASYQYEGAVKEGGRTPSIWDTFAHEFPDKIADGSNGDVAVDFYHRYKDDVKLMKKIGVNGFRFSISWTRILPSGKLCGGVNKEGVAFYNSLINELLANGIEPFVTIFHWDLPQGLENEYDGFLSGQIVNDYRDYAEVCFQEFGDRVKFWTTLNEPWTFCYNGYVNGSFAPGRCSTCTAGNSGTEPYLVAHNLLLSHAAVAQLYKNKYQASQKGQIGIVLVCFWMVPYSDCPYDCEAAQRALDFMLGWFLHPLTYGDYPESMRHLVGERLPQFTEMQAMMMKGSIDFLGLNYYTSIYAANNESPNPHDISYTTDSRVNLFQKRDGILIGPATGTPAFCFCPEGIRDLLVYTKEKYNNPIIYITECGLAEANINTVDQGVKDVERVEFYYEHLKFLRSAIKKGVNVKGFFTWSLLDDWEWNSGFNVRFGIVYIDHEDGLKRYLKYSALWFKKLFGK | 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.
Catalytic Activity: 7-[beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranosyloxy]isoflavonoid + H2O = a 7-hydroxyisoflavonoid + beta-D-apiofuranosyl-(1->6)-D-glucose.
Sequence Mass (Da): 60626
Sequence Length: 538
Subcellular Location: Plastid
EC: 3.2.1.161
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P09958 | MELRPWLLWVVAATGTLVLLAADAQGQKVFTNTWAVRIPGGPAVANSVARKHGFLNLGQIFGDYYHFWHRGVTKRSLSPHRPRHSRLQREPQVQWLEQQVAKRRTKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIDILTEPKDIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEANNYGTLTKFTLVLYGTAPEGLPVPPESSGCKTLTSSQACVVCEEGFSLHQKSCVQHCPPGFAPQVLDTHYSTENDVETIRASVCAPCHASCATCQGPALTDCLSCPSHASLDPVEQTCSRQSQSSRESPPQQQPPRLPPEVEAGQRLRAGLLPSHLPEVVAGLSCAFIVLVFVTVFLVLQLRSGFSFRGVKVYTMDRGLISYKGLPPEAWQEECPSDSEEDEGRGERTAFIKDQSAL | 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 factor prohormone into its active hormone BNP(1-32) . By mediating processing of accessory subunit ATP6AP1/Ac45 of the V-ATPase, regulates the acidification of dense-core secretory granules in islets of Langerhans cells (By similarity).
Catalytic Activity: Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors.
PTM: The inhibition peptide, which plays the role of an intramolecular chaperone, is autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound to furin as a potent autoinhibitor. Following transport to the trans Golgi, a second cleavage within the inhibition propeptide results in propeptide dissociation and furin activation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 86678
Sequence Length: 794
Domain: Contains a cytoplasmic domain responsible for its TGN localization and recycling from the cell surface.
Subcellular Location: Golgi apparatus
EC: 3.4.21.75
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P61154 | MVKVVRNVVCPFCGTLCDDLEILVEDNHIVGTRHACRIGNAKFMHFEGAVRYTEPLMRENKKDDFKKVDYETAIEETARLLTEATLPLIYGWSATECHAHMYGVELAELVGAVIDNTASVUHGPSLLAVQDVGYPVCTLGEVKNRADVIIFWGSNPMHAHPRHMSRYSVFARGFFRERGREDRTLIVVDPRETDTAKLADIHLQVEPHKDYELVSAMRAVLKGFELQVDKVAGVPADLIYEAVEVCKNAQFGELFFAMGVTMTRGKHRNIDNAIQLVIDLNAYTKFGLMPMRGHYNVNGFNQVLTWVTGYPFGVDFSRGYPRYNPGETTANDLLQRGETDMMLNIASDPGAHFPQKAVQHMAKIPLVCIDPHETPTTQLANIIIPPAIAGVEVEGTAYRMDGVPIQLRKVIDPPEGVLPDREILKILIKKVKEML | 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 Length: 435
Pathway: One-carbon metabolism; methanogenesis from CO(2); 5,10-methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 1/3.
EC: 1.2.7.12
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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 Length: 273
Pathway: One-carbon metabolism; methanogenesis from CO(2); 5,10-methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 1/3.
EC: 1.2.7.12
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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]-[ferredoxin]
Sequence Mass (Da): 28641
Sequence Length: 270
Pathway: One-carbon metabolism; methanogenesis from CO(2); 5,10-methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 1/3.
EC: 1.2.7.12
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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(+) + methanofuran + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 8345
Sequence Length: 79
Pathway: One-carbon metabolism; methanogenesis from CO(2); 5,10-methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 1/3.
EC: 1.2.7.12
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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-activated chloride current when expressed in Xenopus oocytes .
PTM: Glutathionylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 9263
Sequence Length: 87
Subcellular Location: Cell membrane
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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 hyperpolarization-activated chloride current when expressed in Xenopus oocytes (By similarity).
PTM: Glutathionylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 9526
Sequence Length: 88
Subcellular Location: Cell membrane
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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-activated chloride current when expressed in Xenopus oocytes.
PTM: Glutathionylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 9411
Sequence Length: 88
Subcellular Location: Cell membrane
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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: NAD(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 33618
Sequence Length: 314
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.261
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Q2FPC7 | MSTDPVQVLQPDGFNKSRWTQLPRDVLIGHQAIMQLPDIIADIKPGRSVLLISGGTTREVAGNTVADILKDQYEVRRFVAGKLDADTLEACSQASSSADFLIGVGGGRVIDCAKIVSYKQGKPFISVPTAASHDGIISGRATLPTETGSVSVGAHPPIAVVADTGIISQAPHRLMASGCADVISNYTAILDWELAHRLRGEQISEYAIALSKMTAEILVKDANLIKPGQEEAAWIVVKALVSSGVSMAIAGSSRPASGGEHKFGHALERLMPGAALHGEACGIGSIMTMYLHGGDWREIRSSLARIGAPTTPRELNIPDEVIVEALMKARDIRPERFTILDMGLTRESAEHLVQMLYEE | 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: NAD(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 38362
Sequence Length: 359
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.261
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Q58122 | MIIVTPRYTIIEDGAINKIEEILKKLNLKNPLVITGKNTKKYCRFFYDIVYYDEILNNLEIELKKYTAYDCVIGIGGGRSIDTGKYLAYKLGIPFISVPTTASNDGIASPIVSIRQPSFMVDAPIAIIADTEIIKKSPRRLLSAGMGDIVSNITAVLDWKLAYKEKGEKYSESSAIFSKTIAKELISYVLNSDLSEYHNKLVKALVGSGIAIAIANSSRPASGSEHLFSHALDKLKEEYNLNINSLHGEQCGIGTIMMSYLHEKENKKLSGLHEKIKMSLKKVDAPTTAKELGFDEDIIIEALTMAHKIRNRWTILRDGLSREEARKLAEETGVI | 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: NAD(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 37275
Sequence Length: 335
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.261
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Q8TW08 | MSVPKKRMQLPREVVVGSNVLPEVPKLLRSVGVPDGVVAVFSGRTTMKIAGNEVADHLEEAGYQTSPVIVKGSTGDDVKKALEALDEIDADVVAAVGGGKVIDVAKVASYRRGIPFISVPTSASHDGIASPFASIRREGRPYSEPAQAPLAILADIEVIREAPERLIRAGVGDVVSNVTAVKDWRLAHRLRNEPYSEYASSLSLMAARIVMKNAKPIGKLLPEGIKKLVQALISGGVAMSIAGSSRPCSGSEHLFSHALDVIAERPALHGEQCGVGTIIMEYLHGGNWREIRETLETAGAPTTAEDLGVSDEEIIEALCRAHKIRPDRYTILGDKGLTREAAERAAEETGVIQ | 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: NAD(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 37642
Sequence Length: 353
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.261
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Q5HF86 | MSTNIAINGMGRIGRMVLRIALQNKNLNVVAINASYPPETIAHLINYDTTHGKYNLKVEPIENGLQVGDHKIKLVADRNPENLPWKELDIDIAIDATGKFNHGDKAIAHIKAGAKKVLLTGPSKGGHVQMVVKGVNDNQLDIEAFDIFSNASCTTNCIGPVAKVLNNQFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPELEGKLHGMALRVPTKNVSLVDLVVDLEKEVTAEEVNQAFENAGLEGIIEVEHQPLVSVDFNTNPNSAIIDAKSTMVMSGNKVKVIAWYDNEWGYSNRVVDVAEQIGALLTSKETVSAS | 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, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
Catalytic Activity: D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH
Sequence Mass (Da): 36979
Sequence Length: 341
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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Q8CNY0 | MATNIAINGMGRIGRMVLRIALNNKNLNVKAINASYPPETIAHLLNYDTTHGVYDKKVEPIESGIKVNGHEIKLLSDRNPENLPWNEMDIDVVIEATGKFNHGDKAVAHINAGAKKVLLTGPSKGGDVQMIVKGVNDNQLDIDTYDIFSNASCTTNCIGPVAKVLNDKFGIINGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTKNVSLVDLVVDLEQNVTVTQVNDAFKNADLSGVLDVEEAPLVSVDFNTNPHSAIIDSQSTMVMGQNKVKVIAWYDNEWGYSNRVVEVAVKIGQLIDDKAMVKAI | 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, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
Catalytic Activity: D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH
Sequence Mass (Da): 37092
Sequence Length: 341
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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Q829W3 | MTIRVGINGFGRIGRNYFRALLEQGADIEIVAVNDLGDTATTAHLLKYDTILGRLKAEVTHTADTITVDGKTIKVFSERNPADIPWGELNVDIVIESTGIFTKKADAEKHIAGGAKKVLISAPASDEDITIVLGVNEDKYDPAKHNVISNASCTTNCVAPMAKVLDENFGIVKGLMTTIHAYTNDQRILDFPHKDLRRARAAAENIIPTTTGAAKATALVLPQLKGKMDGISMRVPVPTGSATDLVVEVSREVTKDEVNAAFKKAAEGELQGYLSYTEDPIVSSDIVGDPSSCTFDSAMTMVMEGTSVKILGWYDNEWGYSNRLVDLTVFVGNQL | 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, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
Catalytic Activity: D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH
Sequence Mass (Da): 36162
Sequence Length: 335
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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P00358 | MVRVAINGFGRIGRLVMRIALQRKNVEVVALNDPFISNDYSAYMFKYDSTHGRYAGEVSHDDKHIIVDGHKIATFQERDPANLPWASLNIDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAPLAKVINDAFGIEEGLMTTVHSMTATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSNSSIFDAAAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVAKA | 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 | MKSIGINGYGTIGKRVADAVSAQDDMKIVGVTKRTPDYEAKAAVEKGYDLYISVPERESQFEEAGIEVAGTADELFEKLDLVVDCTPGGIGAQNKTDIYEKIGLKAIFEGGEDHDAIGSSFNAEANYADNIGEDYVRVVSCNTTGLCRTLKPIYDISGIKKVRAVMVRRGADPSDVKKGPINSIVPTTEVPSHHGPDVQTIIDDINVMTMALLVPTTLMHTHNIMVELEDKITTDDVLDAFENAHRVLPVQKSLKLGSTAEIMEYAKDLGRSRGDMYEIPVWKESVNIENGELFYMQAVHQESDVVPENVDAIRAMLELEEDGEKSILKTNKAMGIL | 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 | MAAKNRTIKVAINGFGRIGRLVFRSLLSKANVEVVAINDLTQPEVLAHLLKYDSAHGELKRKITVKQNILQIDRKKVYVFSEKDPQNLPWDEHDIDVVIESTGRFVSEEGASLHLKAGAKRVIISAPAKEKTIRTVVYNVNHKTISSDDKIISAASCTTNCLAPLVHVLEKNFGIVYGTMLTVHAYTADQRLQDAPHNDLRRARAAAVNIVPTTTGAAKAIGLVVPEANGKLNGMSLRVPVLTGSIVELSVVLEKSPSVEQVNQAMKRFASASFKYCEDPIVSSDVVSSEYGSIFDSKLTNIVEVDGMKLYKVYAWYDNESSYVHQLVRVVSYCAKL | 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, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
Catalytic Activity: D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH
Sequence Mass (Da): 37098
Sequence Length: 337
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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Q43727 | MATHSMIIPSPSSSSSSLATAASPFKETLPLFSRSLTFPRKSLFSQVRLRFFAEKHSQLDTSNGCATNFASLQDSGDQLTEEHVTKGESTLSITVVGASGDLAKKKIFPALFALFYEGCLPQDFSVFGYARTKLTHEELRDMISSTLTCRIDQREKCGDKMEQFLKRCFYHSGQYNSEEDFAELNKKLKEKEAGKISNRLYYLSIPPNIFVDVVRCASLRASSENGWTRVIVEKPFGRDSESSGELTRCLKQYLTEEQIFRIDHYLGKELVENLSVLRFSNLVFEPLWSRNYIRNVQLIFSEDFGTEGRGGYFDQYGIIRDIMQNHLLQILALFAMETPVSLDAEDIRSEKVKVLRSMKPLRLEDVVVGQYKGHNKGGKTYPGYTDDPTVPNHSLTPTFAAAAMFINNARWDGVPFLMKAGKALHTRGAEIRVQFRHVPGNLYKKSFATNLDNATNELVIRVQPDEGIYLRINNKVPGLGMRLDRSDLNLLYRSRYPREIPDAYERLLLDAIEGERRLFIRSDELDAAWDLFTPALKELEEKKIIPELYPYGSRGPVGAHYLASKYNVRWGDLGEA | 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 involved in membrane synthesis and cell division .
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 65428
Sequence Length: 576
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Subcellular Location: Plastid
EC: 1.1.1.49
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P9WN70 | MVDGGGGASDLLVIFGITGDLARKMTFRALYRLERHQLLDCPILGVASDDMSVGQLVKWARESIGRTEKIDDAVFDRLAGRLSYLHGDVTDSQLYDSLAELIGSACRPLYYLEMPPALFAPIVENLANVRLLERARVAVEKPFGHDLASALELNARLRAVLGEDQILRVDHFLGKQPVVELEYLRFANQALAELWDRNSISEIHITMAEDFGVEDRGKFYDAVGALRDVVQNHLLQVLALVTMEPPVGSSADDLNDKKAEVFRAMAPLDPDRCVRGQYLGYTEVAGVASDSATETYVALRTEIDNWRWAGVPIFVRSGKELPAKVTEVRLFLRRVPALAFLPNRRPAEPNQIVLRIDPDPGMRLQISAHTDDSWRDIHLDSSFAVDLGEPIRPYERLLYAGLVGDHQLFAREDSIEQTWRIVQPLLDNPGEIHRYDRGSWGPEAAQSLLRGHRGWQSPWLPRGTDA | 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 from D-glucose 6-phosphate (oxidative stage): step 1/3.
EC: 1.1.1.49
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Q9FY99 | MAALSSSVTTRSYHSGYLASFSPVNGDRHRSLSFLSASPQGLNPLDLCVRFQRKSGRASVFMQDGAIVTNSNSSESKTSLKGLKDEVLSALSQEAAKVGVESDGQSQSTVSITVVGASGDLAKKKIFPALFALYYEGCLPEHFTIFGYSRSKMTDVELRNMVSKTLTCRIDKRANCGEKMEEFLKRCFYHSGQYDSQEHFTELDKKLKEHEAGRISNRLFYLSIPPNIFVDAVKCASTSASSVNGWTRVIVEKPFGRDSETSAALTKSLKQYLEEDQIFRIDHYLGKELVENLSVLRFSNLIFEPLWSRQYIRNVQFIFSEDFGTEGRGGYFDNYGIIRDIMQNHLLQILALFAMETPVSLDAEDIRNEKVKVLRSMRPIRVEDVVIGQYKSHTKGGVTYPAYTDDKTVPKGSLTPTFAAAALFIDNARWDGVPFLMKAGKALHTRSAEIRVQFRHVPGNLYNRNTGSDLDQATNELVIRVQPDEAIYLKINNKVPGLGMRLDRSNLNLLYSARYSKEIPDAYERLLLDAIEGERRLFIRSDELDAAWSLFTPLLKEIEEKKRIPEYYPYGSRGPVGAHYLAAKHKVQWGDVSIDQ | 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 involved in membrane synthesis and cell division .
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 67160
Sequence Length: 596
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Subcellular Location: Plastid
EC: 1.1.1.49
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P0A585 | MKPAHAAASWRNPLRDKRDKRLPRIAGPCGMVIFGVTGDLARKKVMPAVYDLANRGLLPPTFSLVGFARRDWSTQDFGQVVYNAVQEHCRTPFRQQNWDRLAEGFRFVPGTFDDDDAFAQLAETLEKLDAERGTGGNHAFYLAIPPKSFPVVCEQLHKSGLARPQGDRWSRVVIEKPFGHDLASARELNKAVNAVFPEEAVFRIDHYLGKETVQNILALRFANQLFDPIWNAHYVDHVQITMAEDIGLGGRAGYYDGIGAARDVIQNHLMQLLALTAMEEPVSFHPAALQAEKIKVLSATRLAEPLDQTTSRGQYAAGWQGGEKVVGLLDEEGFAEDSTTETFAAITLEVDTRRWAGVPFYLRTGKRLGRRVTEIALVFRRAPHLPFDATMTDELGTNAMVIRVQPDEGVTLRFGSKVPGTAMEVRDVNMDFSYGSAFAEDSPEAYERLILDVLLGEPSLFPVNAEVELAWEILDPALEHWAAHGTPDAYEAGTWGPESSLEMLRRTGREWRRP | 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 from D-glucose 6-phosphate (oxidative stage): step 1/3.
EC: 1.1.1.49
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O59812 | MLSIIVFGASGDLATKMTFPALFALYVRKIIPEDFQIIGYARSKLSQEAANKIVTAHIPIDDTVGASQKALNTFVEHYKYVPGTYDKPESFEMLNSIIAEKETAPASECTRIFYLVLPPHLFAPVSELIKSKAHPNGMVTRLIVEKPIGFDYKSADAILSDLSKHWSAKDTFKVDHFLGEDMIDGFTAIRFANSMFEPIWNREHIESVRVDFREDFGCEGRGGYFEGAGILRDVVQNHLLQLLTLLCIEEPKSQDAEDIIKCKVDFLKSLHPVSKEDIVYGQYTKSANGKVPGYRELDGVADDSEVSTFCALQLRSEAPRWKGIPIIISAGKGLDRDYFEARITFKRREGGMFPTVDSSNVLVLRVYPKEFIALKGHIKQPGFSRQIVPVTLDVKYPEAFPDTWIHKAYEVVIADAINGKHTHFISDDEVRTSWKIFDDVLDTTGDLSPLPYAFGSHHGPDATLEFFKKRNLEWD | 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).
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 53510
Sequence Length: 475
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Subcellular Location: Cytoplasm
EC: 1.1.1.49
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Q8L743 | MSSLSCPTYRSRTSSSSPFLSNHHHSSLINVVDPRRSLSFHYASPQGLNLAELCVVRSQRRSVQSSVVVQDGSVATESSSSEEAKDVGVLTIPSLEADKVVAESDGGEQLSTVSITVVGASGDLAKKKIFPALFALYYEGCLPEHFTIFGYARSKMTDAELRVMVSKTLTCRIDKRANCGEKMEEFLKRCFYHSGQYDSQEHFVALDEKLKEHEGGRLSNRLFYLSIPPNIFVDAVKCASSSASSVNGWTRVIVEKPFGRDSKTSAALTKSLKQYLEEDQIFRIDHYLGKELVENLSVLRFSNLIFEPLWSRQYIRNVQFIFSEDFGTEGRGGYFDNYGIIRDIMQNHLLQILALFAMETPVSLDAEDIRNEKVKVLRSMRPIKLEDVVIGQYKSHSIGGVTYPSYTDDKTVPKGSLTPTFAAAALFIDNARWDGVPFLMKAGKALNTRSAEIRVQFRHVPGNLYNRNSGTDRDQTTNELVIRVQPDEAIYLKINNKVPGLGMRLDQSNLNLLYSARYSKEIPDAYERLLLDAIEGERRLFIRSDELDAAWALFTPLLKEIEEKKTTPEFYPYGSRGPVGAHYLAAKHKVQWGDLSLDQ | 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 involved in membrane synthesis and cell division .
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 67358
Sequence Length: 599
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Subcellular Location: Plastid
EC: 1.1.1.49
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O14137 | MVTFMVFGASGNLANKKTFPALFHLFKRNLVDRSSFYVLGYARSKIPIGEFRESIRESVKPDTESKQVFQDFIDRVSYFSGQYDQSSSYVEFRKHLESVEKKADSSKALRIFYIALPPSVYVTVSSHIYENLYLPGKSRLVIEKPFGKNYQSAVKLKEEVHKHWKEEEIYRIDHYTAKDMVNNFFTLRFANSSSIDAVLNRHSIQSVEIHMYETGGCEGRIGYYDANGVVRDVVQNHLTQIFCIAAMNEPKSASASDVRAEKVNLLKATRPASLKESMLGQYTTSEDGKIPGYLDLEGVPKDSKATTFAASTLHVDNDRWKGVPFVFVSGKRMKKGEVYIKYYFRLKDSGIFSDVKRRRYLILHVQPEEFVNLTCTINKPMTTDLQPIDAYASLNYNEQFKDLMKEKRDGYEILFEDAIRGDPTKFIRYDEVEYAWKIWDEILDSPKKPIPYPAGSDGPEGLEAYMKRHLGHE | 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).
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 54430
Sequence Length: 473
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Subcellular Location: Cytoplasm
EC: 1.1.1.49
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Q9LK23 | MGSGQWHMEKRSTLKNDSFVKEYNPVTETGSLSIIVLGASGDLAKKKTFPALFNLFHQGFLNPDEVHIFGYARSKITDEELRDKIRGYLVDEKNASKKTEALSKFLKLIKYVSGPYDSEEGFKRLDKAILEHEISKKTAEGSSRRLFYLALPPSVYPPVSKMIKAWCTNKSDLGGWTRIVVEKPFGKDLESAEQLSSQIGALFEEPQIYRIDHYLGKELVQNMLVLRFANRLFLPLWNRDNIANVQIVFREDFGTEGRGGYFDEYGIIRDIIQNHLLQVLCLVAMEKPISLKPEHIRDEKVKVLQSVIPIKDEEVVLGQYEGYRDDPTVPNDSNTPTFATTILRINNERWEGVPFILKAGKAMSSKKADIRIQFKDVPGDIFKCQNQGRNEFVIRLQPSEAMYMKLTVKQPGLEMQTVQSELDLSYKQRYQDVSIPEAYERLILDTIRGDQQHFVRRDELKAAWEIFTPLLHRIDKGEVKSVPYKQGSRGPAEADQLLKKAGYMQTHGYIWIPPTL | 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 involved in membrane synthesis and cell division .
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 59157
Sequence Length: 516
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Subcellular Location: Cytoplasm
EC: 1.1.1.49
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Q9FJI5 | MGSGQWHVEKRSTFRNDSFVREYGIVPETGCLSIIVLGASGDLAKKKTFPALFNLYRQGFLNPDEVHIFGYARTKISDEELRDRIRGYLVDEKNAEQAEALSKFLQLIKYVSGPYDAEEGFQRLDKAISEHEISKNSTEGSSRRLFYLALPPSVYPSVCKMIKTCCMNKSDLGGWTRIVVEKPFGKDLESAEQLSSQIGELFDESQIYRIDHYLGKELVQNMLVLRFANRFFLPLWNRDNIENVQIVFREDFGTEGRGGYFDEYGIIRDIIQNHLLQVLCLVAMEKPISLKPEHIRDEKVKVLQSVVPISDDEVVLGQYEGYRDDDTVPNDSNTPTFATTILRIHNERWEGVPFILKAGKALNSRKAEIRIQFKDVPGDIFRCQKQGRNEFVIRLQPSEAMYMKLTVKQPGLDMNTVQSELDLSYGQRYQGVAIPEAYERLILDTIKGDQQHFVRRDELKVAWEIFTPLLHRIDKGEVKSIPYKPGSRGPKEADQLLEKAGYLQTHGYIWIPPTL | 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 involved in membrane synthesis and cell division .
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 59116
Sequence Length: 515
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Subcellular Location: Cytoplasm
EC: 1.1.1.49
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Q43839 | MGVQLRLNPCSSSSAATSPSTFHNGTPYFCKKFNFLPFRTQPLNWVSGIYSRIQPRKHFEVFSSNGFPLNAVSVQDVQVPLTELGSGDTTVSITVIGASGDLAKKKILPALFALFYEDCLPENFVVFGYSRTKLSDEELRNMISTTLTCRIDKRENCDAKMEHFLERCFYHSGQYNSEDDFAELDYKLKEKEGCRVSNRLFYLSIPPNIFVDVVRCASLKASSTSGWTRVIVEKPFGRDLESSSELTRSLKKYLTEEQIFRIDHYLGKELVENLSVLRFSNLVFEPLWSRNYIRNVQFIFSEDFGTEGRGGYFDHYGIIRDIMQNHLLQILALFAMETPVSLDAEDIRNEKVKVLRSMRPLQLEDVVLGQYKGHSNGAKSYPAYTDDPTVPNGSITPTFSAAALFIDNARWDGVPFLMKAGKALHTKRAEIRVQFRHVPGNLYKRNFGTDMDKATNELVLRLQPDEAIYLKINNKVPGLGMRLDRSDLNLLYKAKYRGEIPDAYERLLLDAIEGERRLFIRSDELDAAWALFTPLLKELEEKKIAPELYPYGSRGPVGAHYLAAKHNVRWGDLSGDD | 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 involved in membrane synthesis and cell division.
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 65687
Sequence Length: 577
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Subcellular Location: Plastid
EC: 1.1.1.49
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B5EBB8 | MQKQQLWERYKNLLYHDAELELSVDTSRIDFPEGFLEKMDPRLQQAYQEMEALEQGAVANPDEHRMVGHYWLRAPELAPEATLAEEITSTLAAIEAFASSVHGGNIAAPDGHRFTDLLIIGIGGSALGPQFLADSLGGPKDLLRIWFFDNTDPDGMDKVLSGIGAALKQTLVVVISKSGGTKETRNGMLEACQAFERAGLHFAGHAVAVTGSGSELDRTASRENWLGVFPMWDWVGGRTSVTSAVGLLPAALQGIDVDRLLAGARACDQKTRSRVTRENPAALLALSWFHATQGKGTRDMVLLPYKDRLLLFSRYLQQLIMESLGKGLDRDGKEVLQGIAVYGNKGSTDQHAYVQQLREGVHNFFVTFIEVLKDRQGPSMEVEPGATSGDYLSGFFQGTRSALYEKGRESVTITVRELSPASIGALIALYERAVGLYASLVNVNAYHQPGVEAGKEAAGAVLKLQGEIMELLRRQPNRDFTGEEMALALARPEEVETTFMILRHLAANGDHGVSVTEKDKIWENKYRSKD | 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 | MANDITTTAAWQSLTERYEAFQGTTLRELFQDGGRAEKLSFDAAGLRVDLSKNLLDDAILTDLVALAEQAGLTDRIEAMFRGEHINNTEDRAVLHTALRLPVEESLEVDGQDVAADVHEVLGRMRDFATALRSGAWLGYTGRTIKKVVNIGIGGSDLGPAMATKALRAYATAGITAEFVSNVDPADMVSVLEDLDAESTLFVIASKTFTTQETLANANAAKNWLIEQLGSEEAVSKHFVAVSTNAEKVTAFGINPENMFGFWDWVGGRYSVDSAVGLSLMAVIGPRDFMRFLGGFRAMDEHFRYTDFGQNVPVLMALLSVWYTDFFGAETHAVLPYSEDLSRFAAYLQQLTMESNGKSVRRDGSPVTTGTGEIYWGEPGTNGQHAFFQLIHQGTRLIPADFIGFARPKQDLPAGEKSMHDLLMSNFFAQTKVLAFGKTAEEIAAEGVDDNLINHKVMPGNRPTTTILAEELTPAVLGALIALYEHIVFVQGVIWDINSFDQWGVELGKQQASDLAPAVSGEVEVDSGDSSTDALIRWYRTNR | 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 | MSSSYLKLDFKLKNQVVPFESYQKQVSQIHNAVKSKSVEEKDWLGWLNLASDYNKEEYAKMEEKVAQWLKDKVEVVVVIGIGGSYLGAKTGYEFIFGKYSIKKPQMELVFAGNDISAETLVAKLNYVKDKKFAINVISKSGTTLEPSIAFREFRNLLEQKEVNSWEYIVATTDKQKGVLFELATAKKYTKFVIPDDVGGRFSVLTAVGLFPFLCAGIDAKKVLEGARQMNKELFSENVMENAAYKYAVARHYLHKEKKYAVEIFVSYEPKLRYFAEWWKQLFAESEGKDGKGLWPSSAIFSTDLHSLGQMIQDGPKILFETVLTLENPAYDITFKDNVIDYDKLNYLSDKKLSEVNNVAFNATMEAHSDEGNVPNISMLFKDFSEETLGALFMFFMRAVTMSAYLLGVNPFNQPGVEVYKKNMFFLLGKK | 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 | MGSDITATPAWQALSRHHDEIRAKDLRGLFADDPTRGTGFALTVGDLYIDYSKHRVTRETLDLLLDLARTAGLPAKRDAMFSGAHINTSEDRAVLHTALRLPRDASLTVDGQDVVADVHEVLDRMGDFTDRLRSGEWRGATGERITTVVNIGIGGSDLGPVMVDQALRHYADAGISARFVSNVDPADLVAKLNGLDPATTLFIIASKTFSTLETLTNATAARRWLVDGLGGSAGQDAVSKHFVAVSTNAKLVDDFGIDTANMFGFWDWVGGRYSVDSAIGLSVMAVIGRERFAEFLAGFHLVDEHFRSAPLEANAPVLLGLIGLWYSNFFGAETRAVLPYSNDLARFAAYLQQLTMESNGKSVRADGTPVSTGTGEIFWGEPGTNGQHAFYQLLHQGTRLVPADFIGFSEPTDDLPTADGTGSMHDLLMSNFFAQTQVLAFGKTAEEITGEGTPPNVVPHKVMPGNRPSTSILATKLTPSVVGQLIALYEHQVFVEGVIWGIDSFDQWGVELGKTQAKALLPVLTGADSPAAQSDSSTDALVRRYRTERGRTA | 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 | MTERELWERYQRYLCVVPALDFTLDVSRMRFPADYLERMRPRLEEAFGAMEALEKGAVANPDEKRKVGHYWLRAPELAPEPALQKEITDTVAAIHAFAKNVHEGRVKPQKAQRFTHMLIVGIGGSALGPQLVADALGTAKDPMQVSFFDNTDPDGFDRVLAQLGERLSETLTLVISKSGGTKETRNGMLEAERGYSARGLDFSKHAVAVTGAGSELDNHAKKQGWLRAFPMWDWVGGRTSVTSAVGLLPARLQGLDIDALLKGARDMDAATRERDALKNPAALLALMWHYAGDGRGHKDMVILPYKDRLLLMSRYLQQLVMESLGKETDLDGQVVNQGIAVYGNKGSTDQHAYVQQLREGVLNFFATFIEVLKDRDGGSQEVEPGVTSGDYLLGFLLGTRRALYEKDRESLTLTVPDVSARTLGALIALYERAVGFYATLVHINAYHQPGVEAGKKAAGVVLELQRKLTTRLREARAEARTAEQLAADIGMPDEVETVFKVLQHLAANPDRGVTRTPGATPTQARFQAK | 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 | MITPLTQRPAWKALEAHYQTIKGMHLRQLFADDPKRGERFTAEAVGLYLDYSKNRITDETLHLLVQLAEECGLRERIEAMFRGDAINVTEQRAVLHIALRAPRNEKILVDGNDVVPGVHAVLDRMADFSDKIRSGDWQGHTGKRIRNIINIGIGGSDLGPVMAYEALRHYSLHNLSFRFISNVDGTDFVEATRGLDPEETLFIICSKTFTTTETLANAHTARRWMLRQIKDLEGVRKHFVAVSTNAEEVARFGIDTANMFEFWDWVGGRYSMDSAIGLSTMIAVGPENFREMLAGFHAMDQHFYSAPFDRNLPVLMGLLSLWYNNFFGAQTLAVLPYEQYLKRFPAYLQQLTMESNGKHITLNGSQVDYQTSPIVWGEPGTNGQHSFYQLIHQGTRLIPCDFIGFCQTLNPLGDHHDLLMANLFAQTEALAFGKTEDEVKAEGVPDWLCPHRSFEGNRPTNTILAERLTPHTLGALVALYEQSVFTQGTIWQIDSFDQWGVELGKVLAHRIGQELEDENGKSLKHDSSTNALIQRYNRLKQK | 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
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Q3JCN1 | MKPYLAQARSWASLLQHYGCIKKQHMRDLFAADPQRFDKFSLIFNGILFDFSKNRITEETLKLLLDLARERELQQGISRMFAGEPINNTENRPVLHVALRNRANRPIMVKGKDVMPQVNVVLERMGKFCDRVHRGQWRGFSGERLTDIVNIGIGGSDLGPAMVTEALQPYAKSGFRVHFVSNIDGTQLAETLKTIRPETALFVISSKTFTTQETLTNAHSARNWFLRAAPDDKAIAKHFIAVSTNRSEVEKFGIDPCNMFEFWDWVGGRYSLWSAIGLSIALYLGMENFEQLLEGAHEMDKHFQETPLKQNIPVIAALVGIWNINFLGAQSHAVLPYDQYLERFPAYLQQLEMESNGKHVTRGGASVNYATGNVIWGAPGTNGQHAFFQLLHQGTPLITADFLASAESHNPLGEHHQILLSNFFAQTEALMKGKDEAEVRAELEEANLAKGEVEALIPHKLFDGNRPSNSFLFSKLTPWTLGALIAFYEHKVFTQGLIWDINSFDQWGVELGKQLATTILPELQGGEEVNSHDSSTNGLINYYKRIRHL | 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
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Q2JX86 | MDSLQLWQRYCDWLYYHPELEIFVDISRIRFTPAQVEALRPLFARAFAEMQALEAGAIANPDEGRQVGHYWLRAPELAPTAEIRQAIQDCVEQVESFAKKIHCGTIPASGGGRFTELLWIGIGGSALGPQFVAEALAPLQPPLNIHFIDNTDPDGFDRVLGRLAGKLGQTLVVVTSKSGNTPEPRNALVEVELAYRKAGIPFSAHAVAITGPGSQLEQQARQEGWLAVFPIFDWVGGRTSETSAVGLLPAALQGIDIRALLAGAATMDKATRVPHLERNPAALLAMAWYIVGEGRGRKDMVVLPYKDRLALFSRYLQQLVMESLGKSHDLQGNRVEQGLTVYGNKGTTDQHAYVQQLRDGLNNFFVTFIEVLQDREPGIPSPFVEPEVTSGDYLDGLLQGTRQALYENGRDSVTITLPRVDARSVGALIALYERAVGLYASLIQVNAYHQPGVEAGKKAASAVLQLQRQVLEVMREQKGSLTLPQLAEKLSCPERIETLYWIVRHLQANGRSLVLVGDPGRPLELSIQPRPA | 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
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P22256 | MNSNKELMQRRSQAIPRGVGQIHPIFADRAENCRVWDVEGREYLDFAGGIAVLNTGHLHPKVVAAVEAQLKKLSHTCFQVLAYEPYLELCEIMNQKVPGDFAKKTLLVTTGSEAVENAVKIARAATKRSGTIAFSGAYHGRTHYTLALTGKVNPYSAGMGLMPGHVYRALYPCPLHGISEDDAIASIHRIFKNDAAPEDIAAIVIEPVQGEGGFYASSPAFMQRLRALCDEHGIMLIADEVQSGAGRTGTLFAMEQMGVAPDLTTFAKSIAGGFPLAGVTGRAEVMDAVAPGGLGGTYAGNPIACVAALEVLKVFEQENLLQKANDLGQKLKDGLLAIAEKHPEIGDVRGLGAMIAIELFEDGDHNKPDAKLTAEIVARARDKGLILLSCGPYYNVLRILVPLTIEDAQIRQGLEIISQCFDEAKQ | 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 pathway that allows some E.coli strains to utilize GABA as a nitrogen source for growth . Also catalyzes the conversion of 5-aminovalerate to glutarate semialdehyde, as part of a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate .
Catalytic Activity: 2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate semialdehyde
Sequence Mass (Da): 45775
Sequence Length: 426
Pathway: Amino-acid degradation; 4-aminobutanoate degradation.
EC: 2.6.1.19
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P80404 | MASMLLAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGPLMKTEVPGPRSQELMKQLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPALLKLIQQPQNASMFVNRPALGILPPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENALKTIFMWYRSKERGQRGFSQEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPSFDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGGDNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMTFSKKMMTGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNAAHAGKALLTGLLDLQARYPQFISRVRGRGTFCSFDTPDDSIRNKLILIARNKGVVLGGCGDKSIRFRPTLVFRDHHAHLFLNIFSDILADFK | 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-aminobutanoate = L-glutamate + succinate semialdehyde
Sequence Mass (Da): 56439
Sequence Length: 500
Subcellular Location: Mitochondrion matrix
EC: 2.6.1.19
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P40829 | MTSVEQSRQLVTEIPGPVSLELAKRLNAAVPRGVGVTLPVFVTRAAGGVIEDVDGNRLIDLGSGIAVTTIGNSSPRVVDAVRAQVADFTHTCFIITPYEEYVAVTEQLNRITPGSGEKRSVLFNSGAEAVENSIKVARSYTRKPAVVAFDHAYHGRTNLTMALTAKSMPYKSGFGPFAPEIYRAPLSYPYRDGLLNKDLATDGKLAGARAINVIEKQVGADDLAAVIIEPIQGEGGFIVPAEGFLATLLDWCRKNNVMFIADEVQTGFARTGAMFACEHDGIVPDLICTAKGIADGLPLAAVTGRAEIMNAPHVSGLGGTFGGNPVACAAALATITTIENDGLIQRAQQIERLITDRLLRLQDADDRIGDVRGRGAMIAVELVKSGTAEPDPELTEKVATAAHATGVIILTCGMFGNIIRLLPPLTISDELLAEGLDILSRILGDF | 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
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P50554 | MAFLLTTRRLVCSSQKNLHLFTPGSRYISQAAAKVDFEFDYDGPLMKTEVPGPRSQELMKQLNTIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYNHPALAKLVQQPQNASTFINRPALGILPPENFVDKLRESLMSVAPKGMCQLITMACGSCSNENAFKTIFMWYRSKERGQRGFSKEELETCMVNQSPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPSFDWPIAPFPRLKYPLEEFVTDNQQEEARCLEEVEDLIVKYRKKKRTVAGIIVEPIQSEGGDNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMSFSKKMMTGGFFHKEEFRPSAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNVAHAGKTLLTGLLDLQAQYPQFVSRVRGRGTFCSFDTPDEAIRNKLILIARNKGVVLGGCGDKSIRFRPTLVFRDHHAHLFLNIFSGILADFK | 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 = L-glutamate + succinate semialdehyde
Sequence Mass (Da): 56456
Sequence Length: 500
Subcellular Location: Mitochondrion matrix
EC: 2.6.1.19
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P32503 | MLRFVTKNSQDKSSDLFSICSDRGTFVAHNRVRTDFKFDNLVFNRVYGVSQKFTLVGNPTVCFNEGSSYLEGIAKKYLTLDGGLAIDNVLNELRSTCGIPGNAVASHAYNITSWRWYDNHVALLMNMLRAYHLQVLTEQGQYSAGDIPMYHDGHVKIKLPVTIDDTAGPTQFAWPSDRSTDSYPDWAQFSESFPSIDVPYLDVRPLTVTEVNFVLMMMSKWHRRTNLAIDYEAPQLADKFAYRHALTVQDADEWIEGDRTDDQFRPPSSKVMLSALRKYVNHNRLYNQFYTAAQLLAQIMMKPVPNCAEGYAWLMHDALVNIPKFGSIRGRYPFLLSGDAALIQATALEDWSAIMAKPELVFTYAMQVSVALNTGLYLRRVKKTGFGTTIDDSYEDGAFLQPETFVQAALACCTGQDAPLNGMSDVYVTYPDLLEFDAVTQVPITVIEPAGYNIVDDHLVVVGVPVACSPYMIFPVAAFDTANPYCGNFVIKAANKYLRKGAVYDKLEAWKLAWALRVAGYDTHFKVYGDTHGLTKFYADNGDTWTHIPEFVTDGDVMEVFVTAIERRARHFVELPRLNSPAFFRSVEVSTTIYDTHVQAGAHAVYHASRINLDYVKPVSTGIQVINAGELKNYWGSVRRTQQGLGVVGLTMPAVMPTGEPTAGAAHEELIEQADNVLVE | 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 unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of the virion and are extruded into the cytoplasm.
PTM: Acetylation is necessary for viral assembly.
Sequence Mass (Da): 75994
Sequence Length: 680
Subcellular Location: Virion
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P27400 | MGDHNLNVQELLNLFQNLGIPRQPNHREVIGLRMLGGWWGPGTRYILVSIFLQDDSGQPLQQPRWRPEGRPVNPLVHNTIEAPWGELRQAFEDLDVAEGTLRFGPLANGNWIPGDEYSMEFQPPLAQEIAQMQRDELEEILDITGQICAQVIDLVDMQDAQIRGLERRIQDRLGLRDNLPVAGIQAPPSSPIGQPIASSSLQPIPGSSSSPADLDGIWTPRQIDPRLSRVAYNPFLPGSSDGSGGSIPVQPSAPPAVLPSLPSLPAPVSQPIIQYVAQPPVPAPQAIPIQHIRAVTGNTPTNPRDIPMWLGRHSAAIEGVFPMTTPDLRCRVVNALIGGSLGLSLEPIHCVNWAAVVAALYVRTHGSYPIHELANVLRAVVTQEGVATGFQLGIMLSNQDYNLVWGILRPLLPGQAVVTAMQQRLDQEVNDAARITSFNGHLNDIYQLLGLNARGQSIARAQSASTSGNSASAGRGRRGQRTQQQAGRQQQQQTRRTNQGNQGQRDNNQRQSSGGNQGQRGQGGYDLRPRTYQPQRYGGGRGRRWNDNQQQQQAQPGRSSDQPRSQSQQPQPEARGDQSRTSGAGRGQQGRGNQNRNQRRADANNTRNVDTVTATTTSSSTASSGQNGSSTTPPASGSRNQGD | 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: Specific enzymatic cleavages in vivo by viral protease yield mature proteins. The protease is not cleaved off from Pol. Since cleavage efficiency is not optimal for all sites, intermediary molecules are expressed (By similarity).
Sequence Mass (Da): 69786
Sequence Length: 643
Domain: Gag protein contains 3 glycine-arginine motifs (GR-boxes) necessary for RNA packaging, the first of which has nucleic acid binding properties in vitro.
Subcellular Location: Virion
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Q87039 | MASGSNVEEYELDVEALVVILRDRNIGRNPLHGEIIGLRLTEGWWGQLERFQMVRLILQDEDNEPLQRPRHEIIPRAVNPHTMFVLSGPLAELQLAFQDLDLPEGPLRFGPLANGHYVEGDPYSRSYRPVTMAETAQMTRDELEDTLNTQSEIEIQMINLLELYEVETRALRRQLAERSSIGQGGISPGASHSRPPVSSFSGLPSLPAIPGIHTRAPSPPRATSTPGNIPRSLGDDNMPSSSFAGPSQPRVSFHPGNPFAEAEGHRPRSQSRERRRDIPSAPVISAPVPSAPPMIQYIPVPPPPPVGAVIPIQHIRSVTGEPPRNPREIPIWLGRNAPAIDGVFPTTTPDLRCRIINALLGGNLGLSLTPGDCITWDSAVATLFIRTYGQYPLHQLGNVLKGIADQEGVATAYTLGMMLSGQNYQLVSGIIRGYLPGQAVVTAMQQRLDQEIDDQTRAETFIQHLNAVYEILGLNARGQSIRASVTPQPRPSRGRGRGQSAPEPSQGPVNSGRGRQCPAPGQNDRGSNIQNQGQENSSQGGYNLRSRTYQPQRYGGGRGRRWNENTNNSETRPTEQSPQTPRPIQAGSGVRGNQSQTYKPAAGRGGRGNQNRNQRSSGAGDSRAVNTVTQSATSSTDESSSTTTAAPSGGQGN | 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: Specific enzymatic cleavages in vivo by viral protease yield mature proteins. The protease is not cleaved off from Pol. Since cleavage efficiency is not optimal for all sites, intermediary molecules are expressed (By similarity).
Sequence Mass (Da): 70762
Sequence Length: 653
Domain: Gag protein contains 3 glycine-arginine motifs (GR-boxes) necessary for RNA packaging, the first of which has nucleic acid binding properties in vitro.
Subcellular Location: Virion
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Q02843 | MGGGHSALSGRSLDTFEKIRLRPNGKKKYQIKHLIWAGKEMERFGLHEKLLETKEGCQKIIEVLTPLEPTGSEGLKALFNLCCVIWCIHAEQKVKDTEEAVVTVKQHYHLVDKNEKAAKKKNETTAPPGGESRNYPVVNQNNAWVHQPLSPRTLNAWVKCVEEKRWGAEVVPMFQALSEGCLSYDVNQMLNVIGDHQGALQILKEVINEEAAEWDRTHRPPAGPLPAGQLRDPTGSDIAGTTSSIQEQIEWTFNANPRIDVGAQYRKWVILGLQKVVQMYNPQKVLDIRQGPKEPFQDYVDRFYKALRAEQAPQDVKNWMTQTLLIQNANPDCKLILKGLGMNPTLEEMLIACQGVGGPQHKAKLMVEMMSNGQNMVQVGPQKKGPRGPLKCFNCGKFGHMQRECKAPRQIKCFKCGKIGHMAKDCKNGQANFLGYGHWGGAKPRNFVQYRGDTVGLEPTAPPMETAYDPAKKLLQQYAEKGQRLREEREQTRKQKEKEVEDVSLSSLFGGDQ | 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: Capsid protein p24 is phosphorylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 57702
Sequence Length: 513
Domain: Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. p6-gag contains one L domain: a PTAP/PSAP motif, which interacts with the UEV domain of TSG101 (By similarity).
Subcellular Location: Virion
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P22381 | MGNGNSALLGTDLDKFEKIRLKRGGKKCYRLKHLCWCKGELDRFGLSDKLLETQQGCEKILSVCWPLYDQGSDNLKALVGTVCVVACIHAGIEIKSTQDALKKLKVITRKEEKQEDESKNFPVQRDAAGQYQYTPISPRIIQTWVKTVEEKKWKPEVIPLFSALTEGAISHDLNIMLNAVGDHQGAMQVLKDVINEQAAEWDLTHPQQQPAQPGGGLRTPSGSDIAGTTSTVEEQLAWMNMQQNAINVGTIYKSWIILGMNRLVKSHCPISITDVRQGPKEAFKDYVDRFYNVMRAEQASGEVKMWMQQHLLIENANPECKQILRSLGKGATLEEMLEACQGVGGPQHKARLMAEMMRTVVGQSQNFVQQRGPQRGPVRQPTGRKPICFNCNKEGHVARFFKAPRRKGCWNCGAMDHQKAQCPKPAQQQRVNFLGYGPWGPSKPGNYPAQEVTPTAPPLEEKPLQKTLSTYQKLGRGLRQKMKEEKREEDFHSLSTLFQEDQ | 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: Capsid protein p24 is phosphorylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 56481
Sequence Length: 502
Domain: Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. p6-gag contains one L domain: a PTAP/PSAP motif, which interacts with the UEV domain of TSG101 (By similarity).
Subcellular Location: Virion
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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 | MGQTRIPCLLMRGGTSKGAYFLHDDLPAPGPLRDRVLLAVMGSPDARQIDGIGGADSLTSKVAIIRASQRDDADVDYLFAQVVVDEARVDYGQNCGNILAGVGPFALERGLVAASGASTPVRIFMENTGQIAVAQVPTADGQVEYAGDTRIDGVPGRAAALVVTFADVAGASCGALLPTGNSRDCVEGVEVTCIDNGMPVVLLCAEDLGVTGYEPCETLEADSALKTRLEAIRLQLGPRMNLGDVSQRNVPKMCLLSAPRNGGTVNTRSFIPHRCHASIGVFGAVSVATACLIEGSVAQGLASTSGGDRQRLAVEHPSGEFTVEISLEHGVIKGCGLVRTARLLFDGVVCIGRDTWGGPEK | 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 Mass (Da): 37559
Sequence Length: 361
EC: 5.3.2.8
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P55180 | MAILVTGGAGYIGSHTCVELLNSGYEIVVLDNLSNSSAEALNRVKEITGKDLTFYEADLLDREAVDSVFAENEIEAVIHFAGLKAVGESVAIPLKYYHNNLTGTFILCEAMEKYGVKKIVFSSSATVYGVPETSPITEDFPLGATNPYGQTKLMLEQILRDLHTADNEWSVALLRYFNPFGAHPSGRIGEDPNGIPNNLMPYVAQVAVGKLEQLSVFGNDYPTKDGTGVRDYIHVVDLAEGHVKALEKVLNSTGADAYNLGTGTGYSVLEMVKAFEKVSGKEVPYRFADRRPGDIATCFADPAKAKRELGWEAKRGLEEMCADSWRWQSSNVNGYKSAE | 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
Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
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E8MF10 | MTTVLVTGGAGFIATHTDIELLNKGYDVISVDNYGNSSPVALERVEQITGKPVKRYDGDVRDEALMERVFAENNIDWVIHFAGLKAVGESVAKPIEYYDNNLYSTLVLLKVMKKHNVKKIIFSSSATVYGTPKELPITEETPTGGTTNPYGTSKLFQEQILRDVHVADPSWTIVLLRYFNPVGAHESGLLGEDPKGIPANLTPYVAKVAVGELKEVQVYGDDYDTPDGTGVRDYIHVVDLAKGHVAVIDHIDKEGVFVYNLGTGHGYSVLEVIKAYEKAAGHPIPYAIKPRRPGDIAACYADASKAEKELGWKAELTIDDMAASSLNWQTKNPNGFRDAE | 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 is important for host intestinal colonization by bifidobacteria.
Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Mass (Da): 37226
Sequence Length: 340
Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
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Q3T105 | MAEKVLVTGGAGYIGSHTVLELLEAGYSPMVIDNFHNAIRGGGSMPESLRRVQDLTGRSVEFEEMDILDQAALQRLFKKHSFMAVIHFAGLKAVGESVQKPLDYYRVNLTGTIQLLEIMRAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGCTNPYGKSKFFIEEMIRDLCQADKAWNAVLLRYFNPIGAHASGCIGEDPQGIPNNLMPYVSQVAIGRREVLNVFGNDYDTEDGTGVRDYIHVVDLAKGHIAALRKLKEQCGCRIYNLGTGTGYSVLQMVQAMEKASGKKIPYKVVARREGDVAACYANPSLALKELGWSAALGLDRMCEDLWRWQKQNPSGFGTQA | 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 galactose is converted to the glycolytic intermediate glucose 6-phosphate. It contributes to the catabolism of dietary galactose and enables the endogenous biosynthesis of both UDP-Gal and UDP-GalNAc when exogenous sources are limited. Both UDP-sugar interconversions are important in the synthesis of glycoproteins and glycolipids.
Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Mass (Da): 38254
Sequence Length: 348
Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
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Q564Q1 | MHILVTGAAGFIGSHTVLELLNSGYTVLCIDNFANAISVTDEHGNAISLKRVAQLTGKDVPFQNVDVCDEAALEKVFSENKFDGIIHLAALKAVGESVAKPLQYYSNNLVASLNLIQMCLKYNVKNFVFSSSATVYGPPSELPITEKSQTGQGITNPYGQTKYMMEQILIDVGKANPEWNVVLLRYFNPVGAHKSGLIGEDPKGVPNNLMPYVSQVAIGKLPVLTIYGDQFDTVDGTGVRDYIHVVDLAKGHVKAFDRIKTVGNIGTEIYNLGTGVGYSVRQMVDALKKVSGRDIPVKIGVPRPGDVASVYCDPSLAQEKLGWRAETGLEEMCADLWNWQTKNPQGFSA | 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 galactose is converted to the glycolytic intermediate glucose 6-phosphate. It contributes to the catabolism of dietary galactose and enables the endogenous biosynthesis of both UDP-Gal and UDP-GalNAc when exogenous sources are limited. Both UDP-sugar interconversions are important for the synthesis of glycoproteins and glycolipids.
Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Mass (Da): 37883
Sequence Length: 349
Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
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Q45291 | MKLLVTGGAGYVGSVAAAVLLEHGHDVTIIDNFSTGNREAVPADARLIEGDVNDVVEEVLSEGGFEGVVHFAARSLVGESVEKPNEYWHDNVVTALTLLDAMRAHGVNNLVFSSTAATYGEPDVVPITEDMPTQPTNAYGATKLSIDYAITSYAAAFGLAATSLRYFNVAGAYGNIGENREVETHLIPLVLQVATGHREKTFMFGDDWPTPDGTAVRDYIHILDLAKAHVLALESNEAGKHRIFNLGSGDGYSVKQVVEMCREVTGHPIPAEVAPRRAGDPATLIASSEKAKQELGWTPEHTDLRTIVEDAWAFTSALGDRSHAAKKKA | 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: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
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Q8I136 | MLPRMLKMKTVGTVLAVIWLFGLAFIYVQSTSSSLRPPGRHPPPLPQLDPLIPQNPPQNDEIRPKKSAPPIPTINLAEDTTIHERTEKDVTWKTFDVEKFLNKGKWHQGEDKYKANSFNQEASDALNPTRKIPDSREPQCRDVDYSKVGMQPTTVIITYHNEARSSLLRTVFSVFNQSPEELLLEIVLVDDNSQDVEIGKELAQIQRITVLRNNQREGLIRSRVKGAQVARAPVLTFLDSHIECNQKWLEPLLARIAENPKAVVAPIIDVINVDNFNYVGASADLRGGFDWTLVFRWEFMNEQLRKERHAHPTAPIRSPTMAGGLFAISKEWFNELGTYDLDMEVWGGENLEMSFRVWQCGGSLEIMPCSRVGHVFRKKHPYTFPGGSGNVFQKNTRRAAEVWMDEYKAIYLKNVPSARFVNFGDITDRLAIRDRLQCKSFKWYLENVYPQLEIPRKTPGKSFQMKIGNLCLDSMARKESEAPGLFGCHGTGGNQEWVFDQLTKTFKNAISQLCLDFSSNTENKTVTMVKCENLRPDTMVVEKNGWLTQGGKCLTVNQGSGGDWLIYGAHCELNNGAQRWIFEKLDTYE | 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-[protein] + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 67031
Sequence Length: 589
Domain: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.41
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Q8IA42 | MAIKKRYVKRLLRKVVLLLVVIVTVSLVTTLVVERRMKNAAELTEQLDPNGDPITPVFRAANIHPTRKAPRPPFQDRNSVVDIPRSDKLQGFRLPEPKGERKDWHDYAAMEADRKRSGFGEHGVAVKIENPDEKQLEKEHYEMNGFNGLISDRISVNRSVPDLRLEACKTRKYLAKLPNISVIFIFFNEHFNTLLRSIYSVINRTPPELLKQIVLVDDGSEWDVLKQPLDDYVQQHFPHLVTIVRNPERQGLIGARIAGAKVAVGQVMVFFDSHIEVNYNWLPPLIEPIAINPKISTCPMVDTISHEDFSYFSGNKDGARGGFDWKMLYKQLPVLPEDALDKSMPYRSPVMMGGLFAINTDFFWDLGGYDDQLDIWGGEQYELSFKIWMCGGMLLDVPCSRVAHIFRGPMKPRGNPRGHNFVAKNHKRVAEVWMDEYKQYVYKRDPKTYDNLDAGDLTRQRGVRERLKCKSFHWFMTEVAPDFLVKFPPVEPPSYAAGIIQNVANPVYCLDNMGKSTEEAVGMFSCADNRTHPQPNQFWELSIFRDLRMKGFDSVCLDVHEGPPNATVWMWSCHSQGGNQFWYYDRQTQRLVHGENNKRCLEGFVENGIAKVVANSCENGNDRQRWEFGFVNHTMLDTFYDGLK | 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 threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified. Prefers the diglycosylated Muc5AC-3/13 as substrate.
Catalytic Activity: L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 74040
Sequence Length: 644
Domain: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.41
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Q8N4A0 | MAVRWTWAGKSCLLLAFLTVAYIFVELLVSTFHASAGAGRARELGSRRLSDLQKNTEDLSRPLYKKPPADSRALGEWGKASKLQLNEDELKQQEELIERYAINIYLSDRISLHRHIEDKRMYECKSQKFNYRTLPTTSVIIAFYNEAWSTLLRTIHSVLETSPAVLLKEIILVDDLSDRVYLKTQLETYISNLDRVRLIRTNKREGLVRARLIGATFATGDVLTFLDCHCECNSGWLEPLLERIGRDETAVVCPVIDTIDWNTFEFYMQIGEPMIGGFDWRLTFQWHSVPKQERDRRISRIDPIRSPTMAGGLFAVSKKYFQYLGTYDTGMEVWGGENLELSFRVWQCGGKLEIHPCSHVGHVFPKRAPYARPNFLQNTARAAEVWMDEYKEHFYNRNPPARKEAYGDISERKLLRERLRCKSFDWYLKNVFPNLHVPEDRPGWHGAIRSRGISSECLDYNSPDNNPTGANLSLFGCHGQGGNQFFEYTSNKEIRFNSVTELCAEVPEQKNYVGMQNCPKDGFPVPANIIWHFKEDGTIFHPHSGLCLSAYRTPEGRPDVQMRTCDALDKNQIWSFEK | 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.
Catalytic Activity: L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 66666
Sequence Length: 578
Domain: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.41
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Q95ZJ1 | MIIFKKKAILKVLLLVPVFWICSLIFFAATSNDSSQIGSNNDLANKIAEANFHPKAAKQDVIQGFGPPIEPEPVVENNKVEEEEQPGGNLAKPKFMVDPNDPIYKKGDAAQAGELGKAVVVDKTKLSTEEKAKYDKGMLNNAFNQYASDMISVHRTLPTNIDAECKTEKYNENLPRTSVIICFHNEAWSVLLRTVHSVLERTPDHLLEEVVLVDDFSDMDHTKRPLEEYMSQFGGKVKILRMEKREGLIRARLRGAAVATGEVLTYLDSHCECMEGWMEPLLDRIKRDPTTVVCPVIDVIDDNTFEYHHSKAYFTSVGGFDWGLQFNWHSIPERDRKNRTRPIDPVRSPTMAGGLFSIDKKYFEKLGTYDPGFDIWGGENLELSFKIWMCGGTLEIVPCSHVGHVFRKRSPYKWRTGVNVLKRNSIRLAEVWLDDYKTYYYERINNQLGDFGDISSRKKLREDLGCKSFKWYLDNIYPELFVPGESVAKGEVRNSAVQPARCLDCMVGRHEKNRPVGTYQCHGQGGNQYWMLSKDGEIRRDESCVDYAGSDVMVFPCHGMKGNQEWRYNHDTGRLQHAVSQKCLGMTKDGAKLEMVACQYDDPYQHWKFKEYNEAKAIEHGAKPPS | 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-[protein] + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 71382
Sequence Length: 626
Domain: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.41
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Q6WV17 | MTFSTFTRKMRGRMRSNTCRIVLLTSLVWVIFDFVLIARYSDCIGKDGWRCKRSGEYDVELPNAERLVDDNQLVDDNEINTEKSLDGESGGALIMGQGFASGGISMTYPSVVLKKWFLAPSVQEAKGKPGEMGKPVKIPADMKDLMKEKFKENQFNLLASDMISLNRSLTDVRHEGCRRKHYASKLPTTSIVIVFHNEAWTTLLRTVWSVINRSPRALLKEIILVDDASERDFLGKQLEEYVAKLPVKTFVLRTEKRSGLIRARLLGAEHVSGEVITFLDAHCECTEGWLEPLLARIVQNRRTVVCPIIDVISDETFEYITASDSTWGGFNWKLNFRWYRVPSREMARRNNDRTAPLRTPTMAGGLFSIDKDYFYEIGSYDEGMDIWGGENLEMSFRIWQCGGILEIIPCSHVGHVFRDKSPYTFPGGVAKIVLHNAARVAEVWLDEWRDFYYSMSTGARKASAGDVSDRKALRDRLKCKSFRWYLENVYPESLMPLDYYYLGEIRNAETETCLDTMGRKYNEKVGISYCHGLGGNQVFAYTKRQQIMSDDLCLDASSSNGPVNMVRCHNMGGNQEWVYDAEEKWIRHTNTGQCLQRATRDDANTPLLRPCSYGKGQQWLMESKFKWQAH | 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 transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Prefers EA2 as substrate . In the larval midgut, required for O-glycosylation of apical and luminal proteins within copper cells enabling proper gut acidification .
Catalytic Activity: L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 72097
Sequence Length: 630
Domain: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.41
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Q7Z7M9 | MNRIRKFFRGSGRVLAFIFVASVIWLLFDMAALRLSFSEINTRVIKEDIVRRERIGFRVQPDQGKIFYSSIKEMKPPLRGHGKGAWGKENVRKTEESVLKVEVDLDQTQRERKMQNALGRGKVVPLWHPAHLQTLPVTPNKQKTDGRGTKPEASSHQGTPKQTTAQGAPKTSFIAAKGTQVVKISVHMGRVSLKQEPRKSHSPSSDTSKLAAERDLNVTISLSTDRPKQRSQAVANERAHPASTAVPKSGEAMALNKTKTQSKEVNANKHKANTSLPFPKFTVNSNRLRKQSINETPLGSLSKDDGARGAHGKKLNFSESHLVIITKEEEQKADPKEVSNSKTKTIFPKVLGKSQSKHISRNRSEMSSSSLAPHRVPLSQTNHALTGGLEPAKINITAKAPSTEYNQSHIKALLPEDSGTHQVLRIDVTLSPRDPKAPGQFGRPVVVPHGKEKEAERRWKEGNFNVYLSDLIPVDRAIEDTRPAGCAEQLVHNNLPTTSVIMCFVDEVWSTLLRSVHSVINRSPPHLIKEILLVDDFSTKDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLDSHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYMTVDNFQRGIFVWPMNFGWRTIPPDVIAKNRIKETDTIRCPVMAGGLFSIDKSYFFELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRNDNPYSFPKDRMKTVERNLVRVAEVWLDEYKELFYGHGDHLIDQGLDVGNLTQQRELRKKLKCKSFKWYLENVFPDLRAPIVRASGVLINVALGKCISIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHKSTSVFHPELVNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYYEA | 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 Activity: L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 106266
Sequence Length: 940
Domain: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.41
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O61394 | MIASLIRSRRRSRRCVVYSVFLFGFLALWGSFALALVFLSDMYIGEDQISTQKAIKPIARSNYHVVVGHYNGNLPEDKKRNLTSEELNANLYAPHDDWGEGGAGVSHLTPEQQKLADSTFAVNQFNLLVSDGISVRRSLPEIRKPSCRNMTYPDNLPTTSVIIVYHNEAYSTLLRTVWSVIDRSPKELLKEIILVDDFSDREFLRYPTLDTTLKPLPTDIKIIRSKERVGLIRARMMGAQEAQGDVLTFLDSHCECTKGWLEPLLTRIKLNRKAVPCPVIDIINDNTFQYQKGIEMFRGGFNWNLQFRWYGMPTAMAKQHLLDPTGPIESPTMAGGLFSINRNYFEELGEYDPGMDIWGGENLEMSFRIWQCGGRVEILPCSHVGHVFRKSSPHDFPGKSSGKVLNTNLLRVAEVWMDDWKHYFYKIAPQAHRMRSSIDVSERVELRKKLNCKSFKWYLQNVFQDHFLPTPLDRFGRMTSSSNSSVCLAWTLRSSGIKTASTADCLKIFHKTQLWLYTGDRRIRTDEHLCLSVVQLLHTTSDWKIQLKECAGFDTEYWDFKPKIGRFQNRKTGLCLASPDIFDPTKDEFNPPIVQKCRSSNDRQNWTITEMSWLPEHP | 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 that transfers GalNAc onto serine or threonine residue on peptides that have been tested. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 71115
Sequence Length: 618
Domain: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q6WV16 | MRRPNLKWIVKASLLLLISLTLFVLITSWISSTPYTNKPVHHGVEPVPEKAGLSGDVKVKVPAIKQPEPQKPQEPDFEEDPELQKIDEPEPVEEEVDNPHPADDEPQQQPQEELQMAAPADASVKKDWHDYTFMEKDAKRVGLGEGGKASTLDDESQRDLEKRMSLENGFNALLSDSISVNRSVPDIRHPLCRKKEYVAKLPTVSVIIIFYNEYLSVLMRSVHSLINRSPPELMKEIILVDDHSDREYLGKELETYIAEHFKWVRVVRLPRRTGLIGARAAGARNATAEVLIFLDSHVEANYNWLPPLLEPIALNKRTAVCPFIDVIDHTNFHYRAQDEGARGAFDWEFFYKRLPLLPEDLKHPADPFKSPIMAGGLFAISREFFWELGGYDEGLDIWGGEQYELSFKIWMCGGEMYDAPCSRIGHIYRGPRNHQPSPRKGDYLHKNYKRVAEVWMDEYKNYLYSHGDGLYESVDPGDLTEQKAIRTKLNCKSFKWFMEEVAFDLMKTYPPVDPPSYAMGALQNVGNQNLCLDTLGRKKHNKMGMYACADNIKTPQRTQFWELSWKRDLRLRRKKECLDVQIWDANAPVWLWDCHSQGGNQYWYYDYRHKQLKHGTEGRRCLELLPFSQEVVANKCDTDNRFQQWNFGSFNKTALDNYSQDLVLSL | 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 threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties . Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified . Prefers the diglycosylated Muc5AC-3/13 as substrate . Might have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure .
Catalytic Activity: L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 76972
Sequence Length: 666
Domain: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.41
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O61397 | MIIARKKLQLQRLWRQRGCRVATYICLGVLVLFGFVYNSKGNSMSSIKSDSAAQQFDDLDDLTNKELPGGPDPNTIFRGSELGNYEPKEPEIPSNQPGEHGKPVPVTDEEGMAAGRAAEKEFGFNTYVSDMISMNRTIPDIRPEECKHWDYPEKLPTVSVVVVFHNEGWTPLLRTVHSVLLRSPPELIEQVVMVDDDSDKPHLKEKLDKYVTRFNGKVIVVRTEQREGLINARSIGAKHSTGEVVLFLDAHCEVNTNWLPPLLAPIKRNRKVMTVPVIDGIDSNSWEYRSVYGSPNAHHSGIFEWGLLYKETQITERETAHRKHNSQPFRSPTHAGGLFAINRLWFKELGYYDEGLQIWGGEQYELSFKIWQCGGGIVFVPCSHVGHVYRSHMPYSFGKFSGKPVISINMMRVVKTWMDDYSKYYLTREPQATNVNPGDISAQLALRDKLQCKSFKWYMENVAYDVLKSYPMLPPNDVWGEARNPATGKCLDRMGGIPGPMGATGCHGYGGNQLIRLNVQGQMAQGEWCLTANGIRIQANHCVKGTVNGFWSYDRKTKQIIHSQKRQCITVSESGSEVTLQTCTEDNERQKFVWKEFYQSS | 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 that transfers GalNAc onto serine or threonine residue on peptides that have been tested. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 68108
Sequence Length: 601
Domain: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q8MV48 | MRVSTIRSGRICRLALCLLVLLPLLYLLANWSDHHKRVQEAYHTRFGGPKFAHQRLEGRPREVPKLVDGLGNFEPKDVKPRSGPGENGEAHSLSPDKKHMSDASEMEYGMNIACSDEISMHRSVRDTRLEECRHWDYPFDLPRTSVIIVFHNEGFSVLMRTVHSVIDRSPTHMLHEIILVDDFSDKENLRSQLDEYVLQFKGLVKVIRNKEREGLIRTRSRGAMEATGEVIVFLDAHCEVNTNWLPPLLAPIYRDRTVMTVPIIDGIDHKNFEYRPVYGTDNHFRGIFEWGMLYKENEVPRREQRRRAHNSEPYRSPTHAGGLFAINREYFLELGAYDPGLLVWGGENFELSFKIWQCGGSIEWVPCSRVGHVYRGFMPYNFGKLASKKKGPLITINYKRVIETWFDDTHKEYFYTREPLARYLDMGDISEQLALKKRLNCKSFQWFMDHIAYDVYDKFPGLPANLHWGELRSVASDGCLDSMGHQPPAIMGLTYCHGGGNNQLVRLNAAGQLGVGERCVEADRQGIKLAVCRLGTVDGPWQYNEHTKHLMHRVHKKCMALHPATQQLSLGHCDVNDSYQQWWFKEIRPRW | 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 threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties . Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified. Prefers the monoglycosylated Muc5AC-3 as substrate . Might have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure .
Catalytic Activity: L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 68333
Sequence Length: 591
Domain: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.41
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Q86SF2 | MRLKIGFILRSLLVVGSFLGLVVLWSSLTPRPDDPSPLSRMREDRDVNDPMPNRGGNGLAPGEDRFKPVVPWPHVEGVEVDLESIRRINKAKNEQEHHAGGDSQKDIMQRQYLTFKPQTFTYHDPVLRPGILGNFEPKEPEPPGVVGGPGEKAKPLVLGPEFKQAIQASIKEFGFNMVASDMISLDRSVNDLRQEECKYWHYDENLLTSSVVIVFHNEGWSTLMRTVHSVIKRTPRKYLAEIVLIDDFSNKEHLKEKLDEYIKLWNGLVKVFRNERREGLIQARSIGAQKAKLGQVLIYLDAHCEVAVNWYAPLVAPISKDRTICTVPLIDVINGNTYEIIPQGGGDEDGYARGAWDWSMLWKRVPLTPQEKRLRKTKTEPYRSPAMAGGLFAIEREFFFELGLYDPGLQIWGGENFEISYKIWQCGGKLLFVPCSRVGHIYRLEGWQGNPPPIYVGSSPTLKNYVRVVEVWWDEYKDYFYASRPESQALPYGDISELKKFREDHNCKSFKWFMEEIAYDITSHYPLPPKNVDWGEIRGFETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGADGSKVMITHCNLNEFKEWQYFKNLHRFTHIPSGKCLDRSEVLHQVFISNCDSSKTTQKWEMNNIHSV | 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 threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified.
Catalytic Activity: L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 75389
Sequence Length: 657
Domain: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.41
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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 in limb myogenesis. May be involved in the regulation of the apoptosis in the interdigital tissues of the developing hindlimb. May be involved in the membrane ruffling process.
PTM: Cleaved, during apoptosis, on a specific aspartic residue by caspases.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34901
Sequence Length: 314
Subcellular Location: Cytoplasm
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Q9USU5 | MVSFTKFTLQLLSASAAFAYFEPLTIKGRKFFKNDTQFYIKGVAYQPAVDAEETSTIVDPLAEVNYKNCTEDAKIISNLGANVIRVYAVNASLNHDKCMEAFRNESIYVFLDLANPKTGIDRDTPTWNTDQFSSYQSVIDTFQKYNNTGAFFAGNEVVNNASNAPAVAYVRAAVRDSKNYIKSKKYRTIPVGYAGADIPVVRTELAAYLSCNATKLNNDTNSETDFLGYNMYEWCGHSDFYTSGYAARTQELENFTIPIFLSEFGCNKVTPRVFTEVQAIYSDNMTNVWSGGIVYEYSQEVNDYGLVNVSSTGERVLTTDYNNLKKQWASISPNITYKHSYNPNGTIPECPSRNKTSWAVSANAFPVTPNTTICSNAVKNLKCSANGTPSGSKISQVLSELCYYDNKACSSISSDPYEGTYGNYTGCTGVQQLSIALNAYTQDHGADSCSWGGVGELKA | 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
Sequence Length: 459
Subcellular Location: Endoplasmic reticulum lumen
EC: 2.4.1.-
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Q06135 | MNKKQNFYAAIIVAIFLCLQLSHGSSGVSFEKTPAIKIVGNKFFDSESGEQFFIKGIAYQLQRSEEELSNANGAFETSYIDALADPKICLRDIPFLKMLGVNTLRVYAIDPTKSHDICMEALSAEGMYVLLDLSEPDISINRENPSWDVHIFERYKSVIDAMSSFPNLLGYFAGNEVTNDHTNTFASPFVKAAIRDAKEYISHSNHRKIPVGYSTNDDAMTRDNLARYFVCGDVKADFYGINMYEWCGYSTYGTSGYRERTKEFEGYPIPVFFSEFGCNLVRPRPFTEVSALYGNKMSSVWSGGLAYMYFEEENEYGVVKINDNDGVDILPDFKNLKKEFAKADPKGITEEEYLTAKEPTEVESVECPHIAVGVWEANEKLPETPDRSKCACLDEILPCEIVPFGAESGKYEEYFSYLCSKVDCSDILANGKTGEYGEFSDCSVEQKLSLQLSKLYCKIGANDRHCPLNDKNVYFNLESLQPLTSESICKNVFDSIRNITYNHGDYSKSNPSRSKESLNVKYPSSEERENDGTIAFKTSGFVILLISMIAAGILL | 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.
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 62362
Sequence Length: 555
Subcellular Location: Cell membrane
EC: 2.4.1.-
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Q03655 | MQLSKSILLAALAATPSLVNAMLPIHIKNYRFIKPSSATNSESDNEVFFVKGVDYQPGGSSGYDADSDTDILSDPEVCARDAYAFQQLGVNTVRIYSLNPDLNHDKCMTIFNNAGIYAILDVNSGNYGESLNRADPSGTYDSLYLSRVFKFIDAFKNYPNVLGFFSGNEVINDQSDYAKIDPPYIRAVQRDMKQYISKHANRSIPVGYSAADNTDLRLATFKYLQCNSLDGNKVNDDLDISKSDFFGLNTYEWCSGTSSWESSGYDKLNSTFEDAVIPLIFSEYGCNKNTPRTFDEVSEGLYGGLKNVFSGGLVYEYTEEANNYGLVKLDDSGSLTYKDDFVNLESQLKNVSLPTTKESEISSDSIYKCDNSAITNIYSGFGTNNFTLPSQPAEIANMIEYGVNGTNTGKILTDYAVPTTFNYTIKNNKDDTISATISYDKANSLNELDVTATTVAKSASTSQSSSRSLTSSTSPSSSTGSSSSTGSSSASSSSKSKGVGNIVNVSFSQSGYLALFAGLISALL | 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 biosynthesis and morphogenesis (By similarity).
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
Location Topology: Lipid-anchor
Sequence Mass (Da): 56794
Sequence Length: 524
Subcellular Location: Secreted
EC: 2.4.1.-
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Q9Y7Y7 | MGVANIIYALFLLGPSIFLKATAQTHPIVIKGNAFFDSKTNERFYIRGVDYQPGGSSSLVDPLASRSCKKDVEIFKKLGINTVRVYQVDNSADHDKCMNALSEAGIYVILDLNTYRHSISRAHPALSYNKVYLQHLFATIDAFKGYDNVLGFFSGNEVVNDEDTTAITWVKAVTRDVKAYIKKHSDRHIPVGYSAADVAENRLQLAHYFNCGDESERADFYAFNMYEWCGYSSMTVSGYYDRIKEFSNYSIPLFLSEFGCNTVEINDDTTPNRPFTEIEAIYSHDMTPVFSGGLVYEYSAEPNHYGLVVIDKDDERRVSRNFITLMKQYAKTPNPKGDGGYKKAGSPSKCPANSTQFNAWEKLPEMPEGAKIYMEKGAGEPLGIEGPTNMWSPFHDGDDDESTSRRPKPKNKPSNVTSTTSYTSGMTSSSESGSSKIGVAFCQALFITVLIATLSF | 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.
Location Topology: Lipid-anchor
Sequence Mass (Da): 50763
Sequence Length: 456
Subcellular Location: Cell membrane
EC: 2.4.1.-
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Q08271 | MMVFSSTFIFLILELVVLCEASVHTIQIKDKHFVDTVTGKPFFIKGVDYQPGGSSDVSEKQDPLSNPDACARDILLFQELGINTVRIYSINPDLNHDACMTMLAMAGIYLILDVNSPLQNQHLNRYEPWTTYNEVYLEHVFKVVEQFSHYNNTLGFFAGNEIVNDKRSAQYSPAYVKELIGTMKNYISAHSPRTIPVGYSAADDLNYRVSLSEYLECKDDDKPENSVDFYGVNSYQWCGQQTMQTSGYDTLVDAYRSYSKPVFFSEFGCNKVLPRQFQEIGYLFSEEMYSVFCGGLVYEFSQEDNNYGLVEYQEDDSVQLLADFEKLKSHYQNIEFPSMKTLKETVQMEETPSCAEDYENLKIESKIAKNLGSSLIKKGVKVEKGKYIDIHEDQLSTNVTILDKHGDRWNGPKKIEIRQSLTLADLEGEEQEDADEDKDDLKRKHRNSASISGPLLPLGLCLLFFTFSLFF | 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.
Location Topology: Lipid-anchor
Sequence Mass (Da): 53813
Sequence Length: 471
Subcellular Location: Cell membrane
EC: 2.4.1.-
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O13692 | MNFLHFLTTSLLLLGGSRLALADSASSAIKIKGNAFFNSDTNERFYVRGVDYQPGGSSTLVDPLADTSICKRDLPYLQGLNINTIRVYQVDNSANHDECMSALQDAGIYVILDLATSSNSISRLDAASSYNAVFLQGIFATIDAFKNYTNVLGFFAGNEVANTAENSATTTWVKAALRDAKEYISKNSDRDIPVGYSAADVAEIRVQCADFFACGNSSVRADFYGMNMYEWCGADSSFTISGYDQRMEEFANYSIPLFLSEYGCNDVTKESDGTPDRPFDEVDAIFSSEMSSVFSGGLVYQYSEEGNNYGLVVIDGDNVTISKNYETLKEKYASAANYTGDGDYSSSPATLTCPADDSYFTSFPLPTMPSEAKGFIESGAGQPLGFNAPSNQEFSANATALVSPGPHSVSTTINTNIVQATISQSSTSGSSSGSSSASTTASSSSVSSGSSISSGSSSMSTSYTSASGSSAHSSGSSSGSSSATSSASTFNLSRFYVFAGILAISGLVFA | 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 to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
Location Topology: Lipid-anchor
Sequence Mass (Da): 53693
Sequence Length: 510
Subcellular Location: Secreted
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