ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A0RPL1 | MQENSCEYLKHCGSCTLDMPYSEQIDFKKNFIKEHFKDFHNGEIIFFRSPISKFRSRAEFGLYHDDNSLSYTMRRADGGYLKIDKCSIVDEKISVIMPVLLDLLKENQNLKAKLFGVEFITTRDEILIILLYHKDASTIIQELTWLQSKLKVGLIARSKGKKLVFGSSSLNEKLFINGKSYHYVFGDAAFIQPNRNINENMISWVLDHTTDCKDLLELYCGHGNFTIPLSFKFNKVLATEISKASINSALKNCELNGVDNIKFTRLSAEELMEAFLFKRDFRRLQDIDLRSYEFSHILVDPPRAGCDKSVLDFIRNYENI... | Function: Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
Catalytic Activity: S-adenosyl-L-methionine + uridine(54) in tRNA = 5-methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine... |
Q9PP92 | MSLENFGNFLTLDEKHSFIKKYFKEFYTKDFKLFASKDKHYRTRAELSFYHENDTLFYAMFDPKSKKKYIIEYLDFADEKICAFMPRLLEYLRQDNKLKEKLFGVEFLTTKQELSITLLYHKNIEDIKSNLENLSNILHINLIARSKGKKLIFKTENLRQTLNIQDRKIFYEFNNDCFIQPNTAINEKMITWVCEILNTQKRMDLLELYCGYGNFTLALAPFFFKILATEISKSNINFALKNCELNNTTNIHFARLSSEELSLAIKKEREFFRLKDIRLDDFNFSHVLVDPPRAGLDKSVIDLIKKYGNIIYISCNPMTL... | Function: Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
Catalytic Activity: S-adenosyl-L-methionine + uridine(54) in tRNA = 5-methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine... |
B3PJ74 | MPQPQQHTADYSSAAYEAQLQQKLIRLNQDFASFNLPEISVFRSPEKHFRMRTEFRIWHERGTAMYVMFSQTDKRPYPIREFPIGSERINQLMPELMALVNRHECLRHKLFQVEFLTSLSNQALITLVYHKPLDEEWISAATDLRKQLNVEIIGRSRKQKILLERDHIIECLKVNGREYRYQQVEGSFTQPNARVCEQMLSWAQEQTRHTGGDLLELYCGNGNFTLPLAQNFDRVLATEISKTSVDSALYNSRLNQVENLQIARMSSEEFTQAMDGVREFNRLKHISLNDYRFSTIFVDPPRAGLDPATCHLAQRFDNIV... | Function: Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
Catalytic Activity: S-adenosyl-L-methionine + uridine(54) in tRNA = 5-methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine... |
Q48A12 | MFSHIHPDNYDAQLSKKQQDMAKLFSDFNLPAPDLYPSVPLNYRQRAEFRVWHEGDDLYYIMFDSKTKEKFRVDDFPVASELINNAMKALLATIKDQRELRFKLFQVDFLSTLSGELLISMLYHKPLEDNWQIEAEKLKAQLSTIAPVDIIGRAKKQKIIVDKDYVMESLNVGGKTYVYQQVENSFTQPNAGVNEQMLLWAQQATQNAGGDLIELYCGNGNFSIALAENFERVLGTEISKTSVRSAQINISENGIDNIDIVRMSSEEFSQAMNGERKFRRLEDFDLTTYNYDTVLVDPPRAGLDRDSVELVRRFNKIIYI... | Function: Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
Catalytic Activity: S-adenosyl-L-methionine + uridine(54) in tRNA = 5-methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine... |
A5EXH9 | MTMSNYQRQLFAKHQQLHALLRPFSAPKIRIYPSPEKHYRMRAEFRIWRDDEQLFYAMSRGGALTAQNIVRLHNFPPAYITIDRCMPLLLDALRADPVLHHKLYEVHFLASLRGELLVSLIYHRALTDEWTAAAKALAKRFHILLIGRSRKQKITLERDFILETLNVDGRAFHYHQYEQSFSQPNAYVCQKMLRWACAQAGENAGDLLELYCGNGNFTLPLASHFRRVLATEISKSSITALQENIFLNQTNNIAVARLSAEEFTQAWQKERDFYRLKQAGIELADYQFETVFVDPPRAGIDDNTLFLLQKFPKIIYISCN... | Function: Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
Catalytic Activity: S-adenosyl-L-methionine + uridine(54) in tRNA = 5-methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine... |
A3DBL4 | MRLRKKPWARPALEACSFFVINPTEYKGKWREVFGNSNEIWLELGCGKGGFISKLASTNPDKNFIAVDIKDEVLALAMKKIENEYALIGAETKNIRLMAHEIMLIHRMLDENDQIGRIFINFCNPWPKNRHKARRLTHPNQLNQYRTFLAPNGQIWFKTDDTMLFQDSIKYFEQCNFNIVYLTEDLHASGFEGNIETEHERMFLEQGCKIKFLIAEKK | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25550
Sequence Length: 218
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q6FCN6 | MSHTKIMSTDQLETQITELDNLPEHREIVTFMRRSAPLNTSQRSALEQYQDLILEYPVGDLRQHFEHPEHPLTVEIGFGMGRSLVLMAKAHPERNFVGIEVHVPGIAQCVYEAGMAGLKNLRVLDADAIQVLREMPDNSINCVQLYFPDPWQKKRHFKRRFVIHERMQLVEQKLELGGTFHAATDWEPYAEWMLDVLDNRPALENLAGKGNSYPRPEWRPQTKFERRGIESGHKINDFIFKKIGS | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28398
Sequence Length: 245
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
B7J415 | MEEALKTSHRAIRSFVLRQGRITAAQTRAVAEYLPARQIDAHAEWRDPWNNQRPLMLEIGFGNGEHLAAIAAQRPTWGCIGIEVHTPGVGSLLLQLVEAGTDNVRIVHDDAVTWLKTLPDAILRCIIIQFPDPWPKKRQQKRRLIQPDFAAVLCRLLQPGGELQLATDWADYAGQMLTVLNATPGLQNADADNGYVFRPDNRILTRFERRGQRLGHAVYDLCYRRIP | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25673
Sequence Length: 227
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q0IEN3 | MEVEESKNDASVVASPAPTKLPQKRFYRQRAHSNPIADHSFDYPIHPDDYDWSQHYPTIGDKRVEFADIGCGYGGFLVTLGEMFPDKFAVGMEIRVKVSDYVMDRIQALRKLNEGQYENIACIRTNAMKYLTNFFHKGQLEKMFFLYPDPHFKKAKHKWRIINSALLSEYSYVLRQGGLIYTITDVKDLHEWMCKHIEQHPAFERLTDDEVKADVLSEKLLDSSEEGKKVTRNKGDKFVAIFRKI | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28519
Sequence Length: 245
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q0VLC7 | MLDFINHDKDPETGKVMRKVRSFVLREGRLTAGQRNALDTLWPRFGLERDQGMLNPESVFGRDAPRVLEIGYGMGQSLAQMAAADPDKDFIGIEVHRPGVGALLMEIEQQGLSNLRSYCDDAVEILELCIPDNSLARVQLYFPDPWHKKKHHKRRIVQPAWVALVQRKLQPGGILHMATDWENYAEHMMEVMDAAAGFSNLAGPSAFSPRPSWRPETKFERRGEKLGHGVWDLLFEKRA | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27171
Sequence Length: 239
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q6A6S9 | MRPDPAPLDPTDASPAQARRHQPGLGVEVSAGAHRSGDRVRRGVVSFVRRSPRMNVSQQRAMNTLASTYLIDVPRDATSTSVAPGSRLDLPAIFGRTAPLTVEIGVGSGDVLAALAAAHPERDFIGFEVYLPSIATTLNKLENAGASNARVIMADATAGLDHLFGPADLDELWTFFADPWHKKRHHKRRIVNPDTARLVTSRLRPGGLWRLATDWDDYAHWMLEVLSAEPLLKPVDAGPDGFSPRWPERPVTRYENKGLTAGRTIHDLTWRRVDES | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30383
Sequence Length: 276
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q11UV2 | MARKKLMRFKWNEEVHNLFQPEKENYKAYKGKWHEYFKNDNPVILEVGCGRAEYTTGLAALFPENNYIGLDIKGARLWKGSSLSIETGLTNTAFIRTKLQNLEEFFEPGEVKGIWITFPDPKPRESEAKLRLSGLRFMNIYRRLMPAGGKVFFKTDNRVLFDHTLEVLTDQTLKIKDLVFTHDLYQSPLLAEHYGIQTTYEKTYLNQGVQINYLKFEFLPL | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25884
Sequence Length: 221
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q5XJ57 | MSVCMPQKRYYRQRAHSNPMADHTFQYPVCPEQMDWSPLYPQYFPQQEEAGGAQVEFADIGCGYGGLLVQLSQLFPQQLILGLEIRVKVSDYVQDRIRSLRVAEPGRYQNIACLRSNAMKYLPNFFRKGQLSKMFFLFPDPHFKKTKHKWRIISPTLLAEYAYTLRIGGLVYTNTDVEEVHEWIVQHFSDHPLFSRVTEEQLADDIIVGHLGTCTEEGKKVQRNGGKNFLAVFRRVEDPQT | Function: Catalytic component of METTL1-WDR4 methyltransferase complex that mediates the formation of N(7)-methylguanine in a subset of RNA species, such as tRNAs, mRNAs and microRNAs (miRNAs). Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in a large subset of tRNAs that contain the 5'-RAGGU-3' m... |
Q9RTS6 | MIFRLGDFRFPDDPARLYPDTPDRPWVLEIGFGDGRFWPHYARTFPEPPNYLGVEISGVSLLKAHRRLKDAGLTNAVLTKLPAEVLVAQVIPHGSLDAIIVNFPDPWPKAGHEDHRLLRVPFFQVAASRLKPGGAALLTTDHDEYFEFACAQAEASGVMRVERVGPPPAALETKYAQKWRDLGLGVNHARFVPTRHDPVPNGTFAPYSEEDPAVPHAVLTLPADFSPQHFDKLTVRGKTWTVVLLDLYATLRRGGWVALAHVVEGDLTQEVLVGITEREDGTHLVRLAKFGGPIITPGVKAAVGAVTEWLEGQGAVVKHR... | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35470
Sequence Length: 322
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q551M3 | MVYQKQEPKKKKAIKPYHRIKAHANPASDYNFYYPTGPESYDWTKNYPQQAMNEKKVEIADVGCGYGGLLISLSSLFPERLSVGMELRDKVVQYVEERIDKLREKHVGQFQNISVIRTNAMKYLPNYFEKGQLQKIFFLFPDPHFKKATHKRRIISPTLLSEYAYILAPGAYAYFISDVEELYLWMFEHFKNHPLFEQVERDIAENDSCIPLIVNSTEEGRKVNRIDGKKWFAVFRRITDPSKKDLTFKNYTLTSPKEIDSTTTTTTSTATITEVESK | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32423
Sequence Length: 278
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
B3MYY4 | MARDSEDQDMETETNGAAEGLDPTSAVTGLPQKRFYRQRAHSNPIADHSFDYPARPEDVNWRALYPSIQPDQKVTFADIGCGYGGFLVTLGEMFPEKFSIGMEIRVKVSDYVMDRITALRHKSGEAGAYKNIACLRTNAMKYLPNYFAKGQLEKMFFLYPDPHFKRAKHKWRIINQALLSEYAYVLKKGGLVYTMTDVEDLHQWIVQHMEEHPLYERLKEEEEQSDPITPKLYQSSEEGAKVVRNKGDHFLAIFRRL | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29691
Sequence Length: 257
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
B4JLU7 | MVTNKKEDEALSTTSAVTGLPQKRFYRQRAHSNPIADHSFDYPARPEDVDWRSLYPSINDEQQVEFADIGCGYGGFLVTLGEMYPKKLSIGMEIRVKVSDYVVDRIAALRLKNSETAAYQNIACIRTNAMKYLPNYFRKSQLEKMFFLYPDPHFKRAKHKWRIINQALLSEYAYVLRTGGLVYTMTDVEDLHKWIVSHMTQHPLYERLSDEATKADPITPKLYQSSEEGAKVVRNKGDHFLAIFRRI | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28622
Sequence Length: 247
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
O77263 | MVATGGQAQDQGQNQEPDVLNPTSAVTGLPQKRYYRQRAHSNPIADHSFDYPARPEDVDWRSMYPGIQQGQQVSFADIGCGYGGFLVTLGEMFPEKLSIGMEIRVKVSDYVVDRIAALRRRCADTGAYQNIACLRTNAMKYLPNYFVKGQLEKMFFLYPDPHFKRAKHKWRIINQALLSEYAYILRKGGLLYTMTDVEDLHKWIVTHMEEHPLYERLTEEEANADPITPKLYQSSEEGAKVVRNKGDHFLAIFRRL | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29425
Sequence Length: 256
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q03GC9 | MRVRNKPWAPELIEAHPEKIVEKGQAFKGQWNQRFEKEQPIFIEVGTGKGQFIINMAKKYPQYNFIGIEIQKTVIAIALKNALEEEIPNLQFLYADGAELTDYFEDGEVSKVFLNFSDPWPKTRHEKRRLTFKTFLKVYEQILVKNGEVEFKTDNQGLFEYSLYSLNNYGMTFEGVWLDLHNSEENEDNVETEYEHKFSAKGQPIYKLKAHF | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24942
Sequence Length: 212
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q0TZT0 | MPHAPAKRQKREEYKNALHEDESNAALPKKKFYRQRAHANPFSDHSLTYPKSPADMDWASLYPAYAVVKREQKSAGEEESTPLDEEEQRRLKAITKNVEIADIGCGFGGLLFALAPKFPDTLMLEYVQEKVRALRLQNASIQLYQNASCLRANTMKFLPNFFSKAQLSKIFLCFPDPHFKQRKHKARIVSYTLNSEYAYVLRPGGVVYTITDVKDLHEWMVGHFEKHPSFERCEKEFEEEGEAMDEGVGIMRTETEEGKKVSRNGGMKYVACFRRVEDPEWP | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32547
Sequence Length: 282
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q7MVS9 | METFPHVFQYPFAVLQQQESGFPLRGRWHTDFFHNDHPIVLELGCGRGEYTVGLGKRFPEKNFIGIDIKGARMWAGAKESLQEGMSNVAFLRTDIELLDRFFAEGEVAEIWITFPDPQMKKVGKRLTGTRFLSLYDKVLERGGRIHLKTDSPFLYTYTKALVELNGLPVHEITDDLYGKGCVENEILGIRTYYEQQWLERGLTIKYISFGLGEPDCEYREPDIEIEPDSYRSYNRSRRSQAVPS | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28215
Sequence Length: 244
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
A2BUM1 | MRQHVNPLSKNFFEIDPIPPLNEVFENPQLPLHLDIGCASGDFLMELSLKNKNWNYIGIEIREKLVLNANLKIKNREYKNVYFSFGNAINILNNTNNKTLIDAITSISFYFPDPWFKKKHHKRRVIQPEFINLLSNAMRTRSLIFIKTDVQELFEYMELTILESLKFKKLAYEDFRVNESFNPIKTQTKREKYVLLSQFEIYESIYIRI | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24918
Sequence Length: 209
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
A0LV70 | MHVDIVSIFPEYFRPLELSLIGKARARGVLDVHLWDLRDFTHDPHRTVDDTPYGGGPGMVMRPEPWGETLDAVRAEAARLGVDAPLLIVPTPAGELLTQRAAERYAAEPWLAFACGRYEGIDERVLLDARRHMRVEEVSIGDYVLAGGEAATLVIVEAVARLLPGVVGNQASVLDDSHAQGLLEGPAYTKPAVWRGLEVPEVLLSGNHAAIARWRREQAIRRTAVRRPELLDALPPGSLTPHEEALAAEARLHAGRSAETPPPAGAAGSQAEGPPGTSPSDAAVAH | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30687
Sequence Length: 286
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q0VRF0 | MMTTKPTFAVTLVTLFPEMAQAITGFGVTRRAVDNGQLQVETVNPRDFTEDRHRTVDDRPFGGGPGMVMKVEPLAKALQAARVANPAAKVIYLSPQGQPLTQAKATALAEQPGLILLAGRYEGVDERLLDAEVDEQISIGDYVLSGGELPALVLIDAVSRLIPGVLGHQDSAEQDSFSGEFENLLDCPHYTRPEVYGEQAVPPVLLSGNHELIRRWRLKQALGRTWQQRPDLLEARRARGLSKEEQQLLDEYIAEQPSHTAKTTD | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29160
Sequence Length: 265
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
A6TRS6 | MKVRILTLFPEMFNGPFGTSILKKAQEKELIDIQCFNIRDFALNKHKKVDDYPFGGGAGMVMTPQPIFDCHHHVTQMLNLNEPCKTIYLSPKGSTFTQEKAMELAKEEQLIFLCGHYEGIDQRIIDELVTDEISIGDYVLTGGELPAMVIVDAITRLIPGVLSTEASYEDESFHCGLLEYPHYTRPRAFNGLEVPSVLLSGNHKDIDMWRRKQSIELTFERRPDLLKGLQLKKNEAQWVAELSKKKE | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28173
Sequence Length: 247
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q6A7S7 | MRLDYLSIFPAYFDVLDISLLGKAAVNGLVEVHAHDLRDWTHDRHRTVDDTPCGGGAGMVMKPDPWGEAFDEIIGTEPDSSVHVIFPSPSGAPFTQSAAQELSSAVRIVFCCGRYEGIDHRVIDYARSMWTVHEVSLGDYVLNGGEVAALAITEAVVRLVPGFMGNPESLAEESFSAGQDGLLEYPLFTRPVSWRGLDVPEVLMSGHHGRIAKWRRDESVRLTCERRPDLTDSDFGVPH | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26350
Sequence Length: 239
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q3Z9L3 | MKIDVLTLFPEMFQSPFEESIFKRAADKNLVRLEIHNFRDFSHDKHHAVDDTPYGGGAGMLLKPEPLFEAVEAVMEKDPTPAPVILLSPQGRTFNQSVARELANHQRLIIICGHYEGFDERVREHLATDEISIGDFVLTGGELAAMVVIDAVSRLIPGVLGSDDSSESDSHSNGLLEHPHYTRPPVFRGWDIPEVLLSGNHARIDRWRRKESLRRTLKRRPDMLEKITLSKADRKLIDEILAEENPKD | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28103
Sequence Length: 248
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q1IYA3 | MLTFSFLTLFPELLAPFASEALVGKARARGLLDVQLVNMRDFAENKHLKVDDTPYGGGAGMVIRVDVVERALASLPPADEVILLTPAGERFTQQMAEELSRTTHLAFLCGRYEGFDARVERLATRELSLGDFVMMGGEAAAACVLEAVARLVPGVLGDEDSHRADSFSSGLLDYPEYTRPAEWRGEGVPEVLKGGNHAAVARWRREQALARTLARRPDLLPSAGLTPQDSAYLLTLGVTPEQLAAWGAPPPPLPKRRRGAKPNPN | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28752
Sequence Length: 265
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q6AJE8 | MLFNILTIFPNLLSSPLEEGILKRAQNSGSIDVNIVDIRQYASDKHSTTDARPYGGGEGMVMKAEPLSLAVQDIKKKDAGRVIFLTPQGRKYTQRVAEELAQESSITLVCGRYEGVDERFCEKYIDDEISLGDFILTGGELAALMVVDSVSRILPGVLGCDASVTNDTFSRHLLKHPQYTRPRIFEGLEVPDVLLSGDHQAIEDYRFIASVERTFHKRPGLLKKEIFNKREKKLLKQHNLYSKIVALQDID | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28195
Sequence Length: 251
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
A4J665 | MRIDILTLFPEMFQGPFNHSILKRAQENNLLQIDTINIRDFSQNKHHTVDDTPYGGGAGMVMGPEPLFECFDHLKAKNAGQVGRVIMMCPQGEPFTQEYAKELAREENLVIVCGHYEGIDERVREVLVTDEISIGDYVLTGGELPAMVVVDAVARMIPGVLGETASAEEDSFYNGLLEHPHFTKPREYRGYEVPEILLSGHHGNIRKWRRRQSLLRTLERRPELLKDVELSKEDKKVLLELQNLLLSLNLKQMK | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28963
Sequence Length: 254
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
B2JF31 | MQFDIVTLFPDMFRALTDWGITSRAAKQERYGLRTWNPRDFTTDNYRTIDDRPYGGGPGMVMLARPLEDAINAAKAAQAEQGIGGARVVMMSPQGATLNHDKVMRFAAEPGLILLCGRYEAIDQRLIDRVVDEEVSLGDFVLSGGELPAMALIDAVVRHLPGVLNDAQSAVQDSFVDGLLDCPHYTRPEEYDGVRVPDVLLGGHHAEIEQWRRREALRNTWLKRPDLIVQARKNKLLSRADEAWLASLAKDASKH | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28462
Sequence Length: 255
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q4FP13 | MWQAQIFTLYPDFFPGPLNKGLYGKALTNKIWDLKVVNFREAAEDKHKTVDDTPFGGGSGMLLKADILAKSLDENKKEGERIFYLSPKGKKLDQKLALELSKEKSISLICGHFEGVDERLLSTRNIEELSIGDFILSGGETAAFVVLDSVLRLLPGVLGNEQSKNDESFENGLLEYPQYTKPQIWEEKSVPEVLLSGDHNKIKDWRLSQSEAITRVRRPDLWEKYKKN | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25889
Sequence Length: 228
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
C0QQJ9 | MKFFVLTIFPQFFEGFINTGIVSRAVKKGIVDIKSVDLRDFTEDKHRTVDDVVYGGGPGMLLKPEPIFKAYDSITEKGHKPYVLITEPWGRKFDQKFAEELSKKEEIMIICGRYEGVDERVKSIVDEEVSIGDFILSGGEPAALVIMDAVIRLIPGVVGDSESLNADSFSNDGLLGYPNYTRPAEYRGMKVPEVLRSGNHKLIKLWRRWKQIEKTAVRKPELLKKADLSDSDKKIIDAIKKGLSFEDFLKKYKV | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28794
Sequence Length: 254
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
A4SW75 | MRFDVVTLFPEMFSALTQWGITGRACQQSLASVHLWNPRDFCPDPRKTVDDRAYGGGPGMVMMAKPLEDTVAGIQASHQAAGIKSGPICLLAPQGERFSQKIATDILDYGNLSFICGRYEAVDQRFIDRNVDIQLSIGDFVLSGGEIPAMTIMDAVIRLVPGALGDGESATQDSFMNGLLDYPHYTRPEIYENLLVPDVLLGGHHAKIADWRRQKSLELTLRLRPDLIESARANGLLTREDEQFLRSL | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27464
Sequence Length: 248
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
B5ZC78 | MKISILSLFPELYETWINHSIISNAIKNNQVTIEIINFRLYTNDKHKKVDDYQYGGGAGMVLMIEPIVSAIRAIRTPNSYVILTTPKGQVFNQELANEFVSKYDHIIIIAGHYEGFDERINYYVDAQYSIGDFVLTGGELPSMVISDAVIRLLDGVISSSSLESESFNNYLLDYPVYTRPVVFEGHQVPDVLLSGHHKNIADFRKQQQEMITKKNRPDLYQKYLNSKK | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26088
Sequence Length: 228
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
A5F9A9 | MWVGIVSLFPEMFRSVTDFGVTGQAVKKGLLSVEAWNPRDFAHDKRRTVDDKPYGGGPGMLMMVQPLRDAIHAAKQASPGKTKVIYLSPQGRKLDQQGVEELAQNQNLILICGRYEGVDERIIESEVDEEWSIGDFVMTGGELPAMTLIDSVSRFIPGVLGDFASAEEDSFANGLLDCPHYTRPEVLDGKEVPAVLKSGNHEDIRRWRLKQSLGRTWLRRPELLENLALTDEQEQLLTEYIKETRHQ | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27807
Sequence Length: 247
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q73GD5 | MAFNVTILSIFPEMFPGFLNYSLAGKALEKKIWNLEVINIRSFAKDKHSTVDDVPYGGGAGMVMRSDVVGDAVDSMLSVHKNTKFIYMTPSGTKFNQNIARELLEFPHITILCGRFEGIDQRIIDAYTPYELSIGDYILSGGEPAAMVVLDACIRLLPGVVNNTDSITEESFNYGGGVLEYPQYTRPEQWKGYKVPEVLLSGNHKKISDWRQKQSHVITKKRRPELLSGEINDKFT | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26501
Sequence Length: 236
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q5GT55 | MFDVTILTIFPEMFPGFLNYSLAGKALEKKIWNLQVINIRFFAKDRHLTVDHIPYGGGAGMIMRPDVVGDAVDSVLSTHKDTKFIYMTPSGTKFDQSIARELVGFPHITILCGRFEGIDQRVIDEYTPYELSIGDYILSGGEPAAMVILDVCVRLLPGVVNNSGSITEESFSYSGGVLEYPQYTRPKQWRKHRVPKILLSGNHKKISDWRQKQSQVITKRRRPELLDGEINDKFT | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26641
Sequence Length: 235
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q7TUW5 | MSSFPTVLVIGAGLAGSEAAWQIAQAGVPVRLIEMRPIKHSPAHYSSECAELVCSNSFGALSSDRAAGLLKEELRRLGSIVIRTADSHAVPAGGALAVNRASFSASLTKELSAHPHITIERQEQEHLPDEGQITVLATGPLTSELLAENLRTFTGRSECHFFDAASPIIEGESIDLTLAFRASRYDKGDADYMNCPMDKGQYLAFREALLNAEQAELKEFDKESAKFFEGCLPIEELARRGEDTMRYGPLKPIGLWDPRWGDLNDRDVRRSKRAYAVVQLRKEDLEGRLWNLVGFQTNLKWSEQKRVLKMIPGLHQAEFV... | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 40482
Sequence Len... |
A8F516 | MKVHVVGAGLSGSEIAYQLAIRGLKVILHEMRPSKMTPVHKTSYFAELVCSNSLKSDSIKNASGLLKRELELFGSLILRVARNCAVPAGKALAVDREEFSKQVTHVIRESGIDIVIEELRYIPDSKEDIWIIATGPATSDSFASWLREKVGHNMYFFDAVSPIITADSIDYSVVFRADRYGIGNQDYLNCPMNEYEYDRFYEALINAEVLPVKDFEKDLLFERCKPIEDIAKSGKRSLLFGPMKPTGIIDPRTGKQPFAVVQLRKENLDETLYNIVGFQTRLKWGEQRKIIRLIPGLEKAEIVRYGVMHKNIYINSRKVL... | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 49964
Sequence Len... |
A5V4M8 | MVHQIHVIGGGLAGSEAAWQLAQAGIRVRLSEMRGIEATPAHQTDSLAELVCSNSFRSDDPTNAVGLLHAEMRALGSLIMAKADAHRVPAGSALAVDREGYAEAVTHAVAGHPLIELVRERVDALPADGPVIVATGPLTAAALADSIGAATGADALAFFDAIAPIVHHHSIDMDVAWMASRWDKGETKDYINCPMDKDQYLAFHQALLDGEKTAFKEWEKDTPYFDGCMPIEVMAERGVDTMRYGPMKPVGLDNPRTGRWPYAVVQLRQDNALGTLWNMVGFQTKLKHAEQVRLFRTIPGLGKAEFARLGGLHRNTFIQS... | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 47620
Sequence Len... |
Q5E7Q6 | MSKSFTFKQFHIDIGSCGMPVSTDGVLLGAWADIRACSQILDIGAGTGLLSLMSAQRNSDAHIDAIELMPIAADVARLNFYQSPWKERLTLIHHDFLTYQAPHKYDAIICNPPYFNNGEQSQKGERSTARHTDSLPFDKLLQHCKTLISPTGRASFILPVFEGELFIKVAKNDDFHLTKITKVKTTEKKSPTRLLIELSLFPHIYQESTLTIHDGNGYSDDFIKLTRTFYLNMD | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26383
Sequence Length: 234
Subcellular Location: Cyt... |
Q8A9H7 | MANPFFQFKQFTVWHDKCAMKVGTDGVLLGAWASVQGAHRILDIGTGTGLVALMLAQRSLPDANIVALEIDEAAAGQAKENVARSPWKDRIEVVKQDFLFYQSPDKFDVIVSNPPYFVDSLSCPDQQRSMARHNDSLTYEKLLKGVADLLKKEGTFTIVIPTDVADRVKTAASEYHLYATRQLNVITKPGGTPKRMLITFTFNNEGCIKEELLTEVARHQYSEEYKELTREYYLHLK | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26748
Sequence Length: 237
Subcellular Location: Cyt... |
A0LXM6 | MSNQPFKFKQFSIDQDRCAMKIGTDGVLLGAWASLEHFPDSILDIGTGTGLIALMLAQRSDAELIDALEIEENAYEQSVENFENSDWGDRLFCYHAAFDEFVEEMQDEEKYDLIISNPPFYSENYKTGDEYRDQARFADALPLTELIQGASHLLSENGHLDLIIPFSEERKALEITSSHNLFPNKITRVKGTANSPIKRSLISFNFQKSETVIDELTLEISRHHYTEEFKELVQDFYLKL | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27533
Sequence Length: 240
Subcellular Location: Cyt... |
A8AD10 | MSQSTSTLRRNGFTFKQFFVAHDRCAMKVGTDGILLGAWAPVAGVTRILDIGTGSGLLALMLAQRTDESVTIDAVELDSEAATQAQENIAHSPWPQRITVHTEDVRQWVPRQTARFDLIISNPPYYEQGVECATPQREQARYTTTLDHEALLTTAAECITEEGFFCVVLPEQTGNTFTQQALSMGWHLRLRTDVAETESRLPHRVLLAFSPRTGECFSDRLVIRGPDQLYSEGYTALTQAFYLFM | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27408
Sequence Length: 245
Subcellular Location: Cyt... |
Q11RK8 | MSNSWFQFKQFTVQQDKTAMKVCTDSCVFGATVPVTTSTYTILDIGTGTGLLALMLAQRSNADIDAVELNKDAAQQATDNFFNSPWNERLHVHTCSIQDYFKFTTKQYDLIVCNPPFFSASLKTGNTSKDMALHQSHLLIDELIQVVSFMLKQSGDAYLLISIYEEVNFFQAANRVGLNVKRFQEMYDNETKLIRYVLHLRKDTEHMDHETQNFIIRSADKQYTAQFVEVLRAFYLNL | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27347
Sequence Length: 238
Subcellular Location: Cyt... |
C6CNL2 | MTFQQHTPALRTGGFTFKQFFVAHDRCAMKVGTDGVLLGAWVPLREETRILDIGCGSGLLGLMLAQRSGGRFPIDGVELDAAASTQAADNAAASPWADCIRIYPADIVGYAQTATRRYSLIVSNPPYFSPGVDCASAQRAQARYTTTLTHDALLDCAGRLLEPDGRFCVVLPAVSAEDFLALAQRSAWRADIRVDVADSASRPVNRVLLSLRRGGESEINAIALSRTSLIIRDDDRRYSSSFQALTRDFYLSM | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27554
Sequence Length: 253
Subcellular Location: Cyt... |
C6VS84 | MPRNAHFRFKQFTVRQDQCAMKVCTDACVLGAWADVEDADRILDIGAGTGLLSLMVAQRNTYAMIDAVEIDAEAFYQAGENVEQSPFHDRITLFHSAVQEFVSEHRYDVIITNPPFFQSDLLSPIDKKNIAHHAKSLDFEELLTAIERLLKPEGKFNILFPVDEGSRFAEKAAHAGWKLTRKLTLFHQEDKKAFRLLMRFERAEVAHNVIVEPDLYIYEKDGVTHDPRFRELLKAFYLKF | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27678
Sequence Length: 240
Subcellular Location: Cyt... |
Q8XA22 | MSQSTSVLRRNGFTFKQFFVAHDRCAMKVGTDGILLGAWAPVAGVKRCLDIGAGSGLLALMLAQRTSDSVIIDAVELESEAATQAQENVAQSPWLERINVHTADIQQWVTQQTARFDLIISNPPYYEQGVECATPQREQARYTTSLDHQTLLTCAAECITEEGFFCVVLPEQIGNSFTELALSMGWHLRLRTDVAENEARLPHRVLLAFSPQAGECFSDRLVIRGPDQNYSEAYTALTQAFYLFM | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27243
Sequence Length: 245
Subcellular Location: Cyt... |
Q80ZI1 | MPGCRISACGPGAQEGTAEPGSPPPPPREPLPSLQPPSPSPTSTPTPTKSPPLPEAAETPVEGQELQRWRQGASGGSGGAGPAGIAGAAAGAGGRALELAEARRRLLEVEGRRRLVSELESRVLQLHRVFLAAELRLAHRAESLSRLSGGVAQAELYLAAHGSRLKKGARRGRRGRPPALLASALGLGSCVPWGAGRLRRGQGPEPDSPFRRSPPRGPASPQR | Function: DNA-binding factor that regulates the expression of a subset of genes and plays a key role in tangential, radial, and lateral expansion of the brain neocortex. Regulates neural stem cells proliferation and the production of intermediate neural progenitors and basal radial glial cells affecting the process of ... |
Q96Q11 | MLRCLYHWHRPVLNRRWSRLCLPKQYLFTMKLQSPEFQSLFTEGLKSLTELFVKENHELRIAGGAVRDLLNGVKPQDIDFATTATPTQMKEMFQSAGIRMINNRGEKHGTITARLHEENFEITTLRIDVTTDGRHAEVEFTTDWQKDAERRDLTINSMFLGFDGTLFDYFNGYEDLKNKKVRFVGHAKQRIQEDYLRILRYFRFYGRIVDKPGDHDPETLEAIAENAKGLAGISGERIWVELKKILVGNHVNHLIHLIYDLDVAPYIGLPANASLEEFDKVSKNVDGFSPKPVTLLASLFKVQDDVTKLDLRLKIAKEEK... | Function: Nucleotidyltransferase that catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs, which is necessary for the attachment of amino acids to the 3' terminus of tRNA molecules, using CTP and ATP as substrates . tRNA 3'-terminal CCA addition is required both for tRNA processing and ... |
P96118 | MHALMRLFSDYTLQNVVLGTLFLGLGSGLVGSFAVLRRQSLFGDAVSHATLPGIVIAFLLTGTKSTEILLLGAALSGLVGTVVMLMVMRTTKIDTDGAQGIVLGVFLGFGFLLLTHVQKSPQAAKAGLNKFILGQAATILQRDVLLIIAMEVVIGLLVLLFWKELKLSTFDRDFSAVQGFSPQLMEFMLTALIVVAVVVGVQAVGVILMSALLTAPAVAARQWTNSLRVLCALAALFGGVSGVSGSVVSAQVPRLSTGPVIVLVLTGIALVSIMLGPQRGVLYQLWRRRRVSLLQEEG | Function: Part of an ATP-driven transport system TroABCD for zinc.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31540
Sequence Length: 298
Subcellular Location: Cell membrane
|
P96119 | MTMEVVLIAVVVSVACALCGVFLVLRRISLMSDAISHSVILGIVLGYFLSRTLSSFVPFVGAVIAGICSVICAELLQKTGMVKSDAAVGLVFPAMFGLGVILVSLYAGNVHLDTDAVLLGEIGLAPLDRVSFFAWSLPRSLVQMGSVLCGLLLLLALFFKELKISTFDPVLATSLGFSPTLINYGLMLAVSITCVGAFDSVGAVLVIALMITPPAAALLLTDNLLLMLVLASLLASCASISGLFLAVKIDGSIAGAMATMAGVLFALVYLFSPKHGVVRRCLVMRALKLDLDVVTLAVHLATHRYTVERSVECAEVHLTE... | Function: Part of an ATP-driven transport system TroABCD for zinc.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38764
Sequence Length: 367
Subcellular Location: Cell membrane
|
Q6ETQ7 | MAATTTILSSAAPTPLTAPPRARARAPAARRRRLRARDILGAALGLANGGASAALAAPLSYEETLRLSTDSGGGGGGGGGGEFALPDLGLGGVLDFVAQNPLAAAAGVAAVALPLVLAQVLGGASKPYGVVSAAAAYRALVEEPGAQLVDIRPPGDARQSGAPDLREAKKKAAAVPYDGEDKNGFLKKLSLRFKDPENTTLVILDKFDGNSELVAELVTANGYKAAFAVKDGAEGRRGWLSSSLPWTAPKKGFSLSDLIGDGTDGLPVTLGLAAATGLGILAYTEIETVLQFLGSAAIVQLVASKLIYAEDRKRTLKQID... | Function: Rhodanese domain-containing protein required for anchoring ferredoxin--NADP reductase to the thylakoid membranes and sustaining efficient linear electron flow (LEF).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48403
Sequence Length: 478
Subcellular Location: Plastid
|
Q5SDL7 | MVAMEAMAAMEVMVAAMAATADTVASSAASATATEATVAMDTASLSLPLQLSPRSLPQSSLSATAATVATDTVVSSADTEVSDTEDSAATVSATASLSMLPQSSPRSLPQSSLSATAATVDSVTDMADTAMDTKQFISKGNEHFFAASYLCAWADQSAAGS | Function: Serves as a receptor for ospA protein of B.burgdorferi, the Lyme disease agent. Required for spirochetal colonization. Essential for pathogen adherence to the vector.
PTM: Glycosylated.
Sequence Mass (Da): 16087
Sequence Length: 161
Subcellular Location: Cell membrane
|
B8M9J8 | MPGSLIDTRQQPLSVGIVGGGIIGVILAAGLVRRGIDVKVFEQARGFREIGAGMAFTANAVRCMEMLDPAIVWALRSSGAVPISIGDHQAEARDYLRWVDGYHESSKRLYQLDAGIRGFEACRRDQFLEALVKVLPEGIVECQKRLQKIHEKNETEKVTLEFADGTFAHVDCVIGADGIRSRVRQHLFGEDSPYSHPHYSHKFAFRGLITMENAISALGEDKARTLNMHVGPNAHLIHYPVANETMVNIAAFVSDPEEWPDKLSLVGPATREEAMGYFANWNPGLRAVLGFMPENIDRWAMFDTYDYPAPFFSRGKICLV... | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides . Within the pathway, tropB catalyzes a synthetically challenging asymmetric oxidative dearomatization reaction to convert 3-methylorcinaldehyde into a hydroxycyclohexadione ... |
B8M9K5 | MSIGDEVIPTVDISAWLSSTASPESKNKVVEEVRSACNKYGFFNLVGHGIPAEAREKIFGCTKKFFDLPLEEKMKISVDKSLGKSFRGYEPSLIQTHQDGLLPDTKECFITGAEIPADHPDAGKFSTGPNLWPEGLSDKEFRQPVMEYRALMLDLVSTIVRILGQGIHKAFGHPSDVLNDILINPSIPMRLLHYAPQENPDPRQFGVGDHTDFGCVSILLQQKGTKGLEVWYPPKETWIPVPVIEDAFVINMGDTMHRWTGGYYRSARHRVYITGERRYSVAFFLNGNLNLKIKPLDGSGGEASVGEHINSRLAHTLGDN... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides . The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA . 3-me... |
B8M9J6 | MAYGSQLTLLSGGQSIIILLIVSFLAWRFRVWFRLRHIPGPLGASLTNFVRMSWVFTKKAHLIHQELHQKYGDVVRFGPNMVSISDPASIHIIYPMRKGLVKNDFYVPLRPYTRNRGAIPNVFTALDEDLHMKLKYPVASLFSLSNVSKFEVLVDEVLSVIDEQLDRRFASHGEIFDLTEWLQFFAFDVMGTMTFSKRYGFLEEGKDVGGMLNAIGQFMKQAAPVMQNPWLDRVLYKNRIADSLKRTPGSDIMKFVVAAINERQKSASEDEDFTKARKGKNDFLDEYIITQKKDSNIPPWFVTAWTISNVLAGSDSVGTV... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides . The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA . 3-methylorcinaldehyde is the substrate for the FAD-de... |
B8M9K8 | MVLSDKKFVLVTGGSSGLGFETIKALIQTNQPYHVFLGCLFPDEGQSAVLSLQRDVPETPSTLESILVDVTDDESIDRCFHTVQSKIGHLDVLVNNAGISLQASEIGMREAWNRCYDVNVTGAQIMTHTFVPLLLRSNDPRLIFITSGLSSLTPMSNVYTPTRMTVPAGWPKPEVHPYRAYRATKTALNMVMLEWHWQLREDGVKTWGVSPGFLATNLGASFAGMDGAPPVLPASVGGRLVASVVEGDRDTDVGKIVLKDGEVQPF | Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides . The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA . 3-methylorcinaldehyde is the substrate for the ... |
B8M9K3 | MLHGMSPECALSKLLSSLEFHTLYRYTMTQKHNFPSNNKDTLHLPRILCLHGGGTNARIFRAQCRALEKALRTSFRLCYAEALFPSQPGPDVTAVYRDFGPFRAWIDSPDANPVTMTEALQISICKAIMEDDQRGATGPVVGLLGFSQGAKVCASLILEQQLLGRTFGDHSHLPFRLPQWRFAVLLAGRGPLVTLSHLSVGADIMQKMAHLCENDDSSGLDSQENLGNVILTRELIQVPTIHVHGRKDPALDLHRKLYYDDFDPRYSKVMEWDGAHRVPLKSKDVATLVKEINVLWASVSHSNVQG | Function: Esterase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides . The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA . 3-methylorcinaldehyde is the substrate for the FAD-dependent monooxygenase... |
O27697 | MSGAKSMSYAEMFRRADGCAFVPFVVAGDPDMETSLEIIRTLVDAGADALEVGFPFSDPIADGTSVQGADLRALRAGMTTEKCFQLIERVREFTSIPIGLLVYYNLIYRMGVDEFYRRAAEAGVTGILAADLPPEEASDALRAAEKYDIDQIFIVAPTTGSERLKRISEVSSGFHYLVSVMGVTGARSRVEDATIELIKRVKAEGSLPVMVGFGVSRPEHVRMLRDAGADGVIVGSAIIDVISGNLGDRELMLQRIHEMAGTLKAAGGSG | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 28957
Sequence Length: 270
Pathway: ... |
A6UP14 | MNKPVLVSFLVSGDPNADATLKFMKALDKYSGVIELGIPFSDPVADGATIQAADVRALSNGFKIAKSFEILKEFRKESNTPVILMTYYNPVYNRGIENFVTQAKEAGANGLIIVDLPLQEATEYRKICKKHEMGTVFLSAPNTPEERLKMSDEASTEFLYLISTFGITGARESFEQMTFDFIKRARKTCKGKICVGFGISKGTHAESLIEQGADGVIVGSAFVDIIKTYGDSNEAITKLEELAKELHNGIEKGFEKRNK | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 28526
Sequence Length: 259
Pathway: ... |
B0JXU3 | MTAVTECFRSLRSQGNCALIPFITAGDPDLSTTAQALRILDRAGADLIELGVPYSDPLADGPVIQSAATRALNRGVKLEDVLEIVKNAQGEVKAPIILFTYYNPIYHRGIDVFLDQIKAAGVSGLVVPDLPLEEAESLLQPAAAKGIEVILLVAPTSPPERIQAIALQSQGFIYLVSVTGVTGMRKQVATRVEELLDSIRSVTDKPVGVGFGISEPTQALQVKNWGADAVIVGSAMVKRLADNSPSDGLKSLEEFCRSLKQAIQ | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 28133
Sequence Length: 264
Pathway: ... |
Q740P2 | MTVKQSQASRLSPIFEPCRDDDRAALIGYLPTGYPDVPTSVQAMVALVESGCDIVEVGVPYSDPGMDGPTIARATEAALHGGVRVRDTLAAVEAISAAGGRAVVMTYWNPVLRYGVDAFARDLAAAGGYGLITPDLIPDEAGQWLAASERHGLDRIFLVAPSSTPQRLALTVEASRGFVYAASTMGVTGARDAVSHAAPELVSRVREISDIPVGVGLGVRSREQAAQIGGYADGVIVGSALVSALGDGGLTALRALTEELAAGVRQRAAAS | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 27942
Sequence Length: 271
Pathway: ... |
P16608 | MTTLEAFAKARSEGRAALIPYLTAGFPSREGFLQAVEEVLPYADLLEIGLPYSDPLGDGPVIQRASELALRKGMSVQGALELVREVRALTEKPLFLMTYLNPVLAWGPERFFGLFKQAGATGVILPDLPPDEDPGLVRLAQEIGLETVFLLAPTSTDARIATVVRHATGFVYAVSVTGVTGMRERLPEEVKDLVRRIKARTALPVAVGFGVSGKATAAQAAVADGVVVGSALVRALEEGRSLAPLLQEIRQGLQRLEANPGLKESSKKPLS | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 28937
Sequence Length: 271
Pathway: ... |
A1WSF0 | MSRIEATFRALEDQGRKALIPYVTAGFPFADITPALMHGMVEAGADIIELGVPFSDPMADGPVIQRAGEKALGLGIGMSQVFHQVREFRKRNGTTPVVLMGYANPVERYEQIHGQGAQQGAQGAQEAFVRDAAAAGVDGVLVVDYPPEECTAFAASLRARGMDLIFLLAPTSTAERMAQVAQVASGYVYYVSLKGVTGSGALDRSAVEQMLPRIRQHVRIPVGVGFGIRDAATAQAIGKVADAVIIGSRIIELIEDQEHAKVVPVTIDFLRGIRKALDA | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 29756
Sequence Length: 279
Pathway: ... |
A5CVK4 | MSRLSRVFFDSPKNHKVFIPFITAGDSGLDNTFELMQVLVKNGADVIELGVPFSDPMADGPVISRSYERTVKDGVSLSDVFTVVKKFRQTNNTTAIVLMGYLNPIEVFGYQPFANAASESGVDGVLVVDMPPEEAYGLKQILDGVGINFIFLVAPTTMDERLVFLATIASGFIYFVSLKGVTGAEYLDINLVKTHILRIRQVIDLPIGVGFGIKDAISAKIVSEYADAVIVGSSLVGLVERYANDRTKMLAKVGYLANEISTIIK | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 28826
Sequence Length: 265
Pathway: ... |
O84172 | MFKHKHPFGGAFLPEELLAPIQNLKAEWEILKTQQSFLSELDCILKNYAGRQTPLTEVKNFARAIDGPRVFLKREDLLHTGAHKLNNALGQCLLAKYLGKTRVVAETGAGQHGVATATACAYLGLDCVVYMGAKDVERQKPNVEKMRFLGAEVVSVTKGSCGLKDAVNQALQDWATTHSFTHYCLGSALGPLPYPDIVRFFQSVISAEVKEQIHAVAGRDPDILIACIGGGSNAIGFFHHFIPNPKVQLIGVEGGGLGISSGKHAARFATGRPGVFHGFYSYLLQDDDGQVLQTHSISAGLDYPSVGPDHAEMHESGRAF... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 42618
Sequence Length: 392
Pathway: Amino-acid biosynthesis; L-tryptop... |
Q7NUD8 | MDRYDFPDAQGHFGPYGGVYVAETLMVALDQLKEEYARVKADPTFWQEFHHELKHYVGRPSPVYHAKRWSEQLGGAQIWFKREDLNHTGAHKINNAIGQALLARRMGKKRVIAETGAGQHGVATATVAARYGMECVVYMGAEDVKRQSPNVFRMKLLGATVVPVESGSKTLKDALNEAMRDWVTNVDSTFYILGTAAGPHPYPMLVRDFVSVIGAESKIQMPEAIGRQPDVVVACVGGGSNAIGMFHPYIEVPGVRMVGVEAGGHGVASGKHAAPISSGAPVGVLHGSKSYLMQDADGQIVETHSVSAGLDYPGVGPEHC... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 42969
Sequence Length: 400
Pathway: Amino-acid biosynthesis; L-tryptop... |
A5CRV6 | MTDLRSATGPYFGDFGGRYVPESLVAALDELAEAWEELKVDPAFIEELKELHRSYTGRPSLITEVPRFAEHAGGARIILKREDLNHTGSHKINNVLGQALLTKKIGKKRIIAETGAGQHGVATATAAALFGLDCVIYMGEVDTERQALNVARMRLLGAEVIPVRSGSRTLKDAINDAMRDWVTNVETTNYVFGTVAGPHPFPAMVRDLQKVIGEEAREQVLALTGRLPDAVAACVGGGSNAIGIFHAFLDDADVALYGFEAGGDGADTPRTAATITKGRPGMLHGARSYLLQDEDGQTIDSHSISAGLDYPGVGPEHSWL... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 43087
Sequence Length: 404
Pathway: Amino-acid biosynthesis; L-tryptop... |
B2V2T4 | MDFRTYLKRYPDKNGRFGQYGGAYLTNELIPAFEEIADAYQTICHSSQFISELRRIRKEFQGRPTPVYHCERLSRAIGNCQIYLKREDLNHTGAHKLNHCMGEGLLAKFMGKKRLIAETGAGQHGVALATAAAFFGLECEIHMGEVDIAKQAPNVTRMKILGAKVVPVTHGLKTLKEAVDSAFDSYAKNYKDSIYCIGSALGPHPFPLMVRDFQAVVGYEAKDQFKEMTGFLPDVVTACVGGGSNAAGMFIPFLEEPVDIIGIEPLGRGEKLGDHAASMKYGEKGVMHGFESIMLKDKNGNPAPVYSIASGLDYPSVGPE... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 44798
Sequence Length: 405
Pathway: Amino-acid biosynthesis; L-tryptop... |
B5F4M4 | MTTLLNPYFGEFGGMYVPQILMPALNQLEEAFVSAQKDPEFQAQFADLLKNYAGRPTALTKCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRMGKSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMFADFINDTSVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSISAGLDFPSVGPQHAYLNSIG... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 42868
Sequence Length: 397
Pathway: Amino-acid biosynthesis; L-tryptop... |
Q81GG7 | MGTILDKIVEQKKKEVAELYEIYTPVKTKRKTQSLVEALQQFTVIAEVKRASPSKGDINLHVDVRKQVGTYEKCGAGAVSVLTDGQFFKGSFHDLQTAREESNIPLLCKDFIIDKIQIDRAYEAGADIILLIVAALTKEKLKELYSYVLEKGLEAIVEVHDEQELETAIVLNPHVIGINNRNLKTFEVDLSQTEKLGKRLNEEKLLWISESGIHSKEDIIRVKRAGAKGVLVGEALMTSSSISSFFEDCKVNI | Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Mass (Da): 28290
Sequence Length: 253
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
A8FEK0 | MLNQIIARKKEHIQTLQLPDDGHFERRSFKEALVNTHRSIGLIAEVKKASPSKGIIQPNFDPLQTAKAYEKSNADCLSVLTDEPFFQGKNEYLSLIKKHIARPILRKDFIIDSIQIEESRRIGADAILLIGEVLEPQQLHELYIEAKEKGLDILVEVHAAETLEQILNLFTPEIIGVNNRNLKTFNTTVEQTKEIAPLVPKDCLLVSESGIQTFDDLTFVKKHGASAVLVGESLMREPSQEKAVQTLFGE | Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Mass (Da): 28104
Sequence Length: 250
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
P03964 | MLEKIIKQKKEEVKTLVLPVEQPFEKRSFKEALASPNRFIGLIAEVKKASPSKGLIKEDFVPVQIAKDYEAAKADAISVLTDTPFFQGENSYLSDVKRAVSIPVLRKDFIDSLQVEESRRIGADAILLIGEVLDPLHLHELYLEAGEKGMDVLVEVHDASTLEQILKVFTPDILGVNNRNLKTFETSVKQTEQIASLVPKESLLVSESGIGSLEHLTFVNEHGARAVLIGESLMRQTSQRKAIHALFRE | Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Mass (Da): 27741
Sequence Length: 249
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
Q8AAD6 | MKDILSEIIANKRFEVDLQKQAISIEQLQEGINEVPASRSMKRALASSDSGIIAEFKRRSPSKGWIKQEARPEEIVPSYLAAGASALSILTDEKFFGGSLKDIRTARPLVDVPIIRKDFIIDEYQLYQAKIVGADAVLLIAAALKQEKCQELAEQAHELGLEVLLEIHSAEELPYINSKIDMIGINNRNLGTFFTDVENSFRLAGQLPQDAVLVSESGISDPEVVKRLRTAGFRGFLIGETFMKTPQPGETLQNFLKAIQ | Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Mass (Da): 28828
Sequence Length: 260
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
A6Q3P0 | MILDEIIKKTKADLEKRKKEYPLEWLGRSLAYNPFVPRPVEEVLKSTPDDPYKIIAEVKKASPSKGVIREDFDPVAIAKEYEKGGANAISVLTEPHYFQGHIEYLTQIRRYVPMPLLRKDFIIDKYQLVEALVYGADFVLLIAKALSRKELKELLEYTWHLGMEALVEIHDKADLIKAIFAGANIIGINHRNLETFEMDMSLSEKLIPLIPNGKIIVAESGIHSHEQVVELNKLGVDAFLIGEHFMRQDNIAEVVKKIKGLA | Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Mass (Da): 29800
Sequence Length: 262
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
Q8ESU2 | MTFLAKILEEKQTEVNSRKQEKIDFGSRNIPVHSFIQLINQASSLSIIAEIKRASPSKGEIQMDIDPVEQAIKYEQAGASAISVLTDQRFFKGSLNDLQQVSEAVSIPVLCKDFIIDEIQIDDAKDAGASIILLILAALPLERFQELYNYATKQGLEVICEVHTAEELKNALTISPAIIGINNRNLKSFDVDLQTTKQLAQRVDTNKTIIISESGMRTASDATLAAESGAKAILVGETFMRSNQLETDFNNLRVPLVERSI | Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Mass (Da): 28823
Sequence Length: 261
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
B1ZW79 | MPDKLIEIMAHKRREIAPLIRPVTETELAQLDASRPKPPSFADALRRPDGTLAVISEIKRRSPSAGEIKAGASAVEQARRYRAAGADALSILTDTEFFGGTLADLSDVTTEFRDQRPAPPCLRKDFMVHPVQVAQAREAGASAILIIVRALDDAEIQALYSAAQAAGLDALFEVHHETELERALHHRARIIGVNNRDLAVFKTDLALSERLIPQFPRDVIAVSESGIFTGADARRVHAVGAHAVLVGEALMKAPDPAALIAEFRAR | Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Mass (Da): 28837
Sequence Length: 266
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
A1R5S7 | MTVLDDIIVGVKEDMEVRRGLVSLAELKERAANAAPARDAWAALGGPSSIRNDLKVIAEIKRRSPSKGDLASIADPASLAVQYADGGASVISVLTEQRRFGGSLADFDAVRAAVETPLLRKDFTVDEYQIWEARAHGADLILLIVAALSDAELADFSALSHELGMNVLVETHTEEEIERAVAAQAKIIGINVRNLKTLDVDRSVFGSLAGLIPAESVIVAESGVRGPEDVSHYAAGGANAILVGEALVSDSTPRERITEFKAAGAAAIAVRN | Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Mass (Da): 28674
Sequence Length: 272
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
P03947 | MNRFLQLCVDGKTLTAGEAETLMNMMMAAEMTPSEMGGILSILAHRGETPEELAGFVKAMRAHALTVDGLPDIVDTCGTGGDGISTFNISTASAIVASAAGAKIAKHGNRSVSSKSGSADVLEELEVSIQTTPEKVKSSIETNNMGFLFAPLYHSSMKHVAGTRKELGFRTVFNLLGPLSNPLQAKRQVIGVYSVEKAGLMASALETFQPKHVMFVSSRDGLDELSITAPTDVIELKDGERREYTVSPEDFGFTNGRLEDLQVQSPKESAYLIQNIFENKSSSSALSITAFNAGAAIYTAGITASLKEGTELALETITSG... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
Q8AAD5 | MKQILYKLFEHQYLGRDEARTILQNIAQGKYNDVQVASLITVFLMRNISVEELCGFRDALLEMRVPVDLSEFAPIDIVGTGGDGKNTFNISTAACFTVAGAGIPVVKHGNYGATSVSGASNVMEQHGVKFTSDVDQMRRSMEQCNIAYLHAPLFNPALKAVAPIRKGLAVRTFFNMLGPLVNPVLPTYQLLGVYNLPLLRLYTYTYQESKTKFAVVHSLDGYDEISLTNEFKVATCGNEKIYTPEGLGFARYQDTDLDGGQTPEDAAKIFDNIMNNTATEAQKNVVVINAAFAIQVVRPEKTIEECIALAKESLESGRAL... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
Q494D8 | MQKILDTLYQGKNINQKQSEALLHSIIKEKLSAIQIASALISMKIRGETFEEIIGAVNILLTHAKPFPRPNSLFADITGTGGDNSNTINISTTSAIVAATCGAKIIKHGNRSISSLTGSMDLLKQHCLILNSPQQARKNFDELGICFLYAPQYYTVLHRIMPIRKQLKIPTLFNIVGPLINPSKPPLTLIGVYKKELLSPIIRILQLLKYNHAIVVHCGGIDEVGLHSPTHIAELHNSIINNYILTASDFGLDSYPIEILRCYSRKQAREYMINILKGRGKPAHSAVIAANVALLLKLFGYTDLRANAQLALEKIHYGIP... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
C0ZCE2 | MLTYALEQILLGKHLTRTVAEEAMGEIMDGKATPAQIGAFLASLRLKGEQVEEIIGFAKAMRARAMNFPIELPGLVDTCGTGGDGSHTFNISTASAVVAAADGVRIAKHGNRAVSSKSGSADVLEALGVPVNLSPKDAADCLRATNLCFLFAPLYHQAMKHAAGPRKELAIRTVFNLLGPLTNPAGASHQLMGVYDAKLLPNVAAVLHELDVKRALVVAGSDGLDELTVTGTSHIAELRDGRILTYEIEPEQFGLRRHEKDALRGGDANENAKIIHDVFSGARGAARDIVLLNAGAILYLADRVSSIETGVIRAAELIDG... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
A6L7M8 | MKAILSRLFNHEELTRKEAKNLLLNITRGMYNDAQIAALLTVFQMRGIKVEELIGFREALLTTRIPIDFSAYTPIDIVGTGGDGKNTFNISTCACFIVAGAGYHVAKHGNYGATSVSGASNVIEQHGVKFTNNPDKLTRSMEECGMVYMHAQLFNPAMKSVGPVRKALQVRTIFNLLGPLVNPCLPAYQLLGVADLPQMRLYTNVFQKLGIGFAVVNNLDGYDEISLTDEFKVMTNRYETIYKPSELGFSLARQEELYGGNTPEEASKIFNNVLENKATKAQTDCVLINASFAIQAMEPAKPIEECVAIARESLESGKAL... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
Q6L273 | MLNLDFIYENRNMSESEAELCMINIIDAPDTVKAAFLTALYVKGITPDELSGFSRALRKLSSISINIDKLTDIVGTGGDHKNTINVSTAASILLSLRIKIAKHGNFGITGSHGSADFMKFIGYKFEMTEYDIIKNLNEKNYVYILAPVYNKTFAKFSNVRKKLGIKTVFNILGPLTNPLNPENLVIGAYDDETAETYASVMLKQNKRAFIVSSTMDEISPEAESHVYYVNNAIRKFDLDPLSITGKRINESNIIEKDPVKSFNIIIDAFKNKNRDAASFIALNAAPALVLNGISRDITSAYDLCINDIESGAAYERLRRI... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
Q7VCJ6 | MPIVSWPELLEKLLSTKEISEIEAKALMKAWLNDELLPVQTGAFLTALRAKQISGLELSSMAEVLRDACLFPYPLPEVFMVDTCGTGGDGADTFNISTAVAFVTASCGVTIAKHGNRSASGKVGSADVLEGLGIKLNAPLELVVKAIEKNNITFLFAPAWHSSLINLAPLRKALGVRTVFNLLGPLVNPFRPKAQVLGVAKSELLDPMVEALRNLGLERAVVVHGAGGLDEASLEGPNEVRFLENGQITSKTLDVEELGLTISPNSTLKGGSLATNQDILRSLFQGRGTQSQREVVALNSSLVFWASGKELDLKKGVTIA... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
Q971Z7 | MNTAELLRKIIRRENLTEDEARSIANSVMKAEVPEIVTAGFLVGLATKGESVEEITGFAKAMRDNALHINFPSALDTAGTGGDGLNTLNVSTAVALLISQVYPVAKHGNRAVSGKSGSADVLEALGYNIIVKPELAEKLIKESKFVFLFAQLYHPAMKNVANVRKTLGVRTIFNVLGPLTNPANARYQMIGVFSKEFLPKLAEAVVRLDYDRVILYNGFPSLDEISTQGITYVYEIEKDKIVSYTVSINDFGLKDEIPVSKLTVNDATHSALRILKAFKGKDEEARRFIGINTAMALYLIRKVKDLKDGYEYALQLMDSG... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
Q3A6L6 | MIRQAIARVVEGQNLKESDMIEVMNQIMGGEATPAQIGALIVALRMKGETVEEITGAARVMRDHATPVRVGRVLDIDREEINLDQETMAAVLDTCGTGGSGTKSFNISTTVAFVVAACGVKVAKHGNRSVSSMCGSADVLEALGVHLDIGVDTVERCIAEEGIGFLFAPALHGAMRYAIGPRREIGIRTIFNILGPLTNPAGADRQVLGVYREDLVATLADVLCRLGCRRGFVVHGMDGMDEVTLTAPTRIADIREGRYSLSTIAPEDYGLQRCRLEDLAGGDARHNAELVRGILAGEAGPRRDIVLLNSAFALVAAGKA... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
A0LJ59 | MIQDGIKKIIQREDLSETEMSAVMSEIMSGEATDAQIGAFMGALATKGETFEELAGAARTMRRKAARIQVTSPVIVDTCGTGGDRKGTFNISTTAAFVVAGCGVTVAKHGNRSVSSQCGSADLLEALGMRLDAPAEVVEEAIGRIGIGFLFAPLFHGAMRHAARARKEVGVRSIFNMLGPLTNPAGANCQVLGVYAPQLTEMFAQALRLLGARRAFVVHGQDGLDEISVCAPTRVSELDGGLVRTYDLQPELLLGRKADPEDLAGGDPGVNAKITRDVLGGAIGPRRDVVVLNAAAALIAAGAAEGFPSAVRNAEESIDG... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
Q0B006 | MFDRYLKSVVEGDYLNSEEAYLTARMLLHEDIPEIKAAAFLSALRTRKESQEELTGFVQALYEEAKMVDCGMEVLDTCGTGGDGLGTFNISTASALVVASCGVAVAKHGNRAVTGKVGSADVLEALGVEVQLEPDEARQLLDKAGITFLFAPHYHPILKQVGGLRRGLGIATIFNFMGPLLNPCRPSYQVLGISDSNLQEAVAGTLQRLGRKRALVVHAFNGMDEISPEGKTRVFDVGEHGLEVFDIDPEELGIGGFSLDAIQGGDATASARLVIKVLQGEPGPYRDTVILNTAAALLTAGRAKNIQEGMQMAAEAIDAG... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
Q88WI1 | MTQIKICGLMRPADVVMVNQALPDAIGMVFAPGRRRRITMATARQLSQQLDPRIRRVGVFTTNQLSEILALVQQHIIQVVQLHATVDDPRIASLMAAHVPVIQAMTPANATQCQADYLLLDNARPGSGQVLDWNQLQSQRPVRPFILAGGLTPTNIVTAINKVYPAMVDVASGVETAGNKDREKINLMVQRAHQTGVSTPLLTEIRRN | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 22828
Sequence Length: 208
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
Q5ZVY5 | MNPSRIRIKMCGMTRSEDIQYAIDLGVDAIGLIFYPKSVRNVSLEKARIIVNNIPPFVDIVAVLVNPEQSFVQLIINEIPVQLLQFHGEESSEFCRQFNKPFIKAIHPKTAIQIQSAVDEFFDASAILLDTPSDKERGGTGLTFDWNIIPENLSKPYILAGGLNESNILEAITMCHPYAVDVCSGIEASPGVKDHLKMSRFIKAIWG | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 23046
Sequence Length: 207
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
B1XY47 | MILSPARTRIKICGLTRPGDVDVAVAAGADAIGLVFYPRSPRHVSLALASDLARRLPPFVTPVGLFVNASPEDVERACEQIPNLLLQFHGDETPAQCEASGRPYLRAARMDPGFDLLNFARSYTSAQAILLDAHVEGYGGGGKVFDWSLIPSDVPRPVVLSGGLNPANVTDGVLRVRPWAVDVSSGVESAKGIKDAVLMRQFCEAVRDADARSIDASSGY | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 23443
Sequence Length: 220
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
Q72RH2 | MITNSLQKTKVKICGIKDLEIAKICKEEGADYIGFNFVSSSPRKIELSNAQKIVEYYKSEKNSPEIVLLFYQNSFEEIESITSVLDHDLVQWVWDDPLINRKKLLYKRQICSYRVQTQIHDQDLKDIEAEFLILDSYSKGVGGGTGETFNWELISKVKRKFLLAGGLDPSNVVNAIEIVKPFGVDVASGVESSPGIKDPQKVIQFIRNVKSTS | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 24066
Sequence Length: 213
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
Q01128 | MTVSTTSLCTPIVKICGLTVEAAHCAISSGADLIGMILVPDLKRTVQQTKLKAISRAVTRIPGVPTSPSRGIDRPSHGLVRGTFSADYTSWPLVVGVFRNQSLDEVLRMLRNYDLDIVQLHGSEPLHQWTREIPVPVIKKFGLGEDDLMAPGLHAVTLLDGGAGGEGQKISWEGLPGSGAFMLAGGLTVDNVAVAVKIPNVAGVDVSSGVATDGMQDLEKNCRCLFRNAKGW | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 24625
Sequence Length: 232
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
Q8Y6Q5 | MIVKICGLKKAVDVAAAVENGADMIGFVFAKSKRQVTVDEAHELAKNIPAGVKKVGVFVNPTEEELTAAIKGVPLDIVQLHGQEPAEQANRTDAEVIKAFPVKDGKLPDNINDYPNAYILLDAPAEEYEGGSGKTFDWDKIDRDLLTKNKLIIAGGLNAQNVQEAIKRFEPYAVDISSGVETNGEKDPQKIKCFIKTAKGVE | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 21876
Sequence Length: 202
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
Q2W020 | MPVEVKICGITDEDAMDVAIEEGADYVGLVFFPPSPRNVTPDRAAELVEFAPGDVTKVGLFVDPDDATLDTVLTRVRLDLLQLHGHETPERVEAIRLEYGLPVMKVLSVSDAADLDAAEPYLAVADRLLFDAKPPKGAVLPGGNAVSFDWSILTGRKWGLPWMLAGGLTPANVAEAVRISGAAAVDVSSGVESAPGIKDSDKIRAFIKAARGGRP | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 22757
Sequence Length: 215
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
Q0ATJ7 | MTDIKFCGLKTGRDIAAAEAAGARWTGYVIFPKSPRHVSPTLAGELCHLARTSETVAVTVNPDDDLLAQIRDAMRPDWIQLHGSESPQRVVQARAYAKRGIIKALPVAEASDLDAANPYDRVADMLLFDAKPPAGADRPGGLGHGYDYALLKSLQISVPWLLSGGLDDTNVCAAVAAAGAKAVDVSSGIESAPGIKDAGRIAGFASALAAC | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 21964
Sequence Length: 211
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
P06558 | MTHVVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVETILAANPDLICLSPGPGYPADAGNMMALIERTLGQIPLLGICLGYQALIEYHGGKVEPCGPVHGTTDNMILTDAGVQSPVFAGLATDVEPDHPEIPGRKVPIGRYHSLGCVVAPDGIESLGTCSSEIGDVIMAARTTDGKAIGLQFHPESVLSPTGPVILSRCVEQLLAN | Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia ... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.