ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q47LH5 | MTTSFARNVPLADYTTLGLGGPAARFCSVASTDELIATVRDVDRSGDPLLVLGGGSNLVVADEGFAGTVIQVDSSDLSYTEVDDTVVRVRVDAGMEWDSFVARCVDEGLSGVEALSGIPGRVGATPIQNVGAYGQDISQTVVEVTVYDRAADRTRVLSAAECGFAYRTSIFKGRDRYVVCDVVFELTRSKLSRPIRYAELARSLGVSQGDQVPLADVRDAVLSLRRSKGMVLDPADPDTRSAGSFFTNPILSADEFARFTQRVAEVLGPEVTPPAYPDGDGRVKTSAAWLIERAGFPKGYGTGPVGISTKHTLALTNRGG... | Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 37700
Sequence Length: 356
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
A6LN73 | MKLIDTLLKLGNDVHINEKMKCHVSFKIGGPVRLFIIPYTVDMFLETLNVLDNVKILGNGTNVLPKDEYMDFNVISTEKLTGIFVENDTIICESGLSLKKLCLYAAKEGFSGFENAYGIPGSVGGAAYMNAGAFGWETAEMIEFVDVYDGKKVLRLDRTEMKFSYRNSIFKENEDLIILRVGFRIIKGDSYNIFSRMKQVMIKRVEKQPLEFPSAGSVFKRPRKGFYVGSAIEKIGLKGFRIGGAMISEKHAGFIINYNNAKSSDVKDMIELVKDKIYKNFGVKLETEIEIW | Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 32986
Sequence Length: 292
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
A5ILF5 | MFEKLSCHTSIKIGGRVKYLVLPNDVFSLERAINVLGDVPFQMMGLGTNLLVQDDDLDIAVVKTERLNQIEIKGEKVLVESGTPLKRLCLFLMEAELGGLEFAYGIPGSVGGAIYMNAGAYGGEIGEFVEAVEVLRDGKRTWLSKNEIFFGYRDSTFKREKSIITRVMMSFKREKKEVIKAKMDDYIKRRLEKQPLDLPSAGSVFKRPREDFYVGKAIESLGLKGYRIGGAQISEKHAGFIVNAGNATFDDVMKLIEFVRKKVKEKYGVELETEVEIWWNGRRW | Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 32164
Sequence Length: 284
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
Q5SJC8 | MRVERVLLKDYTTLGVGGPAELWTVETREELKRATEAPYRVLGNGSNLLVLDEGVPERVIRLAGEFQTYDLKGWVGAGTLLPLLVQEAARAGLSGLEGLLGIPAQVGGAVKMNAGTRFGEMADALEAVEVFHDGAFHVYCPEELGFGYRKSHLPPGGIVTRVRLKLKERPKEEILRRMAEVDRARKGQPKRKSAGCAFKNPPGQSAGRLIDERGLKGLRVGDAMISLEHGNFIVNLGQARAKDVLELVRRVQEELPLELEWEVWP | Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Sequence Mass (Da): 29180
Sequence Length: 265
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.98
|
A7GX33 | MKKVHFIGIGGIGISAIARFLFEKGHKISGSDIKESKTTQELKEQGMDVITPHCKEAIKDQDFVVYSAAIKDDNVELVEARKKGIKCFSRKEILPYVLEDKRVFAVAGAHGKSTTSAMLSSLIEGSVIIGAISKQFGSNMRYAQSDNVVFEADESDSSFLNSNPYLAVVTNAEPEHMEHYDYDLAKFYAAYKGFLERAKVRVINAEDEFLSTLKLDAIRLFPSSDITELAMVVRDYQPYTSFNLKNLGKFEVFGMGQHIAIDASLAILAALHETPLKDIRENLLNFKGIKKRFDILSADKNFILIDDYAHHPTEIRATLN... | Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
Sequence Mass (Da): 48425
Sequence Length: 435
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.8
|
Q9PNN7 | MMQNIHFIGIGGIGISALARFLREKGFKISGSDLKESKITKELEKEGVKVSIPHHKDNILNKDLVIYSAAIKEENPEFKYAKELGIKCLSRKEALPLILEDKRVFAVAGAHGKSTTSSILASLLDDASVIIGAILKEFGSNMIYKESQNLVFEADESDSSFLNSNPYLAIVTNAEAEHLDHYGNEVSKLHHAYTQFLDVAKIRVINAEDEFLKNYKNESIKLYPSKDIKNCTMCIENFKPFTSFELKDLGEFKVFGMGYHLALDASLAILAALNFLDIETIRTRLKNYQGIKKRFDILHADENLVLIDDYGHHPTEIKAT... | Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
Sequence Mass (Da): 48372
Sequence Length: 432
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.8
|
Q3AAE7 | MAYYSTVLKRKVRKMLAVHFIAIGGIGMSGLARILQSKGYRVSGSDLKETELTKKLRAEGITVFIGHREENLASDVSLVVVSTAVSQDNPELLKAKRLGIPVMHRGELLARLMQEKKGIAVAGTHGKTTTSSMIAYVLEKEGFDPVIAVGGEIVDLGYNAKAGQGEYMVAEADESDGSFLKLLPYAAVITNIEADHLDYYQSFEEIKKAFKKFADNIRPEGFGVFCWDNLQVREMLKGYKKRKFTYGFSPGSDFMLRDYREEQNQLVANIYYKNTLEGELRLKVPGKHNILNAAAATAVLRNIGLSFKAISERLLEFNGA... | Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
Sequence Mass (Da): 51804
Sequence Length: 464
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.8
|
Q11GS6 | MKMPQTIGVVHFVGIGGIGMSGIAEVLHTLGYHVQGSDQAENANVVRLREKGIKAFIGHAAENLGDAEVVVISSAIKRDNPEYVAARERHLPIVRRAEMLAELMRFRQAVAIGGTHGKTTTTSMVAALLDAGGLDPTVINGGIINVYGTNARMGEGDWMVVEADESDGTFLKLPADIAVITNIDPEHLDHYGSFDKVREAFRQFVENVPFYGLGVMCIDHPEVQALVSRIEDRRVVTYGENLQADVRFENHRMENGHSVFDVIIRARKSDAVKAMRDLRLPMPGRHNVSNATAAIAVANELGMGEEAIRKGLAAFGGVKR... | Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
Sequence Mass (Da): 50425
Sequence Length: 465
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.8
|
A9WG70 | MSHYHIIGIAGAGMSAIAHLLLDQGHTVSGSDLTANHATAALQARGVQVWRGHDPAYVQGADVVLATAAIRGTHPELEAAAAAGIPRLSRADLWRLWSEQRPVIAIAGTHGKTTTTALTALALRGAGIRCGFLIGADVPALGGSAQWGDPEAPLVIEADEYDRVFLALTPALAIITNVEWDHPDVYPTPSEYTAAFAAFSRQVRDPRRLLVCADDPGALALAGQSEARLYGIDEHIATDPVSCRLAPLDWTASGVTGTATGQQFDLWYYDRRSFGRRLAATVTLAIPGEHNVRNATAALAAAALWGADLRTAVTALAEYR... | Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
Sequence Mass (Da): 50498
Sequence Length: 474
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.8
|
Q9CE10 | MEKTYHFTGIKGSGMSALALMLHQMGKKVQGSDSTDYFFTQRGLEQADVPLLPFDEKNIKPEFELIAGNAFRDDNNVEIAFAHKNGFPFKRYHEFLGHFMEDFTSIGVAGAHGKTSTTGMLAHVMSNIVDTSYLIGDGTGRGIEGSEYFVFESDEYERHFMPYHPEYTIMTNIDFDHPDYFEGIEDVTSAFQDYANNIKKGIFAYGEDVNLRKLTAKAPIYYYGFEANDDYRAENLVRSTRGSSFDAYFRGEKIGHFVVPAYGKHNVLNALSVVAVCHNLGLDMTEVADHLLTFRGVKRRFTEKKVGETVIIDDFAHHPT... | Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
Sequence Mass (Da): 50050
Sequence Length: 443
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.8
|
A9KQI8 | MYHIDFTKPIHVHFIGIGGISMSGLAELLHTKGFTVSGSDAKDSKIVDRLRHLGITIFIGQKAENITEDIDLVVYTAAVKSDNVEYQAVQKHNIPMLDRADFLGQVMLQYKNAIGVSGTHGKTTTTSMVSLMMLEGNFDPTISVGGILDNIEGNIRIGHSENFIVESCEYKNSFLSFNPAHAIILNIEAEHLDFFKDIEDIRTSFHTFAKKLPDYGNLVVWGGIDRYEELIEDLSCNVITYGMFSSEEEREQNKDRYDYAACNVTSDDFGLRSYDLYKHGKFVDRINLAVIGDHNVLNSLAAISLVDTLGGTMSAIKKAL... | Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
Sequence Mass (Da): 52275
Sequence Length: 469
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.8
|
Q5ZSA5 | MNNSEQFLSPRMGRVEQIHFVGIGGAGMCGIAEVLHNQGYRITGSDLGESGTVQRLRSLGIQVYIGHRLENIKGADVVVRSSAVDFNNPEIVAARELMIPVIPRAAMLAELMRFRHGIAIAGTHGKTTTTSLVSSLLAEGGLDPSFVIGGKLNSCGANAQLGKSAYFVVEADESDASFLFLKPMMAVVTNIDADHMDTYEGDFEKLRTTFLEFLHHLPFYGLAVVCLEDEEICRILPAIQRPTLTYGFKEEAHYRAINWTQKGMLSEFVVVRPAPHKQLTIQFQYPGRHNVLNALASIAIATELGVDDDSIVRGLQKFQG... | Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
Sequence Mass (Da): 51965
Sequence Length: 469
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.8
|
Q1AVX4 | MKVHMIGVGGAGMSGIAEVLARRGHEVTGSDLKESPYTRRLAAAGVKVYIGHEARQVGDAEVVVISTAIPKTNPELLEARRRSIPVIPRAEALARILAEGRGIAVAGTHGKTTTTSMIAHSLRALGENPTALVGGELNDIGSNVIFGREDLIVAEADESDRSILRLHPQAAVITNIEYDHPDFYASLEEVVETFARFVAGLPPEGHLVLCADDPRCRRLAELAPCPVTTYGLSGGELRARVLSPGSYLLFEGARKRGEVSLGVYGRHNVLNSLAAAGIARWLGHDPLEAARTLGSFGGVRRRFQLKGERSGVRVVDDYAH... | Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
Sequence Mass (Da): 48093
Sequence Length: 447
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.8
|
A4X981 | MRLSDLRGRKVAVWGTGREGRAAVVAIAAHGPADLVAVDDGGSTVSPPWDGFLATAAPLVTGDAGAQRLAAADVVVRSPGVPNTHPWLAELWRRQVPVTQGTALWMADHAARTVGVTGSKGKSTTSSLISHLLAAVDQPNVFGGNIGVPTLDLPAADLYVLELSSYQCSDLTDSPRVAVVTALFPEHLDAHGGEREYYRDKLNLLAHGPETVVVNGADPRLAAELGDRPVVRAGTPDTTHVAGGPDGTPWFHLGDQPLFPRAVLPLVGRHNEGNLCVALAVLDVLGVDVLARRDTLAVAVAGFQGLAHRLTEIVDPSGLT... | Function: Cell wall formation. Catalyzes the addition of L-glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine.
Catalytic Activity: ATP + L-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate
Sequence Mass (Da): 46954
Sequenc... |
Q2P5V2 | MRISQFEGKAVALWGWGREGRGAYRALRAQLPTQSLTMFCNAEEVRELESLADAALHVETDASAQALGRFEIVVKSPGISPYRAEALAAAAQGTQFIGGTALWFAEHAQPDGSVPGAICVTGTKGKSTTTALLAHLLRVAGHRTALVGNIGQPLLEVLAPQPPPAYWAIELSSYQTGDVGRSGARPELAVVLNLFPEHLDWHGDEARYVRDKLSLVTEGRPRIVLLNAADPLLASLQLPDSEVLWFNHPEGWHLRGDVVYRGEQAIFDSADVPLPGVHNRRNLCAVLAALEALGLDAEALAPAALSFRPLPNRLQVLGSV... | Function: Cell wall formation. Catalyzes the addition of L-glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine. Has weak activity with D-glutamate.
Catalytic Activity: ATP + L-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutama... |
Q6FFC2 | MLIQRGGLKVVAGLGISGVSAVNFLHEQGYRVAVTDSRETPPGHDQIPQDVQTSFGQLDTELLLQAEEIILSPGLAPQLPEIQQAIAQGIPVIGDIQVLRRATQVPIVAITGSNAKSTVTTLFGQMAKDAGKRVAVGGNLGRPGLDLLKDEPELLVLELSSFQLETTSHLNAEVAVILNMSEDHLDRHGDMLGYHQAKHRIFQGVKKVVYNRDDSLTRPLVPDSTPMQSFGLNAPDIKQYGVLREDDGTMWLARGRTRLIKSSELYIQGTHNIANALACLALGEAIGLPVESMLETLKQFKGLEHRCEYVKTVNDVRYYN... | Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
Sequence Mass (Da): 48460
Seq... |
Q7NEZ5 | MAAVAVVGAGKSGQAAARWLALGGRRVVLWDGRDSEALRVVAGALAPFGVEAVLGREFVPEEPDLSLVVVSPGVRWDHPGLVAARARGVTVTGEVGLAWESLSHRRWLCVTGTNGKTTTTALVGHILKTAGLRAPVCGNIGRPVTDLLLEPEDYDWIVAELSSFQIESAQGIRPEVAVWTTFTPDHLNRHGTLERYAAIKAGLLMQARRAVLNGDDAYLGARRSAWPDAWWTSTQAPAAVSLAGKDICIENRPVLPVSAVRLPGAHNLQNVLMAVAACHLTGVGDAAIASGVASFIGVPHRLEAVGEYRGVRFINDSKAT... | Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
Sequence Mass (Da): 46888
Seq... |
Q5FUJ7 | MSGFPSDLLAGERYAVCGLGRNGTAVVQALLGMGAEVQAWDDRNADLPAQPNLTVAPLTDLSGMTALILSPGIPHLLPKAHPVADLARAQGIQILSDAEILYRAVRKSGSKAAFIAVTGTNGKSTTTALIAHLFTTAGRPCAAGGNLGTASLALPLLPDDGVYVIEMSSYMLERLDRFHANAACLLNLTPDHLDRHGDMAGYAAAKAHVFDNMGPDDLAVIGMDDDWCRAIASQVASRGVQVVELDADALPPYDGPALPGRHNAQNVGAALTIASHLGLDEAAIRTGLKSFPGLEHRLQKVAECDGVSFINDSKATNAEA... | Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
Sequence Mass (Da): 46959
Seq... |
Q2S9Z0 | MSILARDRNIAVIGLGKTGLSCADYLTRRGYGFCVMDTRENPSGLAELNAINPDVPVVTGKLDQDMLARAAEIWLSPGVPLSHPDLQAVKGQVKICGDVDVFSREANAPILAITGSNGKSTVTTLVGEMAKACGVNVAVGGNLGTPVLDLLADEVELYVVELSSFQLETTDRLGALAATVLNLSEDHMDRYADMMAYHLAKLRVFYGCRRQVLNRDDALAQPPLSREAEITWFTLKTPEPGQYGVLEEKDGAWLAYGAEKLLPVEQMRIRGKHNWSNALAALALADAAGLEREPCLQALREFTGLTHRCEWVADKDGVAY... | Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
Sequence Mass (Da): 47719
Seq... |
O25236 | MKISLLGHGKTTLALGRFFKKNHNEVKFFDDKFLSSFKDSEGFLCYPSKDFNPNDSQLEIVSPGISFTHPLVIKAKHLVSEYDYINSLFDLVFTPTIISISGTNGKTTTTEMLTMLLEDFKAVSGGNIGTPLIELFEKRSPLWVLETSSFSLHYTNKAYPLIYLLINIEADHLTWHCNFENYLNAKLKVLTLMPKTSLAILPLKFKEHPIIQNSQAQKIFFDKSEEVLERLKIPSNALFFKGAFLLDAALALLVYEQFLKIKNLKWQDYRENALKRLNAFKIGSHKMEEFRDKQGRLWVDDSKATNIDATLQALKTFKNQ... | Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
Sequence Mass (Da): 47998
Seq... |
Q31I61 | MYLVAGLGLTGQSVLNYFASQGEPCYALDTRPEFDTSELEKAYPDVAFATGTLPTQWCGKIDSIVLSPGIAKSEPWVKHCINQGTEVIGDIELFARAAGKPIVAITGSNGKSTVTTLVAEALKEAGYAVGVGGNIGCPALDLLTHPTEFDVYVLELSSFQLETTYSLQTIAATVLNISEDHMDRYLALEDYIQAKMTILNNTELAVLPLDFERVGIARPGDEVRFGLNYAEALPPKEYGIVMKNGQAWLGWEDHASVPVTAMAQQGLHHQLNALAMMALCRPFDLSDAVFEKVLKTFKGLPHRTQVVLEQEGVRWINDSK... | Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
Sequence Mass (Da): 48509
Seq... |
Q5R0M3 | MTKIAWQNTKHIVVLGLGKTGVSVLRYLQHKRQQDQKLAEVKIQVFDSRENPPGLEEAKQILGDAELINRHWELEDTLAADLIIASPGIDLREDPVVLARDADIPIVGDVELFAQESKLPIVAVTGSNGKSTVTRMVEFVAKQCGKNVAAAGNIGVPVLDLLLQEQHPDAVILELSSFQLESVSSLKLKAAALMNISADHMDRYCTLDEYVKAKQRIFTHAKTWILNRQQQDTWPHPVTGKLMTFGNDSHPKHFGLLSGNIDRVSGPVAVTFDGSVVLRADQLQLQGIHNLVNVQAALALCQAIDIDIEAAVRAVKEFKG... | Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
Sequence Mass (Da): 50481
Seq... |
Q1IKG8 | MDVRGKRVLVVGLGKSGIASATFLQAQGAKVTVSDSKSEAQLRQEIPLLLDKGITVETGHHGERTFRDQDLIVISPGVPFDQPQLEQARKQGIPVIGEIELAAQFVPGHVIAITGSNGKTTTTSLCGDILQSGGKKTLVGGNIGTPAISFAQLANDDTWSVLEISSFQLETIERFRPEIAAILNITPDHLDRHGTFEKYAAAKERIFENQREHDFAILNADNEPCVEIAKRVKSQVLWFSRQHEVKHGTFVREDKIYFRDPKGEREIMPVADMLLKGAHNVENVLAAVCVGVAASVAPEQIRKAVSQFKAVEHRLEYTAT... | Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
Sequence Mass (Da): 49582
Seq... |
Q8CSX6 | MLNYTELENKNVLVVGLAKSGYEAAKLLLKLGANVKVNDGKDLSQDAHAKDLESMGIEVISGSHPFSLLDDDPIIVKNPGIPYTVSIIKEATNRGLKILTEVELSYLISEAPIIAVTGTNGKTTVTSLIGDMFQKSVLTGRLSGNIGYVASKVAQEVKSDEYLITELSSFQLLGIEEYKPHIAIITNIYSAHLDYHETLENYQNAKKQIYKNQTKDDYLICNYHQRHLIESENLEAKTFYFSTQQEVDGIYIKDGFIVFNGIRIINTKDLVLPGEHNLENILAAVLASIIAGVPVKAIVDSLVTFSGIDHRLQYIGTNRT... | Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
Sequence Mass (Da): 50149
Seq... |
Q82AD8 | MTNWQGKNVTVAGLGVSGIPAARVLHGLGAVVTVVNDGDDERSRAQAADLEALGITVRLGDGATLPEGTELIVTTPGWQPDKPLFAAAAEAGVPVWGDVELAWRLRGPGSAPWLAVTGTNGKTTTVQMLASILTAAGLRTAAVGNIGVSLLDAVLGEETYDVLAVELSSYQLHWAPSLRAHSATVLNIAPDHLDWHGSMEAYTADKGRIYEGNRVACVYNVADKATEDLVRAADVEEGCRAVGFTLGTPGPSQLGVVEGILVDRAFVEDRQKNAQELAEVADVHPPAPHNIANALAAAALARAFGVPASAVRDGLRAFRP... | Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
Sequence Mass (Da): 48547
Seq... |
Q9S2W9 | MPSEFSGKHVTVAGLGVSGVPAAKVLHGLGAQVTVVNDGDDERARTQAAELEPLGVTVRLGDGDTLPEGTELIVTAPGWKPTKPLFTAAGQAGVPVWGDVELAWRLRGLNGRKPAPWLAVTGTNGKTTTVQMLASILKAAGLRTAAVGNIGVSLLDAVTGEQEYDVLAVELSSYQLHWAPSLRAHSAAVLNLAPDHLDWHGSMEAYAADKGRIYEGNHVACVYNVADKATEDLVRAADVEEGCRAIGFTLGTPGPSQLGVVEGLLVDRAFVEDRQKNAQELAEVSDVNPPAPHNIANALAAAGLARAFGVSAAAVRDGLR... | Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
Sequence Mass (Da): 49143
Seq... |
Q4L525 | MNANELFEKIRVKQVIGTLDINVTDITTDSRTASEGSIFVASKGYTVDSHKFCQNVVDQGAKVIVVNHQQDINGDVTQVIVPDTLRVASLLAHTLYDFPSHQLTTIGVTGTNGKTSIATMIHLIYRGLGKGSAYLGTNGFQINEHKTRGANTTPETVSLTKKIKQAVDENAEAMTMEVSSHGLSLGRLRGVEFDVAIFSNLTQDHLDFHGTMEAYGHAKSLLFSQLGEDLSKEKYAVLNNDDDFSKYLASVTPYEIFTYGIDHDAQFMAKNIQESLQGVHFDFDTPIGTYSVKTPYVGKFNISNIMAAMIAVWSKGTSME... | Function: Catalyzes the addition of L-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Catalytic Activity:... |
Q9S2W7 | MTYPGPPRPVRISATPLAELADQLGVAAPDGSAEITGITHDSRAVRPGDLYAALPGARLHGADFVTQAAGLGAAAVLTDPAGAERAAAAGLPALVVDDPRARMGELAATIYGHPGRDLLQIGITGTSGKTTTAYLVEGGLRTAKSTGLIGTVEMRIGDERIKSERTTPEATDLQALFAVMRERGTEAVAMEVSSHALVLGRVDACVFDIAVFTNLSPEHMEFHSGMEDYFQAKAQLFTPKRSRLGVVNVDDEYGRRLAKEATVPVVTYSAEGHPDADWRADEVEVGPLDSTFTVLGPKGERIAAKSPLAGPFNVANTLAA... | Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Cat... |
Q9A196 | MITIEQLLDILKKDHNFREVLDADGYHYHYQGFSFERLSYDSRQVDGKTLFFAKGATFKADYLKEAITNGLQLYISEVDYELGIPVVLVTDIKKAMSLIAMAFYGNPQEKLKLLAFTGTKGKTTAAYFAYHMLKESYKPAMFSTMNTTLDGKTFFKSQLTTPESLDLFAMMAECVTNGMTHLIMEVSSQAYLVDRVYGLTFDVGVFLNISPDHIGPIEHPTFEDYFYHKRLLMENSRAVVINSGMDHFSFLADQVADQEHVFYGPLSDNQITTSQAFSFEAKGQLAGHYDIQLIGHFNQENAMAAGLACLRLGASLADIQ... | Function: Catalyzes the addition of L-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Catalytic Activity:... |
Q3J4M2 | MGRPLLLIAAGGTGGHMFPAQALAEAMVRRGWRVKLSTDARGARYAGGFPHVVEIEEVSSATFARGGPLAKALVPLRIAGGVASAVAGFLRDRPSVVVGFGGYPSIPALSAAVALRLPRMIHEQNGVLGRVNRLFAPRVQAVCCGTWPTDLPEGVEGYYTGNPVRAAVLERAAAPYIVPGDYPMSLVVIGGSQGARVLSDVVPEAIARLPEEILANLRIAHQAREEDVARVTEAYDRAGLLAEVKTFFTDIPRRLSEAQLVISRSGASSVADISIIGRPAILVPFAAATADHQTANARGLVEAEAAILIPESALDPGALS... | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muram... |
Q9Z702 | MMKKIRKVALAVGGSGGHIVPALSVKEAFSREGIDVLLLGKGLKNHPSLQQGISYREIPSGLPTVLNPIKIMSRTLSLCSGYLKARKELKIFDPDLVIGFGSYHSLPVLLAGLSHKIPLFLHEQNLVPGKVNQLFSRYARGIGVNFSPVTKHFRCPAEEVFLPKRSFSLGSPMMKRCTNHTPTICVVGGSQGAQILNTCVPQALVKLVNKYPNMYVHHIVGPKSDVMKVQHVYNRGEVLCCVKPFEEQLLDVLLAADLVISRAGATILEEILWAKVPGILIPYPGAYGHQEVNAKFFVDVLEGGTMILEKELTEKLLVEK... | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muram... |
B3QWT7 | MKLIFAGGGTGGHVFPAIAIAQEILRTQQNAEIQFVGTERGIEATAVPKQGFPMHLIPVAGVKRGFSPKELFENLKVPMRLQRSLSACHDILQREKPNVVIGTGGFVSGPIVWEAQSKKIPTLIQEQNSMPGVTTRLLSLRASEVHLSFEESKTYIRRTNGVFVTGNPTRQFQSHRPAQAKAFFSLDSTRKTLLVFGGSLGARSINQAIESNLEEWLEKFNLIWQTGKLDFADIATRIGSRKNLWYNAFIDQMDMAYAAADLAVCRAGASTLAEITHLGKPSVLVPYPYAAANHQFYNAKSLADNHAALLIENKDIGLET... | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muram... |
Q8KGD4 | MKVLFAGGGTGGHLYPGVAMAAELKKRVPGISISFAGTSAGIEATEVPRLGYRLVLFPVRGLKRGLSIRALVENALILGDFAKSLSMAMALVRKEQPDVVVGTGGYVSAPLLLAAQLSGKKTLIQEQNAFPGVTTRLLARMATEVHLSFEESRKFFGGKSEVFVTGNPAREFPAESRESCLDFFGLDRSLPTLLVFGGSRGARAINNAVLKLCHRLEGTVNLIWQTGALDADRMRGEIGTSATRWIGPYIQEMGKAYGAADLVLCRAGASSLAELTNLGKPSVLIPYPYAAADHQRHNAMALVSAGASVMIDDSKIGEEA... | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muram... |
A1R5F8 | MTFDSANASKPLSVVLAGGGTAGHVSPLLAIADAIREKRPEAAILAVGTPSGMETRLVPAAGYELATIDRVPFPRRPSADLVKLPARLSGAVRQARRILEEARADVLVGVGGYVCTPMYLAARKLRIPIVIHEANMKAGLANRVGARFSNHVAVAFAGTRLRGARHVGMPMRRAISGLDRAVAAPAARAALGLDAQRPALIVTGGSSGALSINRAITAALPALAAAGVQTLHITGNGKAVKDDDGGLLTADGYRQVEYVDGMENVYAAADVLLARAGAGTVSEVAAVGVPAVFVPLPIGNGEQALNAAPLVAAGGAVMVD... | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muram... |
A6LEU3 | MRKYRIIISGGGTGGHIFPAISIANTFKKRFPDAEILFVGAEDRMEMDKVPAAGYKIVGLPVSGFDRAHLMNNVKVMVRLAKSLRLARKTIREFKPDIAVGVGGYASGPTLWMAASQGVPALIQEQNSYAGVTNKLLAKKASKICVAYEGMEKFFPADKIVITGNPVRQDLEEALSKKEEALAFFGLSPEKKTILVVGGSLGARTINRSIQGDLDKFFASDVQVIWQTGRYYYSDASKHLKAYRGMPVWCSDFITRMDYAYSAADLVISRAGASSISELCLLGKPVVLVPSPNVAEDHQTKNALALVHKDAAVMIADKDA... | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muram... |
Q6MBS7 | MSKRFMITAGGTGGHIFPAQGLAQELIKKTYSSSILFVAGGLSTNKYFDRSIFPFQEVSASPLFSKNPFKLLKGVFNLLRGVWQSIRIIRKFKPDVVVGFGSYYTVPPLLAAKILRIPIVLHEANSIPGKANKWLASMAWRVGIHFPFTATLLKGNTIEVGMPLREGYQLDQIDKIEALSYFGLSKNNSTLLVFGGSQGALAINRLMRNLANTWKNTPIQIIHITGSIQEADELKIFYANYQVKASVKAFEKNMHLAWRAAEVFISRSGASTIAEAMEFEVPGILIPYPHATDHHQDKNADFFVDIVKGGIKIVEEKAKP... | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muram... |
A1AU61 | MKLIIAGGGTGGHLFPGIAVAEEFLSRDPANQVLFVGTERGIEARAVPAAGFPLELISAAGIRGKGGLGKLRGAAMMFNGYRQSCRLLDRFRPDAVLGVGGYASLPMLLAARTRQVPSFIHEQNAVPGMTNRLLSRFADRIFITLEESSRFFAGRRTLLTGNPLRRQILDRLGTRDQGPGIRDQEKHMTDSTGPASRVPGPRFNLLVFGGSQGAHAINMAMVAALPLLKRASVRLGITHQTGESDRERVAAAYRSAGVEARVLPFIADMASEYARADLVVCRAGATTIAEVTALAKACLFIPFPYAVDDHQRRNAEALLR... | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muram... |
Q4FPK5 | MNKKILISTGGSGGHVIPATIIYKHLEDNFDVSMTSDFRGVKFLNKDEYNLKIFNVRPISKNLLIIPLDFIFMIFLIFKSISFFRKNKIDTLISTGGYMSLPLCLGARILNIKLLLFEPNMVLGRSNKFFLSYCQKIFCYSNNIKKFPIKFKNKIKVIPALLRKNFYNKRDYNKSLDTINLLIIGGSQGAKIFDDLVKNAIIELAKNYKLKIYQQTNSINFESFKKIYEDKNIQCELFNFNDDVVNFMQKTDLCITRAGASTLAELNFTETPYLAIPLPTAKDNHQFENAHFYNKLGFNWLLNQKEIDEKTLLNKLINII... | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muram... |
B4RFS0 | MRKTAVVAAGGTGGHLFPAQALAEALIARGWRIVLASDERVAGLAQDFPAERRIGLSAATYRPGDPVGMMRAGFAVLRGAMHARAAFREIGPDVVVGFGGYPSAPALVAAILDRRPTVIHEQNAVMGRTNRILAPHVRTVACAFPTLKKAPPKVAGRAVVVGNPVRPPIRALADVPYVPPEPNGPVRLLVTGGSQGARLLSELVPEAVKALPEDLRRRLTVHQQTRPESMNTARRAYRDALVDAEIAPFFRDIAGRLREAHLVVGRAGAGTVCEFAIAGKPSILVPLAIALDDDQGQNARLLADAGGAEVARENQLTVDT... | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muram... |
Q30PK0 | MRLCITGGGTGGHLMIAEALVEACANDGHEAIFIGSTSGQDRKYFEQNSKFSHVYFLQTTGVVNQRGLGKLKALWLVLRAFFASRAILKKHNIQATYSVGGFSAAAASFASLSRLIPLFIHEQNAVYGKLNSILKPFATRFISAYDEASPIKGYPVKDIFFKNARLRDEIKCVIFLGGSQGAKAINDLALSVALELEARGVKIIHQAGERDYERVKSAYEELGVKAELCGFTKEMPSLMARADLAVSRSGASTLWELCANALPSFFIPFPHAASDHQYHNAKFIVDNELGWCQREEEDLRATLLSILPQNLADKSKALME... | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muram... |
B2V7Y8 | MKKVFISGGGTGGHFYPALSVAENLKEKGFSITYIGTTNGIENKKDFPADEKILYPMRAVRGKSIVGKIQGVFSLLSTTFKVYKQIKKEKPDFSICFGGYTSIPLGLASFLARVPLYIHEQNSIPSYSNKILSYFAKKVFITFELTAKYFDRKKTVLTGMPLRKNIIERAKNYVYKPNQTKTVLVVGGSQGAKKLSESIISLASEMKDIKFILIKGKWQVEVPNLENLTVYEYVDNMEDLYTSADVVISRSGSSSVNEILCFGKYAIFVPFPYAASNHQYYNVKWLKDLGLCELIEEKDLSKEVLKKALEDAFNKDLESL... | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muram... |
Q67Q48 | MRYLITGGGTGGHIYPALSIARALTEQDPEAELLYVGTRTGREAAIVPQAGIAFAVISSGGVVNLGLLQRVRGGLRAARGLLEALGHIRRFRPDIVIGTGGFVAGPVLAAARLARVPLVIQEQNAFPGVTNRLAARWATAVFVPYEEARAHFPPGVRLIRAGNPVRPEIASASREAGRQALGLSERDRVLVIMGGSGGARDFNRVAAEAVLQLDVPGLRVVHITGERYFGQVKAQYGDRAPHVTLLPYAHNMPEVYAAADAGLFRAGALTLAEIQVRRLPSVLIPSPNVTHNHQEWNARTLERRGAAIVLREGGLTPADL... | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muram... |
Q2LR48 | MTVRVIIAGGGTGGHLFPGVAIAEELLRRDRENRVLFVGTKRGIEKKVLKDLGFRLKLLNVEGIKGRGVMRSSLALLKLPGSLMQSMKIIRDFRPDVVIGVGGYASGPAVMAAHLMGIKTAIAEQNSIPGLTNRILGRFVDRVFLSFSDGGKWFSAKKAAVSGNPIRAAFFNGKPVLEKTGDQFSLLVFGGSQGAHAINSAFQDALPFLQLLKGCLRIVHQTGERDCESMAAAYSAQGFSARVVPFIRDMAAAYEAADLLICRAGATSIAEITAIGKAAILIPFPYAIGDHQTENAKVLLKAGAAVMIPEKDLTGKKLAD... | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muram... |
Q3A2G6 | MKLLLAGGGTGGHLFPAVALAQRLLEQDSEAQVQFVGTARGIEARVLPEQGWPLELIDIRGFVNQGLLGKLRMIPCLIRSVWQGLCILRKFQPDVVLGVGGYASAPMLVAARLKRIPTVIHEQNAWPGLTNRLLGPWARCVCLSFSEAERAFHRAATIVTGNPLRKGMEGCPPMDGDAPELLVFGGSRGARAINDAMLEALPRLEPWKDRLRIVHQTGGDDLQRIREGYARAGWPQESVVPFIDDMAAAYARAHLVVCRAGATTLAELAACGRAAILIPYPHAAADHQTVNARAMAKKGAGLVLAQQNLTPETLASLITD... | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muram... |
Q2JW21 | MNGDRRDPTSPPRLLVAASGTGGHIFPALAVVEQLPTWQIEWLGVPQRLEAKLVPDRYPLHRVAMSGWQGSPWQKLGSLVQLARATLQVRQILASGQFDVVLTTGGYIAAPTILAARSLGVPVLLHESNCLPGKVTRWLGRFCRLVALGMAETAEHLPGAVTRVVGTPVRAEFYQPQPLPADLPIPEGDPLIVVMGGSQGARGLNRLVAACAPAWLEAGAWIVHLTGGSEVGIPSHPRYRAFPFRADVAALLQRATFAISRAGALSLAELWATATPAILIPYPFAAEDHQYHNALAFVGRGGGVVMRESEANLDLLRQTA... | Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muram... |
Q1INP0 | MSRQRPVIGVFDSGFGGLTVLREIVRLVPNAEYLYFGDTARLPYGTKSADTVARYALGACHFLEGQGAEHLVIACNTATALAMDAIEAKANVPAIGVVEPGASAAAAISKTRSVAVIGTEATISSHAYHHALERLGINAYEKATPLLVPLVEEGWTDHPVTKQVAEIYLQDAFVRREQRSDVLVLGCTHYPLIRPLLRKVVPSDVAIVDSAESTAKALAKKLGIAPPSASAAGATQAAGARAQMAPSAPEPKEGTPDFRFFVTDSVQKFRRLGSGFLGHPVDNVEHVDLGG | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 30790
Sequence Length: 291
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
|
Q5FLV8 | MDNRPIGLLDSGFGGLSVAKKVIEKLPNESTIFIGDNAHIPYGDRTREDIINLTRRSVKFLLEKNVKLIVIACNTATAVAMPTMQKEVEQQIIGVIQSGALAAARTTKNKNVAVVATNVTVASHAYQKEIKFRDPEIKVTELAAPKLAPLVEAQKDYATNLKVVKESLAPLMGKEFDTLVLGCTHYPLIQKEFEEAINNKEVTILDPADQVAQYTFNVMRRDGLFSDSEKAVHEYYTTGNSETFDKLARTFMDDDTLTSKHVDTENY | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 29669
Sequence Length: 267
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
|
C4Z114 | MKIGIFDSGIGGLSVLHQAMITMPEADYIFYADVDNVPYGEKTREEVRKLVDHAVGFLVDKGCQAIVLACNTATSAAISYLREKYKLPIIGIEPAVKPAVEHTSETGRRVMVVSTPVTAKGEKLKRLIDKYDDKHVVDVVALPKLVRFAQDDDFDSSDVTDYLKCEFAPYNLNDYSELVLGCTHFNYFKDSFAKLFPDDLEMVDGNTGVSNNLKNTVMKKGIFTEKDKGKKGSVEYYYSDRKMESEAEMKHIKKLHERLERMRQI | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 29984
Sequence Length: 265
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
|
Q88V19 | MANEHAIGFMDSGVGGLTVVKQALKQLPRETVYFIGDQARLPYGPRPAEQVRTFSFQMADFLMAKQIKMLVIACNTATAAALPALRQQLSIPVIGVIAPGSRAALKASHRNRIGVIATEGTIRSNAYRDAILTKDPTATVVSQACPKFVPLVESNEYQSTVAKRVVAETLKQLKKQDVDTLVLGCTHYPLLRPLIQNVMGPGVTLIDSGAETVNDVSAVLDYLDIANDRSTKRYPDEYYTTGAADQFEAIARNWLGQPDFHAQHIDLGSEAND | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 29713
Sequence Length: 273
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
|
Q38YM1 | MKKQPIGFMDSGVGGLTLVKEARKRLPNEDMVFIGDQARLPYGEKPAATVREFAWQMANFLRHQEIKALVIACNTATAAALPDLQAQLAIPVIGVIKPGSIAALQTTHNRRVGVIATTGTIQSAAYSQQMAALNPDVQVTGLAAPQFVTMIEANQRHGQAVQTIVNQILQPLQKSEIDTLVLGCTHFPLLTTAIQTAVGPDVTLVNPAVQAITMLEEVLTQQQQLATTTPGTLRMYTTGSVAAFEEIAQQWLAQPDLTAQQVDIQKEKNDGPDR | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 29555
Sequence Length: 274
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
|
Q6AEK8 | MTDAPIGIFDSGVGGLTVARAIRDQLPNESILYVGDTTHSPYGPKPIADVRRYSLEVLDLLVEQGVKLLVIACNTASSAVLRDARERYAVPVVEVIQPAVRRAVAATRTGRVGVIGTVGTIASRAYEDAFAAAPDLRLFPRACPRFVEFVETGVTSGDEVLRVAAEYLQPLRDADVDTLVLGCTHYPFLEGAISYVMGEGVSLVSSDIETAKDVYRILVSGGFERHDSAPPTVRYEATGLDAEHFLRLAHRFIGPEVSQVDLVQTGVIDLSL | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 29312
Sequence Length: 272
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
|
Q8F1S7 | MKEPLKIGLMDSGMGGLSVLKELLKYDSELEIVYYGDLKNSPYGEKDASEVLELVRSVCNFLQKENVSAILLACNTATSAAAQTLRKEFSIPIFGMEPAIKPAILQNPGKKVALLATPVTQREEKLQRLKSELKAEELVLSISCPGLAGLVDQGDFDKAEKYLRPILANLQEQDVENLVLGCTHYVFLKQIILKNFPNVKIYDGNSGTIKHLLNSLQVPRVILNGSQNNRSIYKLILNSEKEFHFRLASELLSLKE | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 28504
Sequence Length: 256
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
|
Q03R52 | MQNDPIGLMDSGVGGLTVLKEVQRLLPTENTVFLGDQARLPYGPRSVAEVTMFTKQIAQFLRQQAGIKALVIACNTATAAALTTMQQTLPIPVIGVIAPGAQAAVQTTRNHRIGVIATAGTVKSDQYRRDILAAAPNSQIFSVACPEMVTLAEQNDLTTTHARSVVAANLASLMDKKIDTLVMGCTHFPLLRSAIQHAVGSQVTLVDPGLATAEQTAAILKTHGLLNPATTRGTAQFFTTGETAHFDTLASQWLDQQPMPAKHVSIAQLTTPMEVN | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 29331
Sequence Length: 276
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
|
Q6GHT5 | MNKPIGVIDSGVGGLTVAKEIMRQLPNETIYYLGDIGRCPYGPRPGEQVKQYTVEIARKLMEFDIKMLVIACNTATAVALEYLQKTLSIPVIGVIEPGARTAIMTTRNQNVLVLGTEGTIKSEAYRTHIKRINPHVEVHGVACPGFVPLVEQMRYSDPTITSIVIHQTLKRWRNSESDTVILGCTHYPLLYKPIYDYFGGKKTVISSGLETAREVSALLTFSNEHASYTEHPDHRFFATGDTTHITNIIKEWLNLSVNVERISVND | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 29702
Sequence Length: 266
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
|
B2VEB1 | MDLGSLISETRNPDTLDLDNLSTLDMVTKLNQQDTTVAGAVSRTLPQVAEAVDSAAATLLAGGRLIYIGAGTSGRLGVLDASECPPTFGIPHGVVIGLIAGGPAALVTSVEGAEDDEGLGISDLQAQNLSANDMVIGLAASGRTPYAIGALRYARQLGCRTAAISCNPHSPLALEAEIAISPLVGPEALTGSTRLKSGTAQKLVLNMISTGAMIKIGKVYQNLMVDMRASNVKLVDRARRMVCEATGCEVAQAESALQQAQYEVKTAILMILTDLTAEQAGQRLAMHGGFLRAALQGHSQQPQAHK | Function: Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein... |
Q5NEW3 | MNILENINTEKRNPRSLNLDSMSIAEAVSLMIDEEYGVIEALKEQHRNITEVILATSYSLRNGGRIIYIGAGTSGRLGILDAVECPPTFSVDYNTIVGLIAGGEKAFIQAQEGAEDDANFGKEDLQSINLTAKDIVIGIAASGRTPYVIGALEYANSIGATTVAISCTKQAKISKYAKYSIEAVPGPEVLTGSTRLKAGTTQKLILNMISTLSMVSVGKVYQNLMVDVKPTNQKLIERSKNIVCEATGVDYTTAEKFYLKANKSVKVAIVMILNNCDYEKALAILKNNNNFIKS | Function: Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein... |
Q7NE68 | MDERLPERAHLVTEQVNPDSARLDRLDSPSLVELFCREDERVVPAVRAAAPAIARAIDLTAAALRGGGRLFYVGAGTSGRLGVLDASECPPTFCTDPEQVQGIIAGGTAALTRSVEGAEDDPEAGAAELAGRALSAADVVVGISAGGTAPYVSGALAYARSLGGVTIFVACVPTNQIPERWDIEIRVPVGPEVLAGSTRLKAGTATKLVLNILSTGAMVRLGKTYGNLMVDVAVSNQKLRDRAVRILTTLTELERTAALALLEASGLRVKVALLMHWSNQDPASCATALEAAGGLLPVALEKLSGR | Function: Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate.
Catalytic Activity: H2O + N-acetyl-D-muramate 6-phosphate = (R)-lactate + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 31768
Sequence Length: 306
Pathway: Amino-su... |
P44862 | MNDIILKSLSTLITEQRNPNSVDIDRQSTLEIVRLMNEEDKLVPLAIESCLPQISLAVEQIVQAFQQGGRLIYIGAGTSGRLGVLDASECPPTFGVSTEMVKGIIAGGECAIRHPVEGAEDNTKAVLNDLQSIHFSKNDVLVGIAASGRTPYVIAGLQYAKSLGALTISIASNPKSEMAEIADIAIETIVGPEILTGSSRLKSGTAQKMVLNMLTTASMILLGKCYENLMVDVQASNEKLKARAVRIVMQATDCNKTLAEQTLLEADQNAKLAIMMILSTLSKSEAKVLLERHQGKLRNALSK | Function: Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein... |
Q28KP2 | MGVAAVFTAVQSDLGALVSEASNSRSADIDLMTTAQILACMNAEDRKIADAVAAELPAIAQTVDRIVAAIGRGGRLIYIGAGTSGRLGVLDASECPPTFSVPPGMVVGLIAGGDTALRTSVEAAEDDEATGAEDVKAIGLTTKDVVIGIAVSGRTPFVMGAIDYARRIGAFTAALTCNPGSPMADLADIAISPVVGPEVVTGSTRLKSGTAQKMILNMLSTASMIRLGKTWGNRMVDVTISNRKLADRATAMLRDATGCSADDARTLLDQSNGSVKLAILMQITGCDADAARANLEAENGFLRKAIERAEKTPPQS | Function: Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein... |
Q8GC81 | MSIDLSKLLTERRNANSANIDTLSTVDMLTVINQEDQQVAQAITPYLPQIAEVVDKVAAALRAGGRLIYIGAGTSGRLGILDASECPPTFGTRPEQVVGIIAGGHKAILSAVENVEDNKAQGAMDLQNLNFSNRDVLVGLAASGRTPYVIGAMEYAHSQNAFVAIVSCNPHGEMAQLADVAITPVVGPEVVTGSTRLKAGTAQKLVLNMISTGAMIRIGKVYSNLMVDVEATNAKLIERQVSIVMEATDCDRATAQNALDACGRHCKTAIVMVLADLSAAEAQSLLAKNNGYIRKALSNT | Function: Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein... |
A0QUZ2 | MMPVDDLQEIPLSKDTTEKSKHTVRAAGAVLWRDASEHGGTTGHPATVEVAVIHRPRYDDWSLPKGKLDQGETEPVAAAREIHEETGHTAVLGRRLGRVTYPIPQGTKRVWYWAAKSTGGDFSPNDEVDKLVWLPVDAAMDQLQYPDDRKVLRRFVKRPVDTKTVLVVRHGTAGRRSRYKGDDRKRPLDKRGRAQAEALVAQLMAFGATTLYAADRVRCHQTIEPLAQELDQLIHNEPLLTEEAYAADHKAARKRLLEIAGRPGNPVICTQGKVIPGLIEWWCERAKVRPETTGNRKGSTWVLSLSDGELVGADYLSPPD... | Cofactor: Can also use Mn(2+), with lower efficiency.
Function: Catalyzes the conversion of 8-oxo-dGTP to 8-oxo-dGDP, and 8-oxo-GTP to 8-oxo-GDP . At high enzyme concentrations, can also catalyze the conversion of 8-oxo-dGDP to 8-oxo-dGMP, and 8-oxo-GDP to 8-oxo-GMP . In addition, catalyzes the hydrolysis of the diaden... |
P9WIY2 | MSIQNSSARRRSAGRIVYAAGAVLWRPGSADSEGPVEIAVIHRPRYDDWSLPKGKVDPGETAPVGAVREILEETGHRANLGRRLLTVTYPTDSPFRGVKKVHYWAARSTGGEFTPGSEVDELIWLPVPDAMNKLDYAQDRKVLCRFAKHPADTQTVLVVRHGTAGSKAHFSGDDSKRPLDKRGRAQAEALVPQLLAFGATDVYAADRVRCHQTMEPLAAELNVTIHNEPTLTEESYANNPKRGRHRVLQIVEQVGTPVICTQGKVIPDLITWWCERDGVHPDKSRNRKGSTWVLSLSAGRLVTADHIGGALAANVRA | Function: Catalyzes the conversion of 8-oxo-dGTP to 8-oxo-dGDP, and 8-oxo-GTP to 8-oxo-GDP.
Catalytic Activity: 8-oxo-dGTP + H2O = 8-oxo-dGDP + H(+) + phosphate
Sequence Mass (Da): 34780
Sequence Length: 317
EC: 3.6.1.69
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P9WIY0 | MLNQIVVAGAIVRGCTVLVAQRVRPPELAGRWELPGGKVAAGETERAALARELAEELGLEVADLAVGDRVGDDIALNGTTTLRAYRVHLLGGEPRARDHRALCWVTAAELHDVDWVPADRGWIADLARTLNGSAADVHRRC | Function: May be involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. Mu... |
P9WIX8 | MPSCPPAYSEQVRGDGDGWVVSDSGVAYWGRYGAAGLLLRAPRPDGTPAVLLQHRALWSHQGGTWGLPGGARDSHETPEQTAVRESSEEAGLSAERLEVRATVVTAEVCGVDDTHWTYTTVVADAGELLDTVPNRESAELRWVAENEVADLPLHPGFAASWQRLRTAPATVPLARCDERRQRLPRTIQIEAGVFLWCTPGDADQAPSPLGRRISSLL | Function: May be involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. Mu... |
P96590 | MYTQGAFVIVLNESQQILLVKRKDVPLWDLPGGRVDPGESAEEAAVREILEETGYNAALSAKIGVYQRPKFQDEQHLFFGSITGGQAMADGTETAGLKWVSPGRLPLFMVPNRKRQINDFKNGAQDVNVTVKDSGLLAAIDLLKRRLGK | Function: May be involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. Mu... |
P57298 | MELLSKKKVYITRGKYKKNIWEFPGGKVKKHENIVHALKRELLEEVGIIVLKINFFQYIEYIYPEKKIKLYFFLKKKWKGRPYSIEGYTYLWKRLCHLRALDFPLANHSVINALKKNNILIKFR | Function: Specifically hydrolyzes both 8-oxo-deoxyguanosine triphosphate (8-oxo-dGTP) and 8-oxo-guanosine triphosphate (8-oxo-GTP) to the related monophosphates, thereby cleaning up the nucleotide pools and preventing misincorporation of 8-oxoGua into DNA and RNA. It prevents replicational errors by removing an oxidati... |
P08337 | MKKLQIAVGIIRNENNEIFITRRAADAHMANKLEFPGGKIEMGETPEQAVVRELQEEVGITPQHFSLFEKLEYEFPDRHITLWFWLVERWEGEPWGKEGQPGEWMSLVGLNADDFPPANEPVIAKLKRL | Function: Specifically hydrolyzes both 8-oxo-deoxyguanosine triphosphate (8-oxo-dGTP) and 8-oxo-guanosine triphosphate (8-oxo-GTP) to the related monophosphates, thereby cleaning up the nucleotide pools and preventing misincorporation of 8-oxoGua into DNA and RNA . It prevents replicational errors by removing an oxidat... |
P44932 | MDKKIIQVAAGIIRNEFGQIYLTQRLEGQDFAQSLEFPGGKVDAGETPEQALKRELEEEIGIVALNAELYERFQFEYPTKIISFFFYLVNEWIGEPFGREGQEGFWVEQHALDAGQFPPANAKLIHRLLNETHNFI | Function: Specifically hydrolyzes both 8-oxo-deoxyguanosine triphosphate (8-oxo-dGTP) and 8-oxo-guanosine triphosphate (8-oxo-GTP) to the related monophosphates, thereby cleaning up the nucleotide pools and preventing misincorporation of 8-oxoGua into DNA and RNA. It prevents replicational errors by removing an oxidati... |
P32090 | MMDKKKLHIAAGVICDKHNNVFIAQRPLKSHMGGFWEFPGGKLEDNETPEQALLRELQEEIGIDVTQCTLLDTVAHDFPDRHITLSFFLVTEWKNELTEKKGSCRVGHLLCL | Function: Specifically hydrolyzes both 8-oxo-deoxyguanosine triphosphate (8-oxo-dGTP) and 8-oxo-guanosine triphosphate (8-oxo-GTP) to the related monophosphates, thereby cleaning up the nucleotide pools and preventing misincorporation of 8-oxoGua into DNA and RNA. It prevents replicational errors by removing an oxidati... |
P0CK10 | MAATMIFGSFTHDLLGKAMSTIHSAVTAEKDIFSSIKERLERKRHGKICRMKNGSIYIKAASSTKVEKINAAAKKLADDKAAFLKAQPTIVDKIIVNEKIQVVEAEEVHKREDVQTVFFKKTKKRAPKLRATCSSSGLDNLYNAVANIAKASSLRVEVIHKKRVCGEFKQTRFGRALFIDVAHAKGHRRRIDCRMHRREQRTMHMFMRKTTKTEVRSKHLRKGDSGIVLLTQKIKGHLSGVRDEFFIVRGTCDDSLLEARARFSQSITLRATHFSTGDIFWKGFNASFQEQKAIGLDHTCTSDLPVEACGHVAALMCQSL... | Function: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense... |
P09511 | MEEDDHAGKHDALSALSQWLWSKPLGQHNADLDDDEEVTTGQEELFLPEEQVRARHLFSQKTISREVPAEQSRSGRVYQTARHSLMECSRPTMSIKSQWSFWSSSPKPLPKIPVPSLTSWTHTVNSTPFPQLSTSSGSQSPGKGRLQRLTSTERNGTTLPRTNSGSSTKAMVLHR | Function: Together with movement protein P3a, facilitates long-distance movement of virions in host . Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding (Probable). The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrie... |
P0CK14 | MAAIMIGSISVPIVESARCATVQTGNRVNIVAPGHVAVCKPQMKSHSYYKHASEKLSKQASESINILNSFFDTDPEMRFRLTRNEMSKVKKGPNGRMILRKPRAQRVLERISFEKIEKGAERQVLPWRVYATVTSIINTFTDERNGIANSSLRSPFYKRSCRKEKKKIVCENVVRSASVNNLCDRVLKIAREKNIPVEMIGKKKNRHTLTFKNFKGSFIGKVSLAHERGQMRHVEMSYEQFGFILQAICRVTNTRCVRDEDIKPGCSGWVLGDDHELTQKFSRLPCLVIRGRDDEGIVNALEPVFFYDDVDHYSSQPEVQ... | Function: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense... |
A2RVU1 | MFIFLFGLAAFFLCLSAEFQKAKALLRAQVFLKGKDLKWDGESCYLPENRAFGLGIAALVCVSVAQIVGNVVICRGFTKTDKTRTTIFCIILLLFSWVNFAVAVTLISVGASMNREQIYGKGWLNRECYLVKDGVFAASGFLSVTTMAAILGAFAFKVKPSLQVENHDKRHTQNV | Function: Together with MWL2, contributes to secondary cell wall biology, specifically lignin biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19317
Sequence Length: 175
Subcellular Location: Cell membrane
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O65708 | MHNLFLYSVVFSLGLVSFITCFAAEFKRTQKEDIRWDTERNCYVPGSHAFGLGSAAVLCFCLAQIVGNIVVFRNHRTRTKREDGYKITDLTLPTVLLLLSWSNFVVVVLILSTAISMSRAQAYGEGWLDEDCYLVKDGVFAASGCLAILGLGALTISATRIKVKKQQQLVQVVIKDQNQDQRRSMEEEQKHDEHQTNKSESVIHLVEEVSSTNISRI | Function: Together with MWL1, contributes to secondary cell wall biology, specifically lignin biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24387
Sequence Length: 217
Subcellular Location: Cell membrane
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P09922 | MDSVNNLCRHYEEKVRPCIDLIDTLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLRKLKEGEEWRGKVSYDDIEVELSDPSEVEEAINKGQNFIAGVGLGISDKLISLDVSSPNVPDLTLIDLPGITRVAVGNQPADIGRQIKRLIKTYIQKQETINLVVVPSNVDIATTEALSMAQEVDPEGDRTIGVLTKPDLVDRGAEGKVLDVMRNLVYPLKKGYMIVKCRGQQDIQEQLSLTEAFQKEQVFFKDHSYFSILLEDGKATVPCLAERLTEELTSHICKSLPLLEDQINSSHQSAS... | Function: Interferon-induced dynamin-like GTPase with antiviral activity against influenza A virus, (IAV), influenza B virus (IBV) and Thogoto virus (THOV). Inhibits FLUAV by interfering with the process of primary transcription, probably by affecting the viral polymerase function.
PTM: ISGylated.
Location Topology: Pe... |
P79135 | MVHSDLGIEELDSPESSLNGSEDMESKSNLYSQYEEKVRPCIDLIDSLRSLGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLRLKKLGNEDEWKGKVSFLDKEIEIPDASQVEKEISEAQIAIAGEGTGISHELISLEVSSPHVPDLTLIDLPGITRVAVGNQPPDIEYQIKSLIRKYILRQETINLVVVPANVDIATTEALRMAQEVDPQGDRTIGILTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQDIKHRMSLDKALQRERIFFEDHAHFRDLLEEGKATIPCLAERLTSEL... | Function: Interferon-induced dynamin-like GTPase with antiviral activity against rabies virus (RABV), vesicular stomatitis virus (VSV) and murine pneumonia virus (MPV). Isoform 1 but not isoform 2 shows antiviral activity against vesicular stomatitis virus (VSV).
PTM: ISGylated.
Location Topology: Peripheral membrane p... |
Q5ZMC2 | MTELEGPEFGKADFVLLDEVTMEHFMENLRLRFSKGRIYTYIGEVVVAMNPYQPLELYGPSVVEQYRGRELYERPPHLFALADAAYKAMKRRAKDTCIVISGESGAGKTEASKYIMQYIAAITNPTQRAEVERVKNGLLKSNCVLEAFGNAKTNRNDNSSRFGKYMDINFDFKGDPTGGHIYNYLLEKSRVLQQQPGERNFHSFYQLLLGAPDALLASLHLQRDPTAYCYTQQGTQGSAGGDDARGYRAVEEAMAVIGFTPEEVGAVQRILAAILHLGNVQFVAEGEVAALEAVEQLAVLAQLTGTTPEQLRQALLARTV... | Function: Unconventional myosin required during immune response for detection of rare antigen-presenting cells by regulating T-cell migration. Unconventional myosins are actin-based motor molecules with ATPase activity and serve in intracellular movements. Acts as a regulator of T-cell migration by generating membrane ... |
B0I1T2 | MEDEEGPEYGKPDFVLLDQVTMEDFMRNLQLRFEKGRIYTYIGEVLVSVNPYQELPLYGPEAIARYQGRELYERPPHLYAVANAAYKAMKHRSRDTCIVISGESGAGKTEASKHIMQYIAAVTNPSQRAEVERVKDVLLKSTCVLEAFGNARTNRNHNSSRFGKYMDINFDFKGDPIGGHIHSYLLEKSRVLKQHVGERNFHAFYQLLRGSEDKQLHELHLERNPAVYNFTHQGAGLNMTVHSALDSDEQSHQAVTEAMRVIGFSPEEVESVHRILAAILHLGNIEFVETEEGGLQKEGLAVAEEALVDHVAELTATPRD... | Function: Unconventional myosin required during immune response for detection of rare antigen-presenting cells by regulating T-cell migration. Unconventional myosins are actin-based motor molecules with ATPase activity and serve in intracellular movements. Acts as a regulator of T-cell migration by generating membrane ... |
P02690 | MSNKFLGTWKLVSSENFDEYMKALGVGLATRKLGNLAKPRVIISKKGDIITIRTESPFKNTEISFKLGQEFEETTADNRKTKSTVTLARGSLNQVQKWDGNETTIKRKLVDGKMVVECKMKDVVCTRIYEKV | Function: May play a role in lipid transport protein in Schwann cells. May bind cholesterol.
Sequence Mass (Da): 14950
Sequence Length: 132
Domain: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Subcellular Location: Cytoplasm
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P0C6G6 | MSNKFLGTWKLTSSENFDEYMKALGVGLGTRSLGNLAGPTVIISKSGDVITIRTESGFKNTEISFKLGQEFEETTADNRKTKSTVTLAGGKLNQVQKWNGNETTIKRELVDGKMVVECSMASVVCTRIYEQV | Function: May play a role in lipid transport protein in Schwann cells. May bind cholesterol.
Sequence Mass (Da): 14492
Sequence Length: 132
Domain: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Subcellular Location: Cytoplasm
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P02689 | MSNKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTKSIVTLQRGSLNQVQRWDGKETTIKRKLVNGKMVAECKMKGVVCTRIYEKV | Function: May play a role in lipid transport protein in Schwann cells. May bind cholesterol.
Sequence Mass (Da): 14909
Sequence Length: 132
Domain: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Subcellular Location: Cytoplasm
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P24526 | MSNKFLGTWKLVSSEHFDDYMKALGVGLANRKLGNLAKPTVIISKKGDYITIRTESAFKNTEISFKLGQEFDETTADNRKAKSIVTLERGSLKQVQKWDGKETAIRRTLLDGRMVVECIMKGVVCTRIYEKV | Function: May play a role in lipid transport protein in Schwann cells. May bind cholesterol (By similarity).
Sequence Mass (Da): 14935
Sequence Length: 132
Domain: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Subcellular Location: Cytoplasm
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Q86VE0 | MASAAAGEAEETTRLRKPRFSFEENQILIREVRAHYPQLYGAQSRRVSVAERRRVWDGIAAKINGITSWKRTGQEVQKRWNDFKRRTKEKLARVPHSTQGAGPAAEDAFSAEEETIFAILGPGVAAPGAGAGAEEPPAAPSSQPPPPSACPQRYVLSEDRREDRRADTSAHSKAGSSSPEPWARPSCTPQEGGCPRPKERESPPPSALQPVQLPRLALSPPPPAPPLPPPPPLAQVAPSPPSPPPPPRPPPTLSASDPSLDFLRAQQETANAIRELAGTLRQGLAKLSEALSALLPLLPGTPVDSLPPPLPPPPPPPPPP... | Function: Transcriptional repressor; DNA-binding protein that specifically recognizes the core sequence 5'-YAAC[GT]G-3'. Dimerization with PFN1 reduces its DNA-binding capacity (By similarity).
Sequence Mass (Da): 42508
Sequence Length: 399
Domain: The proline-rich region is required for PFN1 interaction.
Subcellular L... |
P28991 | MGAIDSFCGDGILGEYLDYFILSVPLLLLLTRYVASGLVYVLTALFYSFVLAAYIWFVIVGRAFSTAYAFVLLAAFLLLVMRMIVGMMPRLRSIFNHRQLVVADFVDTPSGPVPIPRSTTQVVVRGNGYTAVGNKLVDGVKTITSAGRLFSKRTAATAYKLQ | Function: Major envelope protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17744
Sequence Length: 162
Subcellular Location: Virion membrane
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Q04565 | MGGLDDFCNDPIAAQKLVLAFSITYTPIMIYALKVSRGRLLGLLHILIFLNCSFTFGYMTYVHFQSTNRVALTLGAVVALLWGVYSFTESWKFITSRCRLCCLGRRYILAPAHHVESAAGLHSISASGNRAYAVRKPGLTSVNGTLVPGLRSLVLGGKRAVKRGVVNLVKYGR | Function: Major envelope protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18925
Sequence Length: 173
Subcellular Location: Virion membrane
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F8QQ74 | MATETIAMDWVDIGTNGESRLAYLARPVVTGRLPAVIVMPAIHGINTYIKDVAIDLAKAGFVALLIDIHSPEQEPDLSNAEKIQIAVETLDDRKVLKDVDAAVRYLEQHAAVRADRLGILGFCVGGTYALLAARTPAIRVSVGFYGLLEYQSRTDNKPVSPLDSVAQFTAPILFHVGDKDPWIDSKMLAEFTKRMQQHQKSYELCIYRGAGHAFHEHFRDAYRPIAAQSAWNNTLIYLRWHLCGKRTV | Function: Involved in the 5-nitroanthranilic acid (5NAA) degradation. Catalyzes the hydrolysis of the lactone to produce maleylpyruvate biodegradation of 5-nitroanthranilate (Probable).
Catalytic Activity: 2-oxo-3-(5-oxofuran-2-ylidene)propanoate + H2O = 3-maleylpyruvate + H(+)
Sequence Mass (Da): 27660
Sequence Length... |
Q9W4C5 | MELKGVQPSNGSSNGSGNGATNAASTEKTDAEKPTAERTNWGNGLEFLMSCISVSVGLGNVWRFPFTAYENGGGAFLIPYIIVLFLIGKPMYYLEMIMGQFTSQGTVKIWSVVPGFVGVGYGQAFGTICIISYYSSLLALTLYYLFVSFQSELPWSYCRDEWTNCVNSRPQEYVDNLLTGVSLANESARNLSGIVANDETEKLQSSSELYFLNVVIKEKLDISDGVGDPDWKLTLALFVAWVVIFLVIMRGVKSSGKAAYFLALFPYVVLFVLLIRAVTLEGARDGILFFLEPQWGELLNPTVWKEAVVQCFFSLAVGSG... | Function: Unusual broad substrate spectrum amino acid:sodium cotransporter that promotes absorption of the D isomers of essential amino acids. Neutral amino acids are the preferred substrates, especially methionine and phenylalanine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71762
Sequence Leng... |
B4L7U0 | MELKTMPHNGANGSPQHNNNNNSNNNNNVSSDTKTDNNEKEAQKKDEGRTNWSNGIEFLMSCISVSVGLGNVWRFPFTAYENGGGAFLIPYIIVLFLIGKPMYYLEMIIGQFTSQGTVKIWSICPSFVGVGYGQAFATICIITYYSSLLALTLYYLFVSFQSELPWSYCRDEWTNCVNSIPTEFVETALGNTTSALAQQANTLSNTTKLQSSSELYFLNVVIKEKSDISDGIGIPDWKLTIALFVSWVVIFLVIMRGVKSSGKAAYFLALFPYVVLFALLGRAVTLEGAVDGIIFFLQPQWGELLNPIVWKEAVVQCFFS... | Function: Unusual broad substrate spectrum amino acid:sodium cotransporter that promotes absorption of the D isomers of essential amino acids. Neutral amino acids are the preferred substrates, especially methionine and phenylalanine (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 719... |
A0A0P0VI36 | MHASCCCAPPESVSHTRRISYKYSGTSYPTRTTTTSSSAPEFTNKKQSTAMAPTTAAAAASSNGGGESDGSSKEWRLTAPTRGGAMAAAGDKMSIRAVRYKISASVDDRGPRPVLPLAHGDPSVFPEFRTAAEAEDAVADALRSGDFNCYPAGVGLPAARRAVADHLSRDLPYKLSSDDIFLTAGGTQAIEVVISILAQPGTNILLPRPGYPNYEARAAFNNLEVRHFDLIPEKGWEIDLNSLESIADKNTTAIVIINPNNPCGNVYTYEHLSKVAEVARKLGILVITDEVYGNLVFGSSPFVPMGCFGHIVPILTIGSL... | Function: Involved in biosynthesis of mugineic acid family phytosiderophores, which are ferric iron chelators produced in graminaceous plants in response to iron deficiency.
Catalytic Activity: 2-oxoglutarate + nicotianamine = 3''-deamino-3''-oxonicotianamine + L-glutamate
Sequence Mass (Da): 53822
Sequence Length: 494... |
Q13506 | MAAALPRTLGELQLYRILQKANLLSYFDAFIQQGGDDVQQLCEAGEEEFLEIMALVGMASKPLHVRRLQKALRDWVTNPGLFNQPLTSLPVSSIPIYKLPEGSPTWLGISCSSYERSSNAREPHLKIPKCAATTCVQSLGQGKSDVVGSLALQSVGESRLWQGHHATESEHSLSPADLGSPASPKESSEALDAAAALSVAECVERMAPTLPKSDLNEVKELLKTNKKLAKMIGHIFEMNDDDPHKEEEIRKYSAIYGRFDSKRKDGKHLTLHELTVNEAAAQLCVKDNALLTRRDELFALARQISREVTYKYTYRTTKSK... | Function: Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2.
Sequence Mass (Da): 54401
Sequence Length: 487
Domain: The NAB conserved domain 1 (NCD1) interacts with EGR1 inhibitory domain and mediates multimerization.
Subcellular Location: Nucleus
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Q61122 | MATALPRTLGELQLYRILQKANLLSYFDAFIQQGGDDVQQLCEAGEEEFLEIMALVGMASKPLHVRRLQKALRDWVTNPGLFNQPLTSLPVSSIPIYKLPEGSPTWLGISCNSYERSSSSREPHLKIPKCAATTCVQSLGQGKSEVGSLALQSVSDSRLWQGHHATESEHSLSPADLGSPASPKESSEALDAAAALSVAECVERMAPTLPKSDLSEVKELLKNNKKLAKMIGHIFEMSDEDPHKEEEIRKYSAIYGRFDSKRKDGKHLTLHELTVNEAAAQLCVKDNALLTRRDELFALARQVSREVTYKYTYRTTRLKC... | Function: Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2.
Sequence Mass (Da): 54010
Sequence Length: 486
Domain: The NAB conserved domain 1 (NCD1) interacts with EGR1 inhibitory domain and mediates multimerization.
Subcellular Location: Nucleus
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Q15742 | MHRAPSPTAEQPPGGGDSARRTLQPRLKPSARAMALPRTLGELQLYRVLQRANLLSYYETFIQQGGDDVQQLCEAGEEEFLEIMALVGMATKPLHVRRLQKALREWATNPGLFSQPVPAVPVSSIPLFKISETAGTRKGSMSNGHGSPGEKAGSARSFSPKSPLELGEKLSPLPGGPGAGDPRIWPGRSTPESDVGAGGEEEAGSPPFSPPAGGGVPEGTGAGGLAAGGTGGGPDRLEPEMVRMVVESVERIFRSFPRGDAGEVTSLLKLNKKLARSVGHIFEMDDNDSQKEEEIRKYSIIYGRFDSKRREGKQLSLHEL... | Function: Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2. Isoform 2 lacks repression ability (By similarity).
PTM: Sumoylation by EGR2 represses EGR2 transcriptional activity in hindbrain.
Sequence Mass (Da): 56594
Sequence Length: 525
Domain: The NAB conserved domain 1 (NCD1) i... |
Q9LKG8 | MKEDMEVLSLASLPVGFRFSPTDEELVRYYLRLKINGHDNDVRVIREIDICKWEPWDLPDFSVVKTTDSEWLFFCPLDRKYPSGSRMNRATVAGYWKATGKDRKIKSGKTKIIGVKRTLVFYTGRAPKGTRTCWIMHEYRATEKDLDGTKSGQNPFVVCKLFKKQDIVNGAAEPEESKSCEVEPAVSSPTVVDEVEMSEVSPVFPKTEETNPCDVAESSLVIPSECRSGYSVPEVTTTGLDDIDWLSFMEFDSPKLFSPLHSQVQSELGSSFNGLQSESSELFKNHNEDYIQTQYGTNDADEYMSKFLDSFLDIPYEPEQ... | Function: Transcription activator essential for the anti-viral defense called virus basal resistance response pathway . Not involved in HRT-mediated hypersensitive response (HR) and resistance to TCV . Binds DNA non specifically . Activated by proteolytic cleavage through regulated intramembrane proteolysis (RIP) (By s... |
Q9FKA0 | MDYEASRIVEMVEDEEHIDLPPGFRFHPTDEELITHYLKPKVFNTFFSATAIGEVDLNKIEPWDLPWKAKMGEKEWYFFCVRDRKYPTGLRTNRATEAGYWKATGKDKEIFKGKSLVGMKKTLVFYKGRAPKGVKTNWVMHEYRLEGKYCIENLPQTAKNEWVICRVFQKRADGTKVPMSMLDPHINRMEPAGLPSLMDCSQRDSFTGSSSHVTCFSDQETEDKRLVHESKDGFGSLFYSDPLFLQDNYSLMKLLLDGQETQFSGKPFDGRDSSGTEELDCVWNF | Function: Transcription activator that binds to DNA in promoters of target genes on a specific bipartite motif 5'-[ACG][CA]GT[AG](5-6n)[CT]AC[AG]-3' . Promotes lateral root development . Triggers the expression of senescence-associated genes during age-, salt- and dark-induced senescence through a regulatory network th... |
Q9LS24 | MGSSCLPPGFRFHPTDEELIEYYLKRKVEGLEIELEVIPVIDLYSFDPWELPDKSFLPNRDMEWYFFCSRDKKYPNGFRTNRGTKAGYWKATGKDRKITSRSSSIIGYRKTLVFYKGRAPLGDRSNWIMHEYRLCDDDTSQGSQNLKGAFVLCRVAMKNEIKTNTKIRKIPSEQTIGSGESSGLSSRVTSPSRDETMPFHSFANPVSTETDSSNIWISPEFILDSSKDYPQIQDVASQCFQQDFDFPIIGNQNMEFPASTSLDQNMDEFMQNGYWTNYGYDQTGLFGYSDFS | Function: Transcriptional activator involved in the positive regulation of abscisic acid (ABA) responsive genes. Acts as a positive factor of ABA-mediated responses. Involved in the transcriptional activation of ABA-inducible genes in response to dehydration and osmotic stresses. Plays a positive role in both stomatal ... |
O04017 | MDIPYYHYDHGGDSQYLPPGFRFHPTDEELITHYLLRKVLDGCFSSRAIAEVDLNKCEPWQLPGRAKMGEKEWYFFSLRDRKYPTGLRTNRATEAGYWKATGKDREIFSSKTCALVGMKKTLVFYKGRAPKGEKSNWVMHEYRLEGKFSYHFISRSSKDEWVISRVFQKTTLASTGAVSEGGGGGGATVSVSSGTGPSKKTKVPSTISRNYQEQPSSPSSVSLPPLLDPTTTLGYTDSSCSYDSRSTNTTVTASAITEHVSCFSTVPTTTTALGLDVNSFSRLPPPLGFDFDPFPRFVSRNVSTQSNFRSFQENFNQFPY... | Function: Transcription activator of STM and KNAT6. Involved in molecular mechanisms regulating shoot apical meristem (SAM) formation during embryogenesis and organ separation. Required for the fusion of septa of gynoecia along the length of the ovaries. Activates the shoot formation in callus in a STM-dependent manner... |
B2VBT3 | MSLMFDVDAAVYPFPAKPIRLSSDEKLAYRTKIKRLLQERDAVMVAHYYTDPDIQALAEETGGCVADSLEMARFGSQHSAATLLVAGVRFMGETAKILSPEKTILMPTLQAECSLDLGCPIDEFSRFCDAHPDRTVVVYANTSAAVKARADWVVTSSIAVELIEHLDSLGEKIIWAPDRHLGQYVQRQTSADILCWQSACIVHDEFKTQALQRMKLLYPEAAVLVHPESPQAIVDLADAVGSTSQLIQAAQTLPHRQMIVATDRGIFYKMQQACPDKELLEAPTAGEGATCRSCAHCPWMAMNGLKAIADGLEQGGSEHE... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 38737
Sequence Length: 353
Pathway: Cof... |
Q8R6C9 | MKDRIKKLQKEKDVAILAHYYVDGEVQEIADYVGDSFYLAKTATKLKNKTIIMAGVYFMGESIKILNPEKMVHMVDIYADCPMAHMITIKKIKEMREKYDDLAVVCYINSTAEIKAYCDVCITSSNAVKIVSKLKEKNIFIVPDGNLASYITKQVKNKNIILNKGYCCVHNLVHLENVIKLKNEYPNARVLAHPECKEEILNLADYIGSTSGIIEEVLKDGNEFIIVTERGIQHKIYEKAPNKKLYFADTLICKSMKKNTLEKIEKILLDGGDELEVNDEIAKKALIPLEKMLELAGD | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 33814
Sequence Length: 298
Pathway: Cof... |
Q5KWQ2 | MNVLEQLKRLDEMPKRYKTMERSELEARARAVKERFGRRLFIPGHHYQKDEVIQFADATGDSLQLAQLAAKNSEAEYIVFCGVHFMAETADILTSDDQTVILPDLRAGCSMADMADIFQVERAWAALIERFGETIVPLVYVNSTAAIKAFVGRHGGATVTSSNAKKMMAWAFSRNERIFFLPDQHLGRNTAYALGIRLDEMAVWDPHEETLQGADDLDKVKVILWKGHCSVHENFTVRQIEHIRRMKPGIHVIVHPECSWEVVQQADYAGSTKYIIETIRNAPPGTQWAIGTEMNLVNRLKHEHPDKEIVSLNPYMCPCL... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 41593
Sequence Length: 367
Pathway: Cof... |
Q74H71 | MHANDIRQDIRKLLKERNAVLLAHNYMRDEVQEIADITGDSLALSQEAARTDADVIVFCGVHFMAESASILSPDKTVLLPRMDAGCPMADMVTAEALLEMKARHPDVPVVTYVNSSAAVKAVSDICCTSANAVKVVNSLPDPEVIFVPDRNLGQFVAKQSDKTFHFWDGFCPTHERLKPADVQRLKEAHPDALFICHPECNPLVVALADHVCSTSGMYDFCRTNPAKRFIIGTEAGILYRLRLENPDKEFILASPALVCPNMKLTSLEDVLASLQTMSPVVKVPEEIRVPAKLALDRMIAIPRD | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 33546
Sequence Length: 304
Pathway: Cof... |
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