ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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Q47LH5 | MTTSFARNVPLADYTTLGLGGPAARFCSVASTDELIATVRDVDRSGDPLLVLGGGSNLVVADEGFAGTVIQVDSSDLSYTEVDDTVVRVRVDAGMEWDSFVARCVDEGLSGVEALSGIPGRVGATPIQNVGAYGQDISQTVVEVTVYDRAADRTRVLSAAECGFAYRTSIFKGRDRYVVCDVVFELTRSKLSRPIRYAELARSLGVSQGDQVPLADVRDAVLSLRRSKGMVLDPADPDTRSAGSFFTNPILSADEFARFTQRVAEVLGPEVTPPAYPDGDGRVKTSAAWLIERAGFPKGYGTGPVGISTKHTLALTNRGGATTADLLALAREVRAGVARVFGITLVNEPVMIGVTL | 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 | MKKVHFIGIGGIGISAIARFLFEKGHKISGSDIKESKTTQELKEQGMDVITPHCKEAIKDQDFVVYSAAIKDDNVELVEARKKGIKCFSRKEILPYVLEDKRVFAVAGAHGKSTTSAMLSSLIEGSVIIGAISKQFGSNMRYAQSDNVVFEADESDSSFLNSNPYLAVVTNAEPEHMEHYDYDLAKFYAAYKGFLERAKVRVINAEDEFLSTLKLDAIRLFPSSDITELAMVVRDYQPYTSFNLKNLGKFEVFGMGQHIAIDASLAILAALHETPLKDIRENLLNFKGIKKRFDILSADKNFILIDDYAHHPTEIRATLNSVFEYAKLLGVSNVTAIFQPHRYTRLSTNLEGFKECFKGVDELVILPVYAAGEKPIEVDMKGAFSEYSPIFTDKVERVGEAIEFTDEFGVKNRLSDGIVVGFGAGDISVQLRGGY | 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 | MMQNIHFIGIGGIGISALARFLREKGFKISGSDLKESKITKELEKEGVKVSIPHHKDNILNKDLVIYSAAIKEENPEFKYAKELGIKCLSRKEALPLILEDKRVFAVAGAHGKSTTSSILASLLDDASVIIGAILKEFGSNMIYKESQNLVFEADESDSSFLNSNPYLAIVTNAEAEHLDHYGNEVSKLHHAYTQFLDVAKIRVINAEDEFLKNYKNESIKLYPSKDIKNCTMCIENFKPFTSFELKDLGEFKVFGMGYHLALDASLAILAALNFLDIETIRTRLKNYQGIKKRFDILHADENLVLIDDYGHHPTEIKATLSAAQEYVKLGGYKKITAIFEPHRYTRLATNLKEFAKAFEGVDELVILPVYAAGEEPIELDLKAVFPKALFVEDIKREGKFLVASKGQVFEEGLIIGFGAGDISNKLRQKNE | 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 | MAYYSTVLKRKVRKMLAVHFIAIGGIGMSGLARILQSKGYRVSGSDLKETELTKKLRAEGITVFIGHREENLASDVSLVVVSTAVSQDNPELLKAKRLGIPVMHRGELLARLMQEKKGIAVAGTHGKTTTSSMIAYVLEKEGFDPVIAVGGEIVDLGYNAKAGQGEYMVAEADESDGSFLKLLPYAAVITNIEADHLDYYQSFEEIKKAFKKFADNIRPEGFGVFCWDNLQVREMLKGYKKRKFTYGFSPGSDFMLRDYREEQNQLVANIYYKNTLEGELRLKVPGKHNILNAAAATAVLRNIGLSFKAISERLLEFNGAKRRFQILGERNGALIVDDYAHHPTEVEATLRAAKLYKDRDVLVVFQPHRYTRTHFFYKEFARVLVDAEKVVLTGIYSAGEKPIPGVSGEMIAEEMKKLGKNPLYLESLDEVYNYLEQNLKPGLLVLLLGAGNINQVGYKLLGKA | 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 | MKMPQTIGVVHFVGIGGIGMSGIAEVLHTLGYHVQGSDQAENANVVRLREKGIKAFIGHAAENLGDAEVVVISSAIKRDNPEYVAARERHLPIVRRAEMLAELMRFRQAVAIGGTHGKTTTTSMVAALLDAGGLDPTVINGGIINVYGTNARMGEGDWMVVEADESDGTFLKLPADIAVITNIDPEHLDHYGSFDKVREAFRQFVENVPFYGLGVMCIDHPEVQALVSRIEDRRVVTYGENLQADVRFENHRMENGHSVFDVIIRARKSDAVKAMRDLRLPMPGRHNVSNATAAIAVANELGMGEEAIRKGLAAFGGVKRRFTLTGTWNGISIFDDYGHHPVEIRAVLKAAREATSGRIIAIAQPHRYTRLRDLFDEFSACFNDADTVLVAPVYAAGESPIAGISSEALVASLRAAGHRDARFIPGPEAIAPIVREAANEGDFVVFLGAGNITQWAYALPKELCS | 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 | MSHYHIIGIAGAGMSAIAHLLLDQGHTVSGSDLTANHATAALQARGVQVWRGHDPAYVQGADVVLATAAIRGTHPELEAAAAAGIPRLSRADLWRLWSEQRPVIAIAGTHGKTTTTALTALALRGAGIRCGFLIGADVPALGGSAQWGDPEAPLVIEADEYDRVFLALTPALAIITNVEWDHPDVYPTPSEYTAAFAAFSRQVRDPRRLLVCADDPGALALAGQSEARLYGIDEHIATDPVSCRLAPLDWTASGVTGTATGQQFDLWYYDRRSFGRRLAATVTLAIPGEHNVRNATAALAAAALWGADLRTAVTALAEYRGSSRRFEWRGDVGGITVIDDYAHHPTEVQATLLAARQRYPDRRLIVYLQPHTFSRTRSLWDQWPAAFREAAVVLVGDIYPAREQGDPVALAQSLVDHLIAHGIPARYAGPSALAPSALLAVAQSGDVVLTLGAGDSDQVAAAFLEQCSAMSEER | 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 | MEKTYHFTGIKGSGMSALALMLHQMGKKVQGSDSTDYFFTQRGLEQADVPLLPFDEKNIKPEFELIAGNAFRDDNNVEIAFAHKNGFPFKRYHEFLGHFMEDFTSIGVAGAHGKTSTTGMLAHVMSNIVDTSYLIGDGTGRGIEGSEYFVFESDEYERHFMPYHPEYTIMTNIDFDHPDYFEGIEDVTSAFQDYANNIKKGIFAYGEDVNLRKLTAKAPIYYYGFEANDDYRAENLVRSTRGSSFDAYFRGEKIGHFVVPAYGKHNVLNALSVVAVCHNLGLDMTEVADHLLTFRGVKRRFTEKKVGETVIIDDFAHHPTEIEATLDAARQKYPDREIVAVFQPHTFTRTIAFADEFAEVLDHADTVYLAQIYGSAREVDHHEITAQDLADKVRKPAKVIDLDNVSPLLDHDRGVYVFMGAGNIQKYELAFEKLLSQVSTNLQ | 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 | MYHIDFTKPIHVHFIGIGGISMSGLAELLHTKGFTVSGSDAKDSKIVDRLRHLGITIFIGQKAENITEDIDLVVYTAAVKSDNVEYQAVQKHNIPMLDRADFLGQVMLQYKNAIGVSGTHGKTTTTSMVSLMMLEGNFDPTISVGGILDNIEGNIRIGHSENFIVESCEYKNSFLSFNPAHAIILNIEAEHLDFFKDIEDIRTSFHTFAKKLPDYGNLVVWGGIDRYEELIEDLSCNVITYGMFSSEEEREQNKDRYDYAACNVTSDDFGLRSYDLYKHGKFVDRINLAVIGDHNVLNSLAAISLVDTLGGTMSAIKKALLAYKGTERRFERKGVLNGITIVDDYAHHPSEIKATLIAAASYPHKDIWCVFQPHTYTRTKSFFHDFTTALALADKIVLADIYAAREENPGDISSKDIQNELLKIGKEAYYISDFAEIEKFLLEHCTNGDLLITMGAGDVVSIGESLLQK | 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 | MNNSEQFLSPRMGRVEQIHFVGIGGAGMCGIAEVLHNQGYRITGSDLGESGTVQRLRSLGIQVYIGHRLENIKGADVVVRSSAVDFNNPEIVAARELMIPVIPRAAMLAELMRFRHGIAIAGTHGKTTTTSLVSSLLAEGGLDPSFVIGGKLNSCGANAQLGKSAYFVVEADESDASFLFLKPMMAVVTNIDADHMDTYEGDFEKLRTTFLEFLHHLPFYGLAVVCLEDEEICRILPAIQRPTLTYGFKEEAHYRAINWTQKGMLSEFVVVRPAPHKQLTIQFQYPGRHNVLNALASIAIATELGVDDDSIVRGLQKFQGVGRRFQMLGEKQFEKGAAIIVDDYGHHPQEILSTIDAFRRVWPERRLVHVFQPHRYTRTQSLHRQFVDVLSLSDELLLMDIYAAGETAIPGVTSENLANEIRSRDKRVTIVSEQSLKATLDEFIKDGDVILMQGAGSIGQIAVNLMKNM | 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 | MKVHMIGVGGAGMSGIAEVLARRGHEVTGSDLKESPYTRRLAAAGVKVYIGHEARQVGDAEVVVISTAIPKTNPELLEARRRSIPVIPRAEALARILAEGRGIAVAGTHGKTTTTSMIAHSLRALGENPTALVGGELNDIGSNVIFGREDLIVAEADESDRSILRLHPQAAVITNIEYDHPDFYASLEEVVETFARFVAGLPPEGHLVLCADDPRCRRLAELAPCPVTTYGLSGGELRARVLSPGSYLLFEGARKRGEVSLGVYGRHNVLNSLAAAGIARWLGHDPLEAARTLGSFGGVRRRFQLKGERSGVRVVDDYAHHPTEIMAILDVARATAAPEGRIIAVFQPHRYSRTRKLYREFGRAFGRADAVVVTEVYGAGEMPQPGVSGKLVVDAICETSDRPEVYYVPDQEALPEVLRMISGPRDTVITLGAGDISRAGEELLARL | 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 | MRLSDLRGRKVAVWGTGREGRAAVVAIAAHGPADLVAVDDGGSTVSPPWDGFLATAAPLVTGDAGAQRLAAADVVVRSPGVPNTHPWLAELWRRQVPVTQGTALWMADHAARTVGVTGSKGKSTTSSLISHLLAAVDQPNVFGGNIGVPTLDLPAADLYVLELSSYQCSDLTDSPRVAVVTALFPEHLDAHGGEREYYRDKLNLLAHGPETVVVNGADPRLAAELGDRPVVRAGTPDTTHVAGGPDGTPWFHLGDQPLFPRAVLPLVGRHNEGNLCVALAVLDVLGVDVLARRDTLAVAVAGFQGLAHRLTEIVDPSGLTFVDDTLATSPYAAMHAIDAYDGRALTVIVGGADRGLDYTPLRDHLAEREITVIGVPDSGARIVAALDGLPKVRCDVTGDLVEAVRLARRVTPAGGVVLLSPAAPSYGQFRNFEHRSEVFAQAVRDTAG | 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
Sequence Length: 448
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.53
|
Q2P5V2 | MRISQFEGKAVALWGWGREGRGAYRALRAQLPTQSLTMFCNAEEVRELESLADAALHVETDASAQALGRFEIVVKSPGISPYRAEALAAAAQGTQFIGGTALWFAEHAQPDGSVPGAICVTGTKGKSTTTALLAHLLRVAGHRTALVGNIGQPLLEVLAPQPPPAYWAIELSSYQTGDVGRSGARPELAVVLNLFPEHLDWHGDEARYVRDKLSLVTEGRPRIVLLNAADPLLASLQLPDSEVLWFNHPEGWHLRGDVVYRGEQAIFDSADVPLPGVHNRRNLCAVLAALEALGLDAEALAPAALSFRPLPNRLQVLGSVDGISYVNDSISTTPYASLAALACFAQRRVALLVGGHDRGLDWHDFARHMAQQAPLEIVTMAANGPRIHALLAPLADAGRFGLHAANDLEHAMQLARDALGGQGGVVLLSPGAPSFGAYSDYVARGRHFAQLAGFDPAAISAIPGLGVH | 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-glutamate
Sequence Mass (Da): 49747
Sequence Length: 468
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.53
|
Q6FFC2 | MLIQRGGLKVVAGLGISGVSAVNFLHEQGYRVAVTDSRETPPGHDQIPQDVQTSFGQLDTELLLQAEEIILSPGLAPQLPEIQQAIAQGIPVIGDIQVLRRATQVPIVAITGSNAKSTVTTLFGQMAKDAGKRVAVGGNLGRPGLDLLKDEPELLVLELSSFQLETTSHLNAEVAVILNMSEDHLDRHGDMLGYHQAKHRIFQGVKKVVYNRDDSLTRPLVPDSTPMQSFGLNAPDIKQYGVLREDDGTMWLARGRTRLIKSSELYIQGTHNIANALACLALGEAIGLPVESMLETLKQFKGLEHRCEYVKTVNDVRYYNDSKGTNVGATLAAIDGLGAAIEPKQGKVIVILGGQGKGQDFSLLRQSVEKYVKAAILIGEDAQQIEQALTETTQLVHASTLKDAVTQAQQYAQPEDVVLLSPACASFDMFKGYPDRGHQFVACVDALV | 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
Sequence Length: 448
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
|
Q7NEZ5 | MAAVAVVGAGKSGQAAARWLALGGRRVVLWDGRDSEALRVVAGALAPFGVEAVLGREFVPEEPDLSLVVVSPGVRWDHPGLVAARARGVTVTGEVGLAWESLSHRRWLCVTGTNGKTTTTALVGHILKTAGLRAPVCGNIGRPVTDLLLEPEDYDWIVAELSSFQIESAQGIRPEVAVWTTFTPDHLNRHGTLERYAAIKAGLLMQARRAVLNGDDAYLGARRSAWPDAWWTSTQAPAAVSLAGKDICIENRPVLPVSAVRLPGAHNLQNVLMAVAACHLTGVGDAAIASGVASFIGVPHRLEAVGEYRGVRFINDSKATNYDAALVGLTAVPAPSVLIAGGQAKTGESGPWLRAIAERCASVVLIGEAAPLFEKWLRAQDYRAVYTAHTLERAVPMAFEQARAQGAQCVLFSPACASFDQFRNFEERGDRFRALIAALAS | 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
Sequence Length: 441
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
|
Q5FUJ7 | MSGFPSDLLAGERYAVCGLGRNGTAVVQALLGMGAEVQAWDDRNADLPAQPNLTVAPLTDLSGMTALILSPGIPHLLPKAHPVADLARAQGIQILSDAEILYRAVRKSGSKAAFIAVTGTNGKSTTTALIAHLFTTAGRPCAAGGNLGTASLALPLLPDDGVYVIEMSSYMLERLDRFHANAACLLNLTPDHLDRHGDMAGYAAAKAHVFDNMGPDDLAVIGMDDDWCRAIASQVASRGVQVVELDADALPPYDGPALPGRHNAQNVGAALTIASHLGLDEAAIRTGLKSFPGLEHRLQKVAECDGVSFINDSKATNAEAVSKALAAYDKVMWIAGGVAKAGGIESLAPFFRHIAQAFLIGQDADVLAATLETHGVPFQQCGTLEKAVPAAFKAALDENIPVVLLSPACASFDQFRSFEDRGSHFLQICDNIVKSGHSGTNPTQKQED | 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
Sequence Length: 448
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
|
Q2S9Z0 | MSILARDRNIAVIGLGKTGLSCADYLTRRGYGFCVMDTRENPSGLAELNAINPDVPVVTGKLDQDMLARAAEIWLSPGVPLSHPDLQAVKGQVKICGDVDVFSREANAPILAITGSNGKSTVTTLVGEMAKACGVNVAVGGNLGTPVLDLLADEVELYVVELSSFQLETTDRLGALAATVLNLSEDHMDRYADMMAYHLAKLRVFYGCRRQVLNRDDALAQPPLSREAEITWFTLKTPEPGQYGVLEEKDGAWLAYGAEKLLPVEQMRIRGKHNWSNALAALALADAAGLEREPCLQALREFTGLTHRCEWVADKDGVAYINDSKATNVGATQAALAGLGPVTSGGIVLICGGQGKGQDFTPLAPAVKEWVSTLIIIGEDGPKLKEALAGGVMALSAETMEEAVKLAAEKSSPGDLVLLSPACASFDMFKNYEDRGDQFKQWVRAL | 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
Sequence Length: 446
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
|
O25236 | MKISLLGHGKTTLALGRFFKKNHNEVKFFDDKFLSSFKDSEGFLCYPSKDFNPNDSQLEIVSPGISFTHPLVIKAKHLVSEYDYINSLFDLVFTPTIISISGTNGKTTTTEMLTMLLEDFKAVSGGNIGTPLIELFEKRSPLWVLETSSFSLHYTNKAYPLIYLLINIEADHLTWHCNFENYLNAKLKVLTLMPKTSLAILPLKFKEHPIIQNSQAQKIFFDKSEEVLERLKIPSNALFFKGAFLLDAALALLVYEQFLKIKNLKWQDYRENALKRLNAFKIGSHKMEEFRDKQGRLWVDDSKATNIDATLQALKTFKNQKIHLILGGDIKGVNLTPLFEEFKNYKISLYAIGSSAFIIQALALEFNVSCQVCLELEKAVQEIKSVLSQNEIALLSPSAASLDQFSSYKERGEKFKAFVLKD | 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
Sequence Length: 422
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
|
Q31I61 | MYLVAGLGLTGQSVLNYFASQGEPCYALDTRPEFDTSELEKAYPDVAFATGTLPTQWCGKIDSIVLSPGIAKSEPWVKHCINQGTEVIGDIELFARAAGKPIVAITGSNGKSTVTTLVAEALKEAGYAVGVGGNIGCPALDLLTHPTEFDVYVLELSSFQLETTYSLQTIAATVLNISEDHMDRYLALEDYIQAKMTILNNTELAVLPLDFERVGIARPGDEVRFGLNYAEALPPKEYGIVMKNGQAWLGWEDHASVPVTAMAQQGLHHQLNALAMMALCRPFDLSDAVFEKVLKTFKGLPHRTQVVLEQEGVRWINDSKGTNVGATVTAIESIKETLDGQVILIAGGVGKEADFNELGQAVVQSCRQAILFGQDKAIIAQQLPQEKIQLVDTLSEAVLLAKTIAKSGDAVLFSPACASFDQFKNYIERGNAFEAFVQQFIANEVGGKS | 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
Sequence Length: 449
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q5R0M3 | MTKIAWQNTKHIVVLGLGKTGVSVLRYLQHKRQQDQKLAEVKIQVFDSRENPPGLEEAKQILGDAELINRHWELEDTLAADLIIASPGIDLREDPVVLARDADIPIVGDVELFAQESKLPIVAVTGSNGKSTVTRMVEFVAKQCGKNVAAAGNIGVPVLDLLLQEQHPDAVILELSSFQLESVSSLKLKAAALMNISADHMDRYCTLDEYVKAKQRIFTHAKTWILNRQQQDTWPHPVTGKLMTFGNDSHPKHFGLLSGNIDRVSGPVAVTFDGSVVLRADQLQLQGIHNLVNVQAALALCQAIDIDIEAAVRAVKEFKGLPHRCELVSDNEGVLWVNDSKATNIGATAAAVEGLRPMINGRLLLIAGGVGKGADFRELQSTLERVDILLTIGEDGPRIGQLFNGSRQVKSLQQAVELAASLVQTGDMVLLSPACASFDQFQNFEHRGDSFRHAVEALYVNSA | 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
Sequence Length: 463
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q1IKG8 | MDVRGKRVLVVGLGKSGIASATFLQAQGAKVTVSDSKSEAQLRQEIPLLLDKGITVETGHHGERTFRDQDLIVISPGVPFDQPQLEQARKQGIPVIGEIELAAQFVPGHVIAITGSNGKTTTTSLCGDILQSGGKKTLVGGNIGTPAISFAQLANDDTWSVLEISSFQLETIERFRPEIAAILNITPDHLDRHGTFEKYAAAKERIFENQREHDFAILNADNEPCVEIAKRVKSQVLWFSRQHEVKHGTFVREDKIYFRDPKGEREIMPVADMLLKGAHNVENVLAAVCVGVAASVAPEQIRKAVSQFKAVEHRLEYTATVKGVDYYNDSKATNVDATIKALESFSKGVHLILGGKDKGSPYTVLNDLLHERAKTVYTIGAAAAKIEAEVKGVEVVHAETLENAVKLASQKAVKGDVVLLAPACASFDQFQSYEHRGRIFKELVRKMAEQEKK | 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
Sequence Length: 453
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q8CSX6 | MLNYTELENKNVLVVGLAKSGYEAAKLLLKLGANVKVNDGKDLSQDAHAKDLESMGIEVISGSHPFSLLDDDPIIVKNPGIPYTVSIIKEATNRGLKILTEVELSYLISEAPIIAVTGTNGKTTVTSLIGDMFQKSVLTGRLSGNIGYVASKVAQEVKSDEYLITELSSFQLLGIEEYKPHIAIITNIYSAHLDYHETLENYQNAKKQIYKNQTKDDYLICNYHQRHLIESENLEAKTFYFSTQQEVDGIYIKDGFIVFNGIRIINTKDLVLPGEHNLENILAAVLASIIAGVPVKAIVDSLVTFSGIDHRLQYIGTNRTNKYYNDSKATNTLATQFALNSFDQPIIWLCGGLDRGNEFDELIPYMENVRVMVVFGETQDKFAKLGNSQGKYVIKATDVEDAVDKIQDIVEPNDVVLLSPACASWDQYHTFEERGEKFIDRFRAHLPSY | 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
Sequence Length: 449
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q82AD8 | MTNWQGKNVTVAGLGVSGIPAARVLHGLGAVVTVVNDGDDERSRAQAADLEALGITVRLGDGATLPEGTELIVTTPGWQPDKPLFAAAAEAGVPVWGDVELAWRLRGPGSAPWLAVTGTNGKTTTVQMLASILTAAGLRTAAVGNIGVSLLDAVLGEETYDVLAVELSSYQLHWAPSLRAHSATVLNIAPDHLDWHGSMEAYTADKGRIYEGNRVACVYNVADKATEDLVRAADVEEGCRAVGFTLGTPGPSQLGVVEGILVDRAFVEDRQKNAQELAEVADVHPPAPHNIANALAAAALARAFGVPASAVRDGLRAFRPDAHRIAHVADVDGVTYIDDSKATNTHAAEASLAAYGSIVWIAGGLAKGASFDELVAKSAQRLRGVVLIGADRALIREALARHAPEVPVVDLDRTDTGAMPAAVQEARRLAVAGDTVLLAPACASMDMFANYNKRGDAFAEAVRGLGA | 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
Sequence Length: 467
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q9S2W9 | MPSEFSGKHVTVAGLGVSGVPAAKVLHGLGAQVTVVNDGDDERARTQAAELEPLGVTVRLGDGDTLPEGTELIVTAPGWKPTKPLFTAAGQAGVPVWGDVELAWRLRGLNGRKPAPWLAVTGTNGKTTTVQMLASILKAAGLRTAAVGNIGVSLLDAVTGEQEYDVLAVELSSYQLHWAPSLRAHSAAVLNLAPDHLDWHGSMEAYAADKGRIYEGNHVACVYNVADKATEDLVRAADVEEGCRAIGFTLGTPGPSQLGVVEGLLVDRAFVEDRQKNAQELAEVSDVNPPAPHNIANALAAAGLARAFGVSAAAVRDGLRAFTPDAHRIAHVADVDGVAYVDDSKATNTHATEASLAAYESIVWIAGGLAKGATFDELVAGAAKRLRGAVLIGADRALIREALARHAPEVPVVDLDRTDTGAMLQAVQEARRLARPGDTVLLAPACASMDMFTNYNQRGDAFAQAVRELGA | 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
Sequence Length: 471
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.9
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Q4L525 | MNANELFEKIRVKQVIGTLDINVTDITTDSRTASEGSIFVASKGYTVDSHKFCQNVVDQGAKVIVVNHQQDINGDVTQVIVPDTLRVASLLAHTLYDFPSHQLTTIGVTGTNGKTSIATMIHLIYRGLGKGSAYLGTNGFQINEHKTRGANTTPETVSLTKKIKQAVDENAEAMTMEVSSHGLSLGRLRGVEFDVAIFSNLTQDHLDFHGTMEAYGHAKSLLFSQLGEDLSKEKYAVLNNDDDFSKYLASVTPYEIFTYGIDHDAQFMAKNIQESLQGVHFDFDTPIGTYSVKTPYVGKFNISNIMAAMIAVWSKGTSMEDIVRVVENLEPVEGRLEVLDPSLPIDLIIDYAHTADGMNKLIDAVKPFVKQKLIFLIGMAGERDLTKTPEMGAVACRADYVIFTPDNPANDDPKMLTAELAKGATHNHYVEFDDRAEGIKHAIDIAEPGDTVVLASKGREPYQIMPGHIKVPHRDDLIGLEAAYKKFGGGPSEH | 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: ATP + L-lysine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysine
Sequence Mass (Da): 54177
Sequence Length: 494
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.7
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Q9S2W7 | MTYPGPPRPVRISATPLAELADQLGVAAPDGSAEITGITHDSRAVRPGDLYAALPGARLHGADFVTQAAGLGAAAVLTDPAGAERAAAAGLPALVVDDPRARMGELAATIYGHPGRDLLQIGITGTSGKTTTAYLVEGGLRTAKSTGLIGTVEMRIGDERIKSERTTPEATDLQALFAVMRERGTEAVAMEVSSHALVLGRVDACVFDIAVFTNLSPEHMEFHSGMEDYFQAKAQLFTPKRSRLGVVNVDDEYGRRLAKEATVPVVTYSAEGHPDADWRADEVEVGPLDSTFTVLGPKGERIAAKSPLAGPFNVANTLAAIVALAAAGLDPQSAADGVAAVPGVPGRLERVDEGQPFFAVVDYAHKTDAVESVLRALRKVTEGKLHAVLGCGGDRDTTKREPMGAAVARFADTAVLTSDNPRSEDPLAILATMLQGAASVPAHERGEVQVFEDRAAAIAAAVARAEPGDTVLVAGKGHEQGQDIAGVVRPFDDRQVLREAIKKTQG | 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.
Catalytic Activity: ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 52829
Sequence Length: 506
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.13
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Q9A196 | MITIEQLLDILKKDHNFREVLDADGYHYHYQGFSFERLSYDSRQVDGKTLFFAKGATFKADYLKEAITNGLQLYISEVDYELGIPVVLVTDIKKAMSLIAMAFYGNPQEKLKLLAFTGTKGKTTAAYFAYHMLKESYKPAMFSTMNTTLDGKTFFKSQLTTPESLDLFAMMAECVTNGMTHLIMEVSSQAYLVDRVYGLTFDVGVFLNISPDHIGPIEHPTFEDYFYHKRLLMENSRAVVINSGMDHFSFLADQVADQEHVFYGPLSDNQITTSQAFSFEAKGQLAGHYDIQLIGHFNQENAMAAGLACLRLGASLADIQKGIAKTRVPGRMEVLTMTNHAKVFVDYAHNGDSLEKLLSVVEEHQTGKLMLILGAPGNKGESRRADFGRVIHQHPNLTVILTADDPNFEDPEDISKEIASHIARPVEIISDREQAIQKAMSLCQGAKDAVIIAGKGADAYQIVKGQQVAYAGDLAIAKHYL | 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: ATP + L-lysine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysine
Sequence Mass (Da): 53513
Sequence Length: 481
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.7
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Q3J4M2 | MGRPLLLIAAGGTGGHMFPAQALAEAMVRRGWRVKLSTDARGARYAGGFPHVVEIEEVSSATFARGGPLAKALVPLRIAGGVASAVAGFLRDRPSVVVGFGGYPSIPALSAAVALRLPRMIHEQNGVLGRVNRLFAPRVQAVCCGTWPTDLPEGVEGYYTGNPVRAAVLERAAAPYIVPGDYPMSLVVIGGSQGARVLSDVVPEAIARLPEEILANLRIAHQAREEDVARVTEAYDRAGLLAEVKTFFTDIPRRLSEAQLVISRSGASSVADISIIGRPAILVPFAAATADHQTANARGLVEAEAAILIPESALDPGALSEHIAAVLSQPDAARQMARNALAHGRPDATERLVEVVEHLARKET | 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-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38300
Sequence Length: 364
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
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Q9Z702 | MMKKIRKVALAVGGSGGHIVPALSVKEAFSREGIDVLLLGKGLKNHPSLQQGISYREIPSGLPTVLNPIKIMSRTLSLCSGYLKARKELKIFDPDLVIGFGSYHSLPVLLAGLSHKIPLFLHEQNLVPGKVNQLFSRYARGIGVNFSPVTKHFRCPAEEVFLPKRSFSLGSPMMKRCTNHTPTICVVGGSQGAQILNTCVPQALVKLVNKYPNMYVHHIVGPKSDVMKVQHVYNRGEVLCCVKPFEEQLLDVLLAADLVISRAGATILEEILWAKVPGILIPYPGAYGHQEVNAKFFVDVLEGGTMILEKELTEKLLVEKVTFALDSHNREKQRNSLAAYSQQRSTKTFHAFICECL | 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-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39420
Sequence Length: 357
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
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B3QWT7 | MKLIFAGGGTGGHVFPAIAIAQEILRTQQNAEIQFVGTERGIEATAVPKQGFPMHLIPVAGVKRGFSPKELFENLKVPMRLQRSLSACHDILQREKPNVVIGTGGFVSGPIVWEAQSKKIPTLIQEQNSMPGVTTRLLSLRASEVHLSFEESKTYIRRTNGVFVTGNPTRQFQSHRPAQAKAFFSLDSTRKTLLVFGGSLGARSINQAIESNLEEWLEKFNLIWQTGKLDFADIATRIGSRKNLWYNAFIDQMDMAYAAADLAVCRAGASTLAEITHLGKPSVLVPYPYAAANHQFYNAKSLADNHAALLIENKDIGLETSKTEIMSLLQNESRLKQMSENSLKLGKPHATRIIAEHVIRLAELG | 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-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40232
Sequence Length: 365
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
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Q8KGD4 | MKVLFAGGGTGGHLYPGVAMAAELKKRVPGISISFAGTSAGIEATEVPRLGYRLVLFPVRGLKRGLSIRALVENALILGDFAKSLSMAMALVRKEQPDVVVGTGGYVSAPLLLAAQLSGKKTLIQEQNAFPGVTTRLLARMATEVHLSFEESRKFFGGKSEVFVTGNPAREFPAESRESCLDFFGLDRSLPTLLVFGGSRGARAINNAVLKLCHRLEGTVNLIWQTGALDADRMRGEIGTSATRWIGPYIQEMGKAYGAADLVLCRAGASSLAELTNLGKPSVLIPYPYAAADHQRHNAMALVSAGASVMIDDSKIGEEASFDVILTLLRDREKLAQMGEAARREGHPGAAATLAERIIALSKS | 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-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38709
Sequence Length: 364
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
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A1R5F8 | MTFDSANASKPLSVVLAGGGTAGHVSPLLAIADAIREKRPEAAILAVGTPSGMETRLVPAAGYELATIDRVPFPRRPSADLVKLPARLSGAVRQARRILEEARADVLVGVGGYVCTPMYLAARKLRIPIVIHEANMKAGLANRVGARFSNHVAVAFAGTRLRGARHVGMPMRRAISGLDRAVAAPAARAALGLDAQRPALIVTGGSSGALSINRAITAALPALAAAGVQTLHITGNGKAVKDDDGGLLTADGYRQVEYVDGMENVYAAADVLLARAGAGTVSEVAAVGVPAVFVPLPIGNGEQALNAAPLVAAGGAVMVDDKDLSPEWLRSELIPLLTDRSRLNEMARKSEALGIRNADQRMADLVLEAVSA | 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-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38405
Sequence Length: 372
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell membrane
EC: 2.4.1.227
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A6LEU3 | MRKYRIIISGGGTGGHIFPAISIANTFKKRFPDAEILFVGAEDRMEMDKVPAAGYKIVGLPVSGFDRAHLMNNVKVMVRLAKSLRLARKTIREFKPDIAVGVGGYASGPTLWMAASQGVPALIQEQNSYAGVTNKLLAKKASKICVAYEGMEKFFPADKIVITGNPVRQDLEEALSKKEEALAFFGLSPEKKTILVVGGSLGARTINRSIQGDLDKFFASDVQVIWQTGRYYYSDASKHLKAYRGMPVWCSDFITRMDYAYSAADLVISRAGASSISELCLLGKPVVLVPSPNVAEDHQTKNALALVHKDAAVMIADKDAEKDLVPTALKIVHDDERLCTLSRNIETLAQRHSADRIVDEIVKIIDKK | 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-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40344
Sequence Length: 368
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
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Q6MBS7 | MSKRFMITAGGTGGHIFPAQGLAQELIKKTYSSSILFVAGGLSTNKYFDRSIFPFQEVSASPLFSKNPFKLLKGVFNLLRGVWQSIRIIRKFKPDVVVGFGSYYTVPPLLAAKILRIPIVLHEANSIPGKANKWLASMAWRVGIHFPFTATLLKGNTIEVGMPLREGYQLDQIDKIEALSYFGLSKNNSTLLVFGGSQGALAINRLMRNLANTWKNTPIQIIHITGSIQEADELKIFYANYQVKASVKAFEKNMHLAWRAAEVFISRSGASTIAEAMEFEVPGILIPYPHATDHHQDKNADFFVDIVKGGIKIVEEKAKPEIVLKSIQLLIDPIALDKRKSAIHSYKCRPDRTTLCELVLDTSELKSLHKAPQKRK | 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-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 41939
Sequence Length: 376
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
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A1AU61 | MKLIIAGGGTGGHLFPGIAVAEEFLSRDPANQVLFVGTERGIEARAVPAAGFPLELISAAGIRGKGGLGKLRGAAMMFNGYRQSCRLLDRFRPDAVLGVGGYASLPMLLAARTRQVPSFIHEQNAVPGMTNRLLSRFADRIFITLEESSRFFAGRRTLLTGNPLRRQILDRLGTRDQGPGIRDQEKHMTDSTGPASRVPGPRFNLLVFGGSQGAHAINMAMVAALPLLKRASVRLGITHQTGESDRERVAAAYRSAGVEARVLPFIADMASEYARADLVVCRAGATTIAEVTALAKACLFIPFPYAVDDHQRRNAEALLRQSACFMLLERELSAERLAALILQLAGDPRLVRRTGELAFSMARLDAARIIVDEILTPTN | 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-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40969
Sequence Length: 379
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
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Q4FPK5 | MNKKILISTGGSGGHVIPATIIYKHLEDNFDVSMTSDFRGVKFLNKDEYNLKIFNVRPISKNLLIIPLDFIFMIFLIFKSISFFRKNKIDTLISTGGYMSLPLCLGARILNIKLLLFEPNMVLGRSNKFFLSYCQKIFCYSNNIKKFPIKFKNKIKVIPALLRKNFYNKRDYNKSLDTINLLIIGGSQGAKIFDDLVKNAIIELAKNYKLKIYQQTNSINFESFKKIYEDKNIQCELFNFNDDVVNFMQKTDLCITRAGASTLAELNFTETPYLAIPLPTAKDNHQFENAHFYNKLGFNWLLNQKEIDEKTLLNKLINIIDNKEEYLVKKKNMKDFNYENTWNNINLKIISVINEN | 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-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 41442
Sequence Length: 356
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
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B4RFS0 | MRKTAVVAAGGTGGHLFPAQALAEALIARGWRIVLASDERVAGLAQDFPAERRIGLSAATYRPGDPVGMMRAGFAVLRGAMHARAAFREIGPDVVVGFGGYPSAPALVAAILDRRPTVIHEQNAVMGRTNRILAPHVRTVACAFPTLKKAPPKVAGRAVVVGNPVRPPIRALADVPYVPPEPNGPVRLLVTGGSQGARLLSELVPEAVKALPEDLRRRLTVHQQTRPESMNTARRAYRDALVDAEIAPFFRDIAGRLREAHLVVGRAGAGTVCEFAIAGKPSILVPLAIALDDDQGQNARLLADAGGAEVARENQLTVDTMANALEKLLTNPARLQRMAEAARSVAIPDAAERLADVVEQTARGR | 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-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38674
Sequence Length: 365
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
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Q30PK0 | MRLCITGGGTGGHLMIAEALVEACANDGHEAIFIGSTSGQDRKYFEQNSKFSHVYFLQTTGVVNQRGLGKLKALWLVLRAFFASRAILKKHNIQATYSVGGFSAAAASFASLSRLIPLFIHEQNAVYGKLNSILKPFATRFISAYDEASPIKGYPVKDIFFKNARLRDEIKCVIFLGGSQGAKAINDLALSVALELEARGVKIIHQAGERDYERVKSAYEELGVKAELCGFTKEMPSLMARADLAVSRSGASTLWELCANALPSFFIPFPHAASDHQYHNAKFIVDNELGWCQREEEDLRATLLSILPQNLADKSKALMEYSSRDVAKKMITDVVMSLNA | 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-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37393
Sequence Length: 340
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
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B2V7Y8 | MKKVFISGGGTGGHFYPALSVAENLKEKGFSITYIGTTNGIENKKDFPADEKILYPMRAVRGKSIVGKIQGVFSLLSTTFKVYKQIKKEKPDFSICFGGYTSIPLGLASFLARVPLYIHEQNSIPSYSNKILSYFAKKVFITFELTAKYFDRKKTVLTGMPLRKNIIERAKNYVYKPNQTKTVLVVGGSQGAKKLSESIISLASEMKDIKFILIKGKWQVEVPNLENLTVYEYVDNMEDLYTSADVVISRSGSSSVNEILCFGKYAIFVPFPYAASNHQYYNVKWLKDLGLCELIEEKDLSKEVLKKALEDAFNKDLESLSKKIKEYAIFDSDEKIVENILNDFKND | 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-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39217
Sequence Length: 347
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
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Q67Q48 | MRYLITGGGTGGHIYPALSIARALTEQDPEAELLYVGTRTGREAAIVPQAGIAFAVISSGGVVNLGLLQRVRGGLRAARGLLEALGHIRRFRPDIVIGTGGFVAGPVLAAARLARVPLVIQEQNAFPGVTNRLAARWATAVFVPYEEARAHFPPGVRLIRAGNPVRPEIASASREAGRQALGLSERDRVLVIMGGSGGARDFNRVAAEAVLQLDVPGLRVVHITGERYFGQVKAQYGDRAPHVTLLPYAHNMPEVYAAADAGLFRAGALTLAEIQVRRLPSVLIPSPNVTHNHQEWNARTLERRGAAIVLREGGLTPADLAAALTRLLTDEALADRMRAALGEVADPDAARTIARRIVGIARQSREAREARRGR | 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-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39993
Sequence Length: 374
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell membrane
EC: 2.4.1.227
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Q2LR48 | MTVRVIIAGGGTGGHLFPGVAIAEELLRRDRENRVLFVGTKRGIEKKVLKDLGFRLKLLNVEGIKGRGVMRSSLALLKLPGSLMQSMKIIRDFRPDVVIGVGGYASGPAVMAAHLMGIKTAIAEQNSIPGLTNRILGRFVDRVFLSFSDGGKWFSAKKAAVSGNPIRAAFFNGKPVLEKTGDQFSLLVFGGSQGAHAINSAFQDALPFLQLLKGCLRIVHQTGERDCESMAAAYSAQGFSARVVPFIRDMAAAYEAADLLICRAGATSIAEITAIGKAAILIPFPYAIGDHQTENAKVLLKAGAAVMIPEKDLTGKKLADEIQNFYSHPSLLKDMEAKAASLGNIYAASDIVDSCMAMIRL | 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-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38563
Sequence Length: 361
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
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Q3A2G6 | MKLLLAGGGTGGHLFPAVALAQRLLEQDSEAQVQFVGTARGIEARVLPEQGWPLELIDIRGFVNQGLLGKLRMIPCLIRSVWQGLCILRKFQPDVVLGVGGYASAPMLVAARLKRIPTVIHEQNAWPGLTNRLLGPWARCVCLSFSEAERAFHRAATIVTGNPLRKGMEGCPPMDGDAPELLVFGGSRGARAINDAMLEALPRLEPWKDRLRIVHQTGGDDLQRIREGYARAGWPQESVVPFIDDMAAAYARAHLVVCRAGATTLAELAACGRAAILIPYPHAAADHQTVNARAMAKKGAGLVLAQQNLTPETLASLITDLLENRPRLISMSAAAKSLGITGAADRILRVCRNVCGQD | 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-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38514
Sequence Length: 358
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
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Q2JW21 | MNGDRRDPTSPPRLLVAASGTGGHIFPALAVVEQLPTWQIEWLGVPQRLEAKLVPDRYPLHRVAMSGWQGSPWQKLGSLVQLARATLQVRQILASGQFDVVLTTGGYIAAPTILAARSLGVPVLLHESNCLPGKVTRWLGRFCRLVALGMAETAEHLPGAVTRVVGTPVRAEFYQPQPLPADLPIPEGDPLIVVMGGSQGARGLNRLVAACAPAWLEAGAWIVHLTGGSEVGIPSHPRYRAFPFRADVAALLQRATFAISRAGALSLAELWATATPAILIPYPFAAEDHQYHNALAFVGRGGGVVMRESEANLDLLRQTALAWLAQPQVVAQMAANLKATAPPAASKAVARLLQEICRDSAR | 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-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38671
Sequence Length: 362
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.227
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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, and thus plays a role in cell wall recycling.
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-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
EC: 4.2.1.126
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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, and thus plays a role in cell wall recycling.
Catalytic Activity: H2O + N-acetyl-D-muramate 6-phosphate = (R)-lactate + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 31814
Sequence Length: 294
Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
EC: 4.2.1.126
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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-sugar metabolism; N-acetylmuramate degradation.
EC: 4.2.1.126
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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, and thus plays a role in cell wall recycling (By similarity).
Catalytic Activity: H2O + N-acetyl-D-muramate 6-phosphate = (R)-lactate + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 32532
Sequence Length: 303
Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
EC: 4.2.1.126
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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, and thus plays a role in cell wall recycling.
Catalytic Activity: H2O + N-acetyl-D-muramate 6-phosphate = (R)-lactate + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 32510
Sequence Length: 316
Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
EC: 4.2.1.126
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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, and thus plays a role in cell wall recycling.
Catalytic Activity: H2O + N-acetyl-D-muramate 6-phosphate = (R)-lactate + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 31603
Sequence Length: 300
Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
EC: 4.2.1.126
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A0QUZ2 | MMPVDDLQEIPLSKDTTEKSKHTVRAAGAVLWRDASEHGGTTGHPATVEVAVIHRPRYDDWSLPKGKLDQGETEPVAAAREIHEETGHTAVLGRRLGRVTYPIPQGTKRVWYWAAKSTGGDFSPNDEVDKLVWLPVDAAMDQLQYPDDRKVLRRFVKRPVDTKTVLVVRHGTAGRRSRYKGDDRKRPLDKRGRAQAEALVAQLMAFGATTLYAADRVRCHQTIEPLAQELDQLIHNEPLLTEEAYAADHKAARKRLLEIAGRPGNPVICTQGKVIPGLIEWWCERAKVRPETTGNRKGSTWVLSLSDGELVGADYLSPPDEK | 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 diadenosine polyphosphates diadenosine hexaphosphate (Ap6A), diadenosine pentaphosphate (Ap5A) and diadenosine tetraphosphate (Ap4A) .
Catalytic Activity: 8-oxo-dGTP + H2O = 8-oxo-dGDP + H(+) + phosphate
Sequence Mass (Da): 35923
Sequence Length: 322
Domain: Contains an N-terminal Nudix hydrolase domain, followed by a linker region and a C-terminal histidine phosphatase domain. The C-terminal domain is necessary for efficient catalysis by the Nudix hydrolase domain.
EC: 3.6.1.69
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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. MutT specifically degrades 8-oxo-dGTP to the monophosphate (By similarity).
Catalytic Activity: 8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+)
Sequence Mass (Da): 15160
Sequence Length: 141
EC: 3.6.1.55
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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. MutT specifically degrades 8-oxo-dGTP to the monophosphate (By similarity).
Catalytic Activity: 8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+)
Sequence Mass (Da): 23499
Sequence Length: 217
EC: 3.6.1.55
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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. MutT specifically degrades 8-oxo-dGTP to the monophosphate (By similarity). Functions, in conjunction with ytkD, to protect vegetatively growing cells from DNA-damaging agents such as H(2)O(2) or t-BHP (t-butylhydroperoxide). The 2 proteins do not however protect spores.
Catalytic Activity: 8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+)
Sequence Mass (Da): 16398
Sequence Length: 149
EC: 3.6.1.55
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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 oxidatively damaged form of guanine (8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP can be inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions.
Catalytic Activity: 8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+)
Sequence Mass (Da): 15061
Sequence Length: 124
EC: 3.6.1.55
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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 oxidatively damaged form of guanine (8-oxo-dGTP) from DNA and the nucleotide pool . 8-oxo-dGTP can be inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions . MutT may also ensure transcriptional fidelity, removing 8-oxo-GTP from the ribonucleotide triphosphate pool . However, due to the lower efficiency of RNA polymerase 8-oxo-GTP incorporation, MutT is probably not a major contributor to transcriptional fidelity . It also hydrolyzes 8-oxo-dGDP and 8-oxo-GDP to their monophosphate form . In vitro, can also use dGTP, dGDP and other various nucleoside di- and triphosphates, with much lower efficiency . Works cooperatively with MutM and MutY to prevent accumulation in the DNA of oxidized guanine residues .
Catalytic Activity: 8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+)
Sequence Mass (Da): 14927
Sequence Length: 129
EC: 3.6.1.55
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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 oxidatively damaged form of guanine (8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP can be inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions.
Catalytic Activity: 8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+)
Sequence Mass (Da): 15648
Sequence Length: 136
EC: 3.6.1.55
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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 oxidatively damaged form of guanine (8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP can be inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions.
Catalytic Activity: 8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+)
Sequence Mass (Da): 12774
Sequence Length: 112
EC: 3.6.1.55
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P0CK10 | MAATMIFGSFTHDLLGKAMSTIHSAVTAEKDIFSSIKERLERKRHGKICRMKNGSIYIKAASSTKVEKINAAAKKLADDKAAFLKAQPTIVDKIIVNEKIQVVEAEEVHKREDVQTVFFKKTKKRAPKLRATCSSSGLDNLYNAVANIAKASSLRVEVIHKKRVCGEFKQTRFGRALFIDVAHAKGHRRRIDCRMHRREQRTMHMFMRKTTKTEVRSKHLRKGDSGIVLLTQKIKGHLSGVRDEFFIVRGTCDDSLLEARARFSQSITLRATHFSTGDIFWKGFNASFQEQKAIGLDHTCTSDLPVEACGHVAALMCQSLFPCGKITCKRCIANLSNLDFDTFSELQGDRAMRILDVMRARFPSFTHTIRFLHDLFTQRRVTNPNTAAFREILRLIGDRNEAPFAHVNRLNEILLLGSKANPDSLAKASDSLLELARYLNNRTENIRNGSLKHFRNKISSKAHSNLALSCDNQLDQNGNFLWGLAGIAAKRFLNNYFETIDPEQGYDKYVIRKNPNGERKLAIGNFIISTNLEKLRDQLEGESIARVGITEECVSRKDGNYRYPCCCVTLEDGSPMYSELKMPTKNHLVIGNSGDPKYLDLPGEISNLMYIAKEGYCYINIFLAMLVNVDEANAKDFTKRVRDESVQKLGKWPSLIDVATECALLSTYYPAAASAELPRLLVDHAQKTIHVVDSYGSLNTGYHILKANTVSQLEKFASNTLESPMAQYKVGGLVYSENNDASAVKALTQAIFRPDVLSELIEKEPYLMVFALVSPGILMAMSNSGALEFGISKWISSDHSLVRMASILKTLASKVSVADTLALQKHIMRQNANFLCGELINGFQKKKSYTHATRFLLMISEENEMDDPVLNAGYRVLEASSHEIMEKNLSRTVRDILVRLKLVWKIQVNLVYAKALWKIQSRIVPKRADRLARTLQQLVAVSLPEYAQALEKQGESVSRKIFGKHFKCKTQDNMCSF | 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 that limits the accumulation of viral RNAs. May have RNA-binding activity (By similarity).
PTM: Potyviral RNA is expressed as two polyproteins which undergo post-translational proteolytic processing. Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases resulting in the production of at least ten individual proteins. P3N-PIPO is cleaved by P1 and HC-pro proteinases resulting in the production of three individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically (By similarity).
Catalytic Activity: Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.
Sequence Mass (Da): 109980
Sequence Length: 977
Domain: The N-terminus of helper component proteinase is involved in interaction with stylets. The central part is involved in interaction with virions and the C-terminus is involved in cell-to cell movement of the virus (By similarity).
Subcellular Location: Host cell junction
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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 barrier (Probable). Binds ssRNA (By similarity).
PTM: Phosphorylated.
Sequence Mass (Da): 19567
Sequence Length: 175
Domain: The N-terminus is involved in homodimerization (By similarity). The C-terminus binds ssRNA (By similarity). The C-terminus is phosphorylated (By similarity).
Subcellular Location: Host cell junction
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P0CK14 | MAAIMIGSISVPIVESARCATVQTGNRVNIVAPGHVAVCKPQMKSHSYYKHASEKLSKQASESINILNSFFDTDPEMRFRLTRNEMSKVKKGPNGRMILRKPRAQRVLERISFEKIEKGAERQVLPWRVYATVTSIINTFTDERNGIANSSLRSPFYKRSCRKEKKKIVCENVVRSASVNNLCDRVLKIAREKNIPVEMIGKKKNRHTLTFKNFKGSFIGKVSLAHERGQMRHVEMSYEQFGFILQAICRVTNTRCVRDEDIKPGCSGWVLGDDHELTQKFSRLPCLVIRGRDDEGIVNALEPVFFYDDVDHYSSQPEVQFFQGWRRMFDNFKPSSDHVCKVDHGNEECGELAAIFSQALFPVVKLSCQTCREKLSRVSFEEFKDSLAINFTVHKSEWDSLKENPHHDNVLKLIKGATQATQNLKLSSEVMKLVQNHTSTHMKQIQDINRALMKGSLVTQDELDLALKQLLEMTQWFKNHMHLTGEEALKTFRNKRSSKAMINPSLLCDNQLDKNGNFVWGERGYHSKRLFKNFFEEVIPSEGYTKYIVRNFPNGTRKLAIGSLIVPLNLDRARTALLGESIEKEPLTSACVSQQNGNYIHSCCCVTMDDGTPMYSDVKSPTKRHLVIGASGDPKYIDLPASEADRMYIAKEGYCYLNIFLAMLVNVNENEAKDFTKMIRDVLIPMLGQWPSLMDVATAAYILGVFHPETRCAELPRILVDHATQTMHVIDSYGSLTVGYHVLKAGTVNHLIQFASNDLQSEMKHYRVGGTPTQRIKLEEQLIKGIFKPKLMMQLLQDDPYVLILGMVSPTILVHMYRMRHFERGIEMWIKRDHEVGKIFVILEQLTRKVALTEVLVDQLDLISEASPHLLEIMKGCQDNQRAYVPALDLLTVQVEREFSNKELKVNGYPDLQQTLYDMREKNICKAIARFMARAKLAGKIMCNRAIEAILDFYGEKIDPASKRRKARIFAAICSRVLYHDPSTCKEHSRCRHAQI | 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 that limits the accumulation of viral RNAs. May have RNA-binding activity (By similarity).
PTM: Potyviral RNA is expressed as two polyproteins which undergo post-translational proteolytic processing. Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases resulting in the production of at least ten individual proteins. P3N-PIPO is cleaved by P1 and HC-pro proteinases resulting in the production of three individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically (By similarity).
Catalytic Activity: Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.
Sequence Mass (Da): 113760
Sequence Length: 996
Domain: The N-terminus of helper component proteinase is involved in interaction with stylets. The central part is involved in interaction with virions and the C-terminus is involved in cell-to cell movement of the virus (By similarity).
Subcellular Location: Host cell junction
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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 | MDSVNNLCRHYEEKVRPCIDLIDTLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLRKLKEGEEWRGKVSYDDIEVELSDPSEVEEAINKGQNFIAGVGLGISDKLISLDVSSPNVPDLTLIDLPGITRVAVGNQPADIGRQIKRLIKTYIQKQETINLVVVPSNVDIATTEALSMAQEVDPEGDRTIGVLTKPDLVDRGAEGKVLDVMRNLVYPLKKGYMIVKCRGQQDIQEQLSLTEAFQKEQVFFKDHSYFSILLEDGKATVPCLAERLTEELTSHICKSLPLLEDQINSSHQSASEELQKYGADIPEDDRTRMSFLVNKISAFNRNIMNLIQAQETVSEGDSRLFTKLRNEFLAWDDHIEEYFKKDSPEVQSKMKEFENQYRGRELPGFVDYKAFESIIKKRVKALEESAVNMLRRVTKMVQTAFVKILSNDFGDFLNLCCTAKSKIKEIRLNQEKEAENLIRLHFQMEQIVYCQDQVYKETLKTIREKEAEKEKTKALINPATFQNNSQFPQKGLTTTEMTQHLKAYYQECRRNIGRQIPLIIQYFILKTFGEEIEKMMLQLLQDTSKCSWFLEEQSDTREKKKFLKRRLLRLDEARQKLAKFSD | 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: Peripheral membrane protein
Sequence Mass (Da): 72038
Sequence Length: 631
Domain: The C-terminal GTPase effector domain (GED) is involved in oligomerization and viral target recognition.
Subcellular Location: Cytoplasm
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P79135 | MVHSDLGIEELDSPESSLNGSEDMESKSNLYSQYEEKVRPCIDLIDSLRSLGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLRLKKLGNEDEWKGKVSFLDKEIEIPDASQVEKEISEAQIAIAGEGTGISHELISLEVSSPHVPDLTLIDLPGITRVAVGNQPPDIEYQIKSLIRKYILRQETINLVVVPANVDIATTEALRMAQEVDPQGDRTIGILTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQDIKHRMSLDKALQRERIFFEDHAHFRDLLEEGKATIPCLAERLTSELIMHICKTLPLLENQIKETHQRITEELQKYGKDIPEEESEKMFCLIEKIDTFNKEIISTIEGEEFVEQYDSRLFTKVRAEFSKWSAVVEKNFEKGYEAIRKEIKQFENRYRGRELPGFVNYKTFETIIKKQVRVLEEPAVDMLHTVTDIIRNTFTDVSGKHFNEFFNLHRTAKSKIEDIRLEQENEAEKSIRLHFQMEQLVYCQDQVYRRALQQVREKEAEEEKNKKSNHYFQSQVSEPSTDEIFQHLTAYQQEVSTRISGHIPLIIQFFVLRTYGEQLKKSMLQLLQDKDQYDWLLKERTDTRDKRKFLKERLERLTRARQRLAKFPG | 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 protein
Sequence Mass (Da): 74805
Sequence Length: 648
Domain: The C-terminal GTPase effector domain (GED) is involved in oligomerization and viral target recognition.
Subcellular Location: Cytoplasm
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Q5ZMC2 | MTELEGPEFGKADFVLLDEVTMEHFMENLRLRFSKGRIYTYIGEVVVAMNPYQPLELYGPSVVEQYRGRELYERPPHLFALADAAYKAMKRRAKDTCIVISGESGAGKTEASKYIMQYIAAITNPTQRAEVERVKNGLLKSNCVLEAFGNAKTNRNDNSSRFGKYMDINFDFKGDPTGGHIYNYLLEKSRVLQQQPGERNFHSFYQLLLGAPDALLASLHLQRDPTAYCYTQQGTQGSAGGDDARGYRAVEEAMAVIGFTPEEVGAVQRILAAILHLGNVQFVAEGEVAALEAVEQLAVLAQLTGTTPEQLRQALLARTVATGGGELIEKGHSPTEAAYGRDACAKAIYERLFGWIVGRINASITARGYDVRQHGKSTVIGVLDIYGFEIFDTNSFEQFCINYCNEKLQQLFIELILRQEQAEYQREGITWQNIEYFSNEPIVELVEQPHRGILALLDEACLAVGTVTDALFLANMDARLGHHPHYSSRKLCPTDKTMEFDRDFRIKHYAGDVTYSVEGFLDKNKDTLFQDFKRLLYNSMDPVLRAMWPDGEQSITEVTKRPLTAATLFKNSIVALVENLASKEPYYVRCIKPNDQKSPVLFDEERCRHQVAYLGLLENVRVLRAGFAYRQPYDRFLQRYKMTCEYTWPNHLMATDREATQTLLEQHGFQDDVAYGHTKVFIRTPRTLFCLEQERAQLIPIIVLLLQKAWRGALARRWCRYLRAAYAIMGYYKRHKVKAYLLELIRRFQGVRSMPDFGKSLAWPEPPAVLSRFQENSQQLFRRWRARQIVKNIPPSDMAQIRAKVAAMGALHGLRKDWGCQRGWVRDYLSSASENPGLALPFAHRVQALRDKVHFGAVLFSSHVRKINRFNKSRDRAILITDQHLYKLEPRKQYRVMRELPLSMVTGLSVTSCRAQLVVFHTQNHDDLAVCLHKTQPRGDERVGELVGVLLEHCRTTKRELQVHVSDRIQLSLRGRKRLLTVETQPDVAAPDFRKSRDGFVLYWPGS | 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 tension, enforcing cell-intrinsic meandering search, thereby enhancing detection of rare antigens during lymph-node surveillance, enabling pathogen eradication.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 114970
Sequence Length: 1007
Subcellular Location: Cell membrane
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B0I1T2 | MEDEEGPEYGKPDFVLLDQVTMEDFMRNLQLRFEKGRIYTYIGEVLVSVNPYQELPLYGPEAIARYQGRELYERPPHLYAVANAAYKAMKHRSRDTCIVISGESGAGKTEASKHIMQYIAAVTNPSQRAEVERVKDVLLKSTCVLEAFGNARTNRNHNSSRFGKYMDINFDFKGDPIGGHIHSYLLEKSRVLKQHVGERNFHAFYQLLRGSEDKQLHELHLERNPAVYNFTHQGAGLNMTVHSALDSDEQSHQAVTEAMRVIGFSPEEVESVHRILAAILHLGNIEFVETEEGGLQKEGLAVAEEALVDHVAELTATPRDLVLRSLLARTVASGGRELIEKGHTAAEASYARDACAKAVYQRLFEWVVNRINSVMEPRGRDPRRDGKDTVIGVLDIYGFEVFPVNSFEQFCINYCNEKLQQLFIQLILKQEQEEYEREGITWQSVEYFNNATIVDLVERPHRGILAVLDEACSSAGTITDRIFLQTLDMHHRHHLHYTSRQLCPTDKTMEFGRDFRIKHYAGDVTYSVEGFIDKNRDFLFQDFKRLLYNSTDPTLRAMWPDGQQDITEVTKRPLTAGTLFKNSMVALVENLASKEPFYVRCIKPNEDKVAGKLDENHCRHQVAYLGLLENVRVRRAGFASRQPYSRFLLRYKMTCEYTWPNHLLGSDKAAVSALLEQHGLQGDVAFGHSKLFIRSPRTLVTLEQSRARLIPIIVLLLQKAWRGTLARWRCRRLRAIYTIMRWFRRHKVRAHLAELQRRFQAARQPPLYGRDLVWPLPPAVLQPFQDTCHALFCRWRARQLVKNIPPSDMPQIKAKVAAMGALQGLRQDWGCRRAWARDYLSSATDNPTASSLFAQRLKTLQDKDGFGAVLFSSHVRKVNRFHKIRNRALLLTDQHLYKLDPDRQYRVMRAVPLEAVTGLSVTSGGDQLVVLHARGQDDLVVCLHRSRPPLDNRVGELVGVLAAHCQGEGRTLEVRVSDCIPLSHRGVRRLISVEPRPEQPEPDFRCARGSFTLLWPSR | 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 tension, enforcing cell-intrinsic meandering search, thereby enhancing detection of rare antigens during lymph-node surveillance, enabling pathogen eradication. Also required in B-cells, where it regulates different membrane/cytoskeleton-dependent processes. Involved in Fc-gamma receptor (Fc-gamma-R) phagocytosis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 116442
Sequence Length: 1018
Domain: The myosin tail domain mediates binding to phosphatidylinositol-3,4-bisphosphate (PtdIns(3,4)P2), phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) and binds to membranous compartments. It is required for recruitment to Fc-gamma receptor (Fc-gamma-R) phagocytic cups.
Subcellular Location: Cell membrane
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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
|
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
|
Q86VE0 | MASAAAGEAEETTRLRKPRFSFEENQILIREVRAHYPQLYGAQSRRVSVAERRRVWDGIAAKINGITSWKRTGQEVQKRWNDFKRRTKEKLARVPHSTQGAGPAAEDAFSAEEETIFAILGPGVAAPGAGAGAEEPPAAPSSQPPPPSACPQRYVLSEDRREDRRADTSAHSKAGSSSPEPWARPSCTPQEGGCPRPKERESPPPSALQPVQLPRLALSPPPPAPPLPPPPPLAQVAPSPPSPPPPPRPPPTLSASDPSLDFLRAQQETANAIRELAGTLRQGLAKLSEALSALLPLLPGTPVDSLPPPLPPPPPPPPPPRPVLPPPAPKVEITPEPVSVVAAVVDGAVVAARGVIIAPRSEEGAPRPPPAPLPPHDSPPHKRRKGFPTRKRRGRWKSP | 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 Location: Nucleus
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P28991 | MGAIDSFCGDGILGEYLDYFILSVPLLLLLTRYVASGLVYVLTALFYSFVLAAYIWFVIVGRAFSTAYAFVLLAAFLLLVMRMIVGMMPRLRSIFNHRQLVVADFVDTPSGPVPIPRSTTQVVVRGNGYTAVGNKLVDGVKTITSAGRLFSKRTAATAYKLQ | Function: Major envelope protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17744
Sequence Length: 162
Subcellular Location: Virion membrane
|
Q04565 | MGGLDDFCNDPIAAQKLVLAFSITYTPIMIYALKVSRGRLLGLLHILIFLNCSFTFGYMTYVHFQSTNRVALTLGAVVALLWGVYSFTESWKFITSRCRLCCLGRRYILAPAHHVESAAGLHSISASGNRAYAVRKPGLTSVNGTLVPGLRSLVLGGKRAVKRGVVNLVKYGR | Function: Major envelope protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18925
Sequence Length: 173
Subcellular Location: Virion membrane
|
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: 248
EC: 3.1.1.91
|
Q9W4C5 | MELKGVQPSNGSSNGSGNGATNAASTEKTDAEKPTAERTNWGNGLEFLMSCISVSVGLGNVWRFPFTAYENGGGAFLIPYIIVLFLIGKPMYYLEMIMGQFTSQGTVKIWSVVPGFVGVGYGQAFGTICIISYYSSLLALTLYYLFVSFQSELPWSYCRDEWTNCVNSRPQEYVDNLLTGVSLANESARNLSGIVANDETEKLQSSSELYFLNVVIKEKLDISDGVGDPDWKLTLALFVAWVVIFLVIMRGVKSSGKAAYFLALFPYVVLFVLLIRAVTLEGARDGILFFLEPQWGELLNPTVWKEAVVQCFFSLAVGSGPIIMFASYNRFDHGIYRDAMIVTTLDTLTSLLGGITIFAILGNLAHNLQIENIRDVVRSGTGLAFISYPDAISKFQAVPQLFSVLFFFMLFVLGIGSIVALQSTIVTIICDQFKGWKYWKVALTTSVCGFLMGLVYVTPGGQWILTLVDFYGGTYVVFILAIFELAGIVWVYGLQNFCDDIEFMCNRRVSLYWRVCWSFFTPVMMIIIFIYSMVTIEPIKYSELYFPEAANIAGWLLFAIGAAQFPLWGLWYISRHPQGTYWKSLKASLKPSDRWGPANPEIRREWVIFKNQKAAQRATQKDTSKLGFFWRKVANFCGSNK | 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 Length: 641
Subcellular Location: Membrane
|
B4L7U0 | MELKTMPHNGANGSPQHNNNNNSNNNNNVSSDTKTDNNEKEAQKKDEGRTNWSNGIEFLMSCISVSVGLGNVWRFPFTAYENGGGAFLIPYIIVLFLIGKPMYYLEMIIGQFTSQGTVKIWSICPSFVGVGYGQAFATICIITYYSSLLALTLYYLFVSFQSELPWSYCRDEWTNCVNSIPTEFVETALGNTTSALAQQANTLSNTTKLQSSSELYFLNVVIKEKSDISDGIGIPDWKLTIALFVSWVVIFLVIMRGVKSSGKAAYFLALFPYVVLFALLGRAVTLEGAVDGIIFFLQPQWGELLNPIVWKEAVVQCFFSLAVGCGPIIMFASYNRFDHGIYRDAMIVTTLDTLTSLLGGITIFAILGNLAHNLKAENIRDVVRSGTGLAFISYPDAISKFQAVPQLFSVLFFFMLFVLGIGSIVALQSTIVTIICDQFKSWKYWKVALATSACGFLMGLVYVTPGGQWILTLVDFYGGTYVVFILAIFELSGIVWIYGLQNFCDDIEFMSNKNVSMYWRLCWSFFTPVMMIVIFIYSMATIQPIKYSDQYFPLAGDVAGWLLFAVGAAQFPLWGWWYIATHRHGSCAESIKASLKPSSKWGPASPENRQAWLLFKSDLAAKRANEAKSNKFGFFQQKLRNMCGK | 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): 71994
Sequence Length: 645
Subcellular Location: Membrane
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A0A0P0VI36 | MHASCCCAPPESVSHTRRISYKYSGTSYPTRTTTTSSSAPEFTNKKQSTAMAPTTAAAAASSNGGGESDGSSKEWRLTAPTRGGAMAAAGDKMSIRAVRYKISASVDDRGPRPVLPLAHGDPSVFPEFRTAAEAEDAVADALRSGDFNCYPAGVGLPAARRAVADHLSRDLPYKLSSDDIFLTAGGTQAIEVVISILAQPGTNILLPRPGYPNYEARAAFNNLEVRHFDLIPEKGWEIDLNSLESIADKNTTAIVIINPNNPCGNVYTYEHLSKVAEVARKLGILVITDEVYGNLVFGSSPFVPMGCFGHIVPILTIGSLSKRWIVPGWRLGWVAICDPKKTLQETKIATLITNFLNVSTDPATFIQGALPNILKNTKEEFFKRIIDLLTETSDICYRGIKDIKCITCPHKPEGSMFVMVKLNLYLLEGIHDDVDFCCQLAKEESVILCPGSVLGMKNWVRITFAIDSSSLLDGLERIKSFCQRHKKKNPLNYI | 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
EC: 2.6.1.80
|
Q13506 | MAAALPRTLGELQLYRILQKANLLSYFDAFIQQGGDDVQQLCEAGEEEFLEIMALVGMASKPLHVRRLQKALRDWVTNPGLFNQPLTSLPVSSIPIYKLPEGSPTWLGISCSSYERSSNAREPHLKIPKCAATTCVQSLGQGKSDVVGSLALQSVGESRLWQGHHATESEHSLSPADLGSPASPKESSEALDAAAALSVAECVERMAPTLPKSDLNEVKELLKTNKKLAKMIGHIFEMNDDDPHKEEEIRKYSAIYGRFDSKRKDGKHLTLHELTVNEAAAQLCVKDNALLTRRDELFALARQISREVTYKYTYRTTKSKCGERDELSPKRIKVEDGFPDFQDSVQTLFQQARAKSEELAALSSQQPEKVMAKQMEFLCNQAGYERLQHAERRLSAGLYRQSSEEHSPNGLTSDNSDGQGERPLNLRMPNLQNRQPHHFVVDGELSRLYPSEAKSHSSESLGILKDYPHSAFTLEKKVIKTEPEDSR | 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 | MATALPRTLGELQLYRILQKANLLSYFDAFIQQGGDDVQQLCEAGEEEFLEIMALVGMASKPLHVRRLQKALRDWVTNPGLFNQPLTSLPVSSIPIYKLPEGSPTWLGISCNSYERSSSSREPHLKIPKCAATTCVQSLGQGKSEVGSLALQSVSDSRLWQGHHATESEHSLSPADLGSPASPKESSEALDAAAALSVAECVERMAPTLPKSDLSEVKELLKNNKKLAKMIGHIFEMSDEDPHKEEEIRKYSAIYGRFDSKRKDGKHLTLHELTVNEAAAQLCVKDNALLTRRDELFALARQVSREVTYKYTYRTTRLKCGERDELSPKRIKIEDGFPDFQESVPTLFQQARAKSEELAGLGSQQAEKGMAKQMELLCAQAGYERLQQERRLTAGLYRQSSGEQSPDGGLPSDSSDGQGERPLNLRIPSVQNRQPHHFVVDGELSRLYSSEAKSHSSESLGILKDYPHSAFTLEKKVIKTEPEDSR | 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 | MHRAPSPTAEQPPGGGDSARRTLQPRLKPSARAMALPRTLGELQLYRVLQRANLLSYYETFIQQGGDDVQQLCEAGEEEFLEIMALVGMATKPLHVRRLQKALREWATNPGLFSQPVPAVPVSSIPLFKISETAGTRKGSMSNGHGSPGEKAGSARSFSPKSPLELGEKLSPLPGGPGAGDPRIWPGRSTPESDVGAGGEEEAGSPPFSPPAGGGVPEGTGAGGLAAGGTGGGPDRLEPEMVRMVVESVERIFRSFPRGDAGEVTSLLKLNKKLARSVGHIFEMDDNDSQKEEEIRKYSIIYGRFDSKRREGKQLSLHELTINEAAAQFCMRDNTLLLRRVELFSLSRQVARESTYLSSLKGSRLHPEELGGPPLKKLKQEVGEQSHPEIQQPPPGPESYVPPYRPSLEEDSASLSGESLDGHLQAVGSCPRLTPPPADLPLALPAHGLWSRHILQQTLMDEGLRLARLVSHDRVGRLSPCVPAKPPLAEFEEGLLDRCPAPGPHPALVEGRRSSVKVEAEASRQ | 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) interacts with EGR1 inhibitory domain and mediates multimerization.
Subcellular Location: Nucleus
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Q9LKG8 | MKEDMEVLSLASLPVGFRFSPTDEELVRYYLRLKINGHDNDVRVIREIDICKWEPWDLPDFSVVKTTDSEWLFFCPLDRKYPSGSRMNRATVAGYWKATGKDRKIKSGKTKIIGVKRTLVFYTGRAPKGTRTCWIMHEYRATEKDLDGTKSGQNPFVVCKLFKKQDIVNGAAEPEESKSCEVEPAVSSPTVVDEVEMSEVSPVFPKTEETNPCDVAESSLVIPSECRSGYSVPEVTTTGLDDIDWLSFMEFDSPKLFSPLHSQVQSELGSSFNGLQSESSELFKNHNEDYIQTQYGTNDADEYMSKFLDSFLDIPYEPEQIPYEPQNLSSCNKINDESKRGIKIRARRAQAPGCAEQFVMQGDASRRLRLQVNLNSHKSETDSTQLQFIKKEVKDTTTETMTKGCGNFTRSKSRTSFIFKKIAAMGCSYRGLFRVGVVAVVCVMSVCSLVA | 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 similarity).
PTM: Phosphorylated at Thr-142. Phosphorylation at Thr-142 is required for nuclear import.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 50891
Sequence Length: 451
Domain: The NAC domain includes a DNA binding domain and a dimerization domain.
Subcellular Location: Nucleus
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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 that may involve cross-talk with salt- and H(2)O(2)-dependent signaling pathways . Regulates also genes during seed germination . Regulates positively aging-induced cell death . Involved in age-related resistance (ARR) against Pseudomonas syringae pv. tomato and Hyaloperonospora arabidopsidis . Antagonizes GLK1 and GLK2 transcriptional activity, shifting the balance from chloroplast maintenance towards deterioration during leaf senescence . Promotes the expression of senescence-associated genes, including ENDO1/BFN1, SWEET15/SAG29 and SINA1/At3g13672, during senescence onset .
PTM: Ubiquitinated by NLA. Ubiquitination of NAC92 leads to its degradation by the proteasome during leaf senescence under nitrogen deficiency.
Sequence Mass (Da): 32984
Sequence Length: 285
Domain: The NAC domain includes a DNA binding domain and a dimerization domain.
Subcellular Location: Nucleus
|
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 closure and water loss under dehydration stress conditions. Acts synergistically with ABF2 to activate the dehydration stress-response factor RD29A transcription. Binds to the consensus core cis-acting elements 5'-CGTA-3' and 5'-CACG-3' at the RD29A promoter . Involved in hypocotyl graft union formation. Required for the auxin-mediated promotion of vascular tissue proliferation during hypocotyl graft attachment .
Sequence Mass (Da): 33580
Sequence Length: 292
Domain: The NAC domain includes a DNA binding domain and a dimerization domain.
Subcellular Location: Nucleus
|
O04017 | MDIPYYHYDHGGDSQYLPPGFRFHPTDEELITHYLLRKVLDGCFSSRAIAEVDLNKCEPWQLPGRAKMGEKEWYFFSLRDRKYPTGLRTNRATEAGYWKATGKDREIFSSKTCALVGMKKTLVFYKGRAPKGEKSNWVMHEYRLEGKFSYHFISRSSKDEWVISRVFQKTTLASTGAVSEGGGGGGATVSVSSGTGPSKKTKVPSTISRNYQEQPSSPSSVSLPPLLDPTTTLGYTDSSCSYDSRSTNTTVTASAITEHVSCFSTVPTTTTALGLDVNSFSRLPPPLGFDFDPFPRFVSRNVSTQSNFRSFQENFNQFPYFGSSSASTMTSAVNLPSFQGGGGVSGMNYWLPATAEENESKVGVLHAGLDCIWNY | 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. Controls leaf margin development and required for leaf serration. Involved in axillary meristem initiation and separation of the meristem from the main stem. Regulates the phyllotaxy throughout the plant development. Seems to act as an inhibitor of cell division.
Sequence Mass (Da): 41434
Sequence Length: 375
Domain: The NAC domain includes a DNA-binding domain and a dimerization domain, and confers the specificity of the transactivated target genes.
Subcellular Location: Nucleus
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B2VBT3 | MSLMFDVDAAVYPFPAKPIRLSSDEKLAYRTKIKRLLQERDAVMVAHYYTDPDIQALAEETGGCVADSLEMARFGSQHSAATLLVAGVRFMGETAKILSPEKTILMPTLQAECSLDLGCPIDEFSRFCDAHPDRTVVVYANTSAAVKARADWVVTSSIAVELIEHLDSLGEKIIWAPDRHLGQYVQRQTSADILCWQSACIVHDEFKTQALQRMKLLYPEAAVLVHPESPQAIVDLADAVGSTSQLIQAAQTLPHRQMIVATDRGIFYKMQQACPDKELLEAPTAGEGATCRSCAHCPWMAMNGLKAIADGLEQGGSEHEILINDALREGALIPLNRMLTFAKDLKLKVRGNA | 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: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.72
|
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: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.72
|
Q5KWQ2 | MNVLEQLKRLDEMPKRYKTMERSELEARARAVKERFGRRLFIPGHHYQKDEVIQFADATGDSLQLAQLAAKNSEAEYIVFCGVHFMAETADILTSDDQTVILPDLRAGCSMADMADIFQVERAWAALIERFGETIVPLVYVNSTAAIKAFVGRHGGATVTSSNAKKMMAWAFSRNERIFFLPDQHLGRNTAYALGIRLDEMAVWDPHEETLQGADDLDKVKVILWKGHCSVHENFTVRQIEHIRRMKPGIHVIVHPECSWEVVQQADYAGSTKYIIETIRNAPPGTQWAIGTEMNLVNRLKHEHPDKEIVSLNPYMCPCLTMNRIDLPHFVWALESLEQGAIVNRITVPKDIAAEAKEALDRMLSLA | 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: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.72
|
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: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.72
|
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