ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q2GH90 | MYKQSWELLGNGQHADLTVAYINARIIDPESKLDIRGSLLTKGDKIIDFGPDLFANGIPSTIDEVIDCNNNILLPGLIDIHVHFREPGQEHKETINTGSKSAAAGGITTVVCQPNTIPTISSVITAKYIKMRALESAYVNIEFYASITKSDNSLSDMALLKEVGAVGFTDDGMPVMNALTMRQALSYSSMLDTVIAQHAEDLNISNNGCINEGIISYELGLKGIPDISESIIVNRDIALMKNIKNVHYHILHVSSQESLHIIKQAKSQGLKVTCEVTPHHFTLTERDIMTHGSLAKMNPPLRTENDRLSMIEGLKSGIID... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 49167
Sequence Length: 447
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pa... |
B2KCN5 | MKYLIKNAHVIDPANKIDGLKDILIENGKIAAVENKIEDNAAKIIDAKGLTAMPGFVDMHTHLREPGQEGKETIFTGTKAALKGGFTTVCMMPNTNPAMDSKNNLAIAQDIIRKTANVNVEIMGAITKNRAGKELSNFAELKQAGAIALSDDGSGVEDDAVMQAAFKESVKQDILLISHSEDSKLSAGGVMNEGLISTKLGLKPISNASEYEMVKREIQLAKGLDAKIHIAHVSTKESCEIIAKAKKQGVMVTAEATPHHFTLTDKACESFSGNTKMNPPLRSEADVEALKQALKDGTIDAIATDHAPHAVHEKEVEFDL... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 46430
Sequence Length: 432
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pa... |
Q74DP4 | MNLLIKGGRVIDPSQGIDEVLDILVENGAIKELGKGLAAPAGAGVVDAAGLIVTPGLIDMHVHLRDPGLEYKEDIVTGTRAAAAGGFTSVACMPNTKPVNDNKAVTSYIVAKAKAEGLVNVFPVGSITQGSKGDALAEMGDLKEAGCVAVSDDGRPVTSSELMRRALEYAKGMGIMVISHAEDLSLVGEGVMNEGFVSTELGLKGIPWAAEDAATARDVYLAEFTNSPLHIAHVSTMGSLRIIRNAKARGVKVTCETAPHYFSLTDDAVRGYNTNAKMNPPLRTADDLAAVKEALKDGTIDAIATDHAPHHLDEKDVEFN... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 44258
Sequence Length: 425
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pa... |
Q9KXR3 | MSKTLIRGAKVLGGEPQDVLIDGTVVEAVGTNLSAEGAEVVEADGKVLLPGLVDLHTHLREPGREDSETVLTGTRAAASGGYTNVFAMANTFPVADTAGVVEQVWRLGQESGYCDVQPIGAVTVGLEGAKLAELGAMHESAAGVTVFSDDGKCVHDAVIMRRALEYVKAFNGVVAQHAQEPRLTEGAQMNEGVVSAELGLGGWPAVAEESVIARDVLLAEHVGSRVHICHLSTAGSVEIVRWAKSRGIDVTAEVTPHHLLLTDELVRSYNPVYKVNPPLRTERDVMALREALADGTIDIVATDHAPHPHEDKDCEWAAAA... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 45271
Sequence Length: 428
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pa... |
Q8DPQ5 | MLLIKNGRVMDPKSGLDQVCDVLVQDGKIIKIAPEITEEGAETIDATGHVVAPGLVDIHVHFREPGQTHKEDIHTGALAAAAGGFTTVVMMANTSPTISDVETLQAVLQSAAKEKINVKTVATITKNFNGKNLTDFKALLEAGAVGFSDDGIPLESSKIVKEAMEEAKKLNTFISLHEEDPGLNGVLGFNENIAREHFHICGATGVAEYAMMARDVMIAYATKAHVHIQHLSKEESVKVVEFAQGLGAEVTAEVAPQHFSKTEALLLTQGSNAKMNPPLRLESDRRAVIEGLKSGVITVIATDHAPHHVDEKNVEDITKA... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 45325
Sequence Length: 422
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pa... |
O08357 | MWIKGKAYYEGEIKEICINFDRSIKEIRANCKPDMTFTNEELILPASVDLHVHVRGAQLSYKETVATATSEAVYGGVGVIVDMPNTVPYINTPERIKERLREFQLYSRTDYGIYSGVSKEVEEIDKLPIAGYKIYPEDLEKEETRYVLEKSKKLKILHPEMPFVSKIERSLRRSYWMETAAINLVKGNMHITHITNFETLQLAKSMGFTTDITAHHLVVDGERDCISKVNPPIRDYVTRLKLFLKGLFEVDCIASDHAPHSKEEKRMNFDLCPPGIAGVSFSTPYIYSLMFKGLISIDRAVSLLSGNPSRILNIPTGKIK... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 44248
Sequence Length: 389
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pa... |
B2V5I6 | MILIKNGHIVDPQNNLNDKFDILIEKGEIKKIEKNIQPFAGCEVIDAEGKIITPSFTDIHVHFRDPGQTYKEDIESGSKAAVAGGYTTVVCMPNTIPAIDDVPIVRYIIEKGEEIGLCRVLPSAAITKGRKGKELTEMALLKDAGAVYFTDDGAPVMDSFIMRKAMEYAGSLGTFVADHCEDLNLSQNGVAHEGEIAAALGLPPLPPEAEDTMVARDCILSIQTGMPVHICHISTKLSVEIVAWAKAMGAKVTAEVTPHHLYLTDEEFLDFSCIAKVSPPLRTHEDIEATRWALASGIIDFVATDHAPHAHYEKMQELQA... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 46638
Sequence Length: 423
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pa... |
Q2LVI3 | MKILLKGGRVIDPAQNLDGQMDLLLENGKIAAIAEAVGSVPEDTRLLDLKGMILLPGLVDMHTHLREPGYEYKETIRSGSEAAAVGGFTSIACMPNTLPVNDNRTVTEYILKRAKECDTVHVYPVAAVSRNSEGKILAEFGDLKEAGAIAFSDDGKPVMNSILMRRALEYASSLDRIIISHCEDLNLSAGGLMNEGKISTELGLPGIPTLAEDVMVARDLLLAEFSGAALHIAHVSSAGAVRMIRDAKKRGVRVTAETTPHYFTLTDEAVTNFNTNTKVSPPLRSREDLQAVREGLRDGTLDAIVTDHAPHALTDKEVEF... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 46033
Sequence Length: 426
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pa... |
A0LK22 | MKKGKADPCNYLFRRARVIDPARDLDAVADVLVVDGILTDIKPNIDLPSDRLAHFAVIDASEKWIVPGLIDMHVHLREPGEEYKETIATGTMAAVAGGYTAVACMPNTKPVNDCAAVTEYILERAREQGHCRVLPVGAVSSGLEGRSLAEFGELKGSGAVAVTDDGRPVANSMLMRRALEYAKNFDLPVISHAEDPALSEGGLMNEGPTSTLLGLHGIPKAAEEVMVARDLALAELTGARLHIAHVSTAGAVRMIGEAKSRGVPVTAETAPHYFTLTDDRLMTFDTLYKVNPPIRGPADVEAIKRGLADGTIDAVATDHA... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 47298
Sequence Length: 439
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pa... |
A9BJH4 | MIDTKVNIAGVEFKNPVIAASGTFGFGREFLEYFPISKLGGLATKGLTLREREGNKGVRIHETIGGIMNSIGLQNPGIDAFIEEELPFLNSQDTVIIANVSGNTIDEYVISVEKLNQTDIDMIELNISCPNVKEGGISFGTKAEIASNVVTQVRKVCQKPLIVKLSPSAENIVEMAESCVEAGADALSLVNTFPALAIDISKKKAIFDNITAGLSGPCIKPIALRMVYEVSKAVDVPIIGIGGIMDYRDAIEYIMAGAWAVQVGTANFINPNACAEIIEGIEEYLQKEGISTLEEIRGII | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 32196
Sequence Length: 300
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway... |
A6L5H1 | MADLSVNIGDLKLCNPVMTASGTFGYGKEFEDFVDLEKIGGIIVKGTTLHHREGNPYPRMAETPMGMLNAVGLQNKGVDYFVEHIYPQIRDIHTNMIVNVSGSAVEDYVKTAEIINDLDHIPAIELNISCPNVKQGGMAFGVSACGCSEVVKAVRNVYKKTLIVKLSPNVTDITEIARAAEASGADSVSLINTLLGMAVDAEKRRPVLSTITGGMSGAAVKPIALRMVWQVAKAVNIPVIGLGGIMGWKDAVEFMLAGATAIQIGTANFIDPAITVKVSEGINDYLERHGYTSVKDIIGALEV | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 32303
Sequence Length: 303
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway... |
Q7MVJ6 | MVRTEVEIGRGLTIKNPVMTASGTYGYGTEYKDFIDIDRLGAIVVKGTTLHHREGNAYPRMAETPSGMLNAVGLQNKGVHYFVEHIYPVIKDYRTEMIVNVSGSTLDDYAETSRIINELEHIRAIELNISCPNVKQGGMAYGVTCEGAASVVKAVRRAYDKTLIVKLSPNVTDITEIARAVESEGADAISMVNTFLGMAIDAEKRRPILSTTTGGLSGPCIKPIALRMVWQTAKVVQVPIIGMGGIASAADAIEFLLAGATAVQVGCYNFVDPAAASYIVDGIEDYLRRHGISDVKELIGSLVIEHN | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 33120
Sequence Length: 307
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway... |
Q9V0Y6 | MLEVNLFGIKFKNPLILASGVVDMTPELLRRAHREGAGGVVTKSIGMEPRKGYENPTIVELPYGLINAMGLPNPGWEAFLEEFRKEKFDFPVIVSIFGGTPEEFAFLAEKLGEVADAFELNLSCPHAKGYGMEIGQKPENVYEVVKAVKDVTDKPVIAKLTPNVSDIRELGLAAEKAGADGVSAINTVKAIAIDIYAKRPILSNKFGGYSGPGVKPIALRAVYDLASSLDIPVIGIGGITTWQDAVEFLLAGASALQIGTAVYLRGFSVFREIAEGISRYLKEEGYSSVKEIIGLALKV | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 32175
Sequence Length: 299
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway... |
Q8DQ37 | MTTNRLQVSLPGLDLKNPIIPASGCFGFGQEYAKYYDLNLLGSIMIKATTLEPRFGNPTPRVAETPAGMLNAIGLQNPGLEVVLAEKLPWLEREYPNLPIIANVAGFSKQEYAAVSHGISKATNVKAIELNISCPNVDHCNHGLLIGQDPDLAYDVVKAAVEASEVPVYVKLTPSVTDIVTVAKAAEDAGASGLTMINTLVGMRFDLKTRKPILANGTGGMSGPAVFPVALKLIRQVAQTTDLPIIGMGGVDSTEAALEMYLAGASAIGVGTANFTNPYACPDIIENLPKVMDKYGISSLEELRQEVKESLR | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 33167
Sequence Length: 312
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway... |
O08358 | MIQVAGVNFEDPIVIASGIVPPTKEYMQNVCEKYEPSAITSKTLTYSPLEPHRSPTFVKISDNCYLNAIGLGNPGIQILRDLGEIKCKLIISIGGSNVNEYIDAVSKINDIPVMIELNVSSPNRRGFGESNLTYVEEIVKNVKSIVKKPVFVKLGPWDNIVEIAGRALSAGADGLTLINTLKGMLIDVEDFKPILSYGTGGISGKCIHALAVRVIHDVFKEYEPEIIGVGGVFDWRDAIELISVGAKLVGLGTVLVEKGFDVIREIREGIGTYLEEKGLKVEEIRGIGVKR | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 31667
Sequence Length: 291
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway... |
Q0AXG6 | MDLTVNLGGIKLKNPVAVASGTFGYGLEYADFIEPEKIGAVIVKGTTLHPRPGNPGPRIYETPAGMLNAIGLENPGIEVFLREYLPRLRERQVTVIANIAGNSIEEYALMASLLQGQEGIAGIELNISCPNVKQGGIQFGTDPETVRQVVAAVKKETSLPVIPKLSPNVTDIVAIALAAADGGADALSMINTLGGMAININLKKPVLGNIFGGLSGPAIKPVALKMIYQVYREVDLPILGGGGIVNHIDALEFFMAGATAVSIGTGNFVNPCLALELLEGIKKYMQEQGFSSIQELVGIAHA | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 31726
Sequence Length: 302
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway... |
Q9HL35 | MADLSTSVAGIRLENPLMLASGILDENGYTMLDVMNNGAAAVVTKSIGMEERNGYSAPVIVEYGDSLINAVGLSNPGIDNFAEEIRIAKRSGKPVIGSVFASDAESFVNLGRKMQEYGCDAVELNLSCPHVKGFGLEVGSDPDLVEDIVNEMKSKISVPVFAKLSPNVSDIIEIAKAAEKADAYVLINTVKAMKIDIRARMPVLTNAYGGLSGPAIKPVGVRYVYEVKKETGKDIIGVGGITTYEDAVEYIMAGASAVQIGTALYTVGKSVFRNIISQMNTFMDDEKFHSIQDMVGVAIR | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 32057
Sequence Length: 300
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway... |
Q9WYG8 | MLELKPPLVLLSGPAGFGEYLKLMDHRYVGGVLLKTVTLHPKEGNPTPRMADSDFYVINRIGLENPGIHAFVENIPELPVPMIASLGGDSFEEYLEVARVFKKVADRFYAVEFNFSCPNVKEGGLSIVKNAEEWKKLLNTLRKELPDSFLIAKVGVEGIFVEDAAEFVMKTGWDGITLVNTVRGLHFEKDTMILGGLSGPVLKPIALRAVYEVKKRFPELFVIASGGVYSVKDAEEFLKVGADVIGVGSALFKDPGVVEEIGKYLLEVKR | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 29742
Sequence Length: 270
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway... |
B0KA32 | MNLQVEVGGLKLKNPVMTASGTFGFGREYGEYIDLNQLGAIVVKGLTVNPKEGNPPPRVYETPCGMLNSVGLQNPGINAFIEKELPFLRDYDVAVIVNIAGETIEEFAYMAKKLDIDGVDGIEINVSCPNVKKGGMAFGINPEDIFNITKEVKKVTQKTVIVKLTPNVGDIGVCAKAAEDGGADAVSLINTIAGMAINIDTRTPVFKNVIAGLSGPAIKPIALRMVYEAARAVKIPVIGMGGISSFKDALEFMIAGAKAVAIGTCNFVNPNCTIEVIEGIKQYMVLNNIEDINEIIGSLKVD | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 32119
Sequence Length: 302
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway... |
Q2SCG9 | MSYQLARQFLFRLPAEASHNISLKMLKMADNAGMLGMFMPQMYSRPVELMGITFPNAVGLAAGLDKNGDYIDGLSKLGFGFIEVGTVTPKPQDGNPPPRLFRLEERSAIINRMGFNNYGVDYMTERLRKKKYGGVIGVNVGKNKDTPAEEAASDYIACINKVYPYASYITINISSPNTPGLRALQFGDSLRSMLQEIKDCQERMNQQHGRYVPFVVKIAPDMSDDEVHMVARTLLDYNMDGAIATNTTLSREGVESLAHGKEQGGLSGAPLTKRSTHVVKELCVALEGRIPVIASGGVMSAQDAVDKVRAGAKLVQVYSG... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37114
Sequence Length: 341
Pathway: Pyrimidine ... |
A1WTJ3 | MYALIRQLLFRLEPEQAHRVSMQLARLGLRIAAVPGVRSLPAVPRRVMGIDFPNPVGLAAGFDKDGEYMDVLEQLGFGFLELGTVTPRAQPGNPQPRVFRIPEHEALINRMGFNNQGAEPLVRRLEVSRHRGVVGINIGKNRDTPPERAVEDYAQALGMVYGVADYVAVNLSSPNTPGLRDLQHEGALRNLIDRLQTERKRLAELHDKRVPLVVKIAPDWEAGELDATLDILLERRVDGIVATNTTLGRTGVEQTPQARESGGLSGAPLREQAEWVLEQVAARRDRRTALIAAGGIMSGEDVTRRLDLGADLVQLYTGMI... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37518
Sequence Length: 342
Pathway: Pyrimidine ... |
Q5UYF1 | MRPYDIAKPFLFSLPAETANKSVHRLLETVDGTRVADVMADRYTVADERLAVEAFGHTFDNPVGVAAGFDKNATIPETLASLGFGFAEVGGVTAEPQAGNARPRMFRLKADEAIINRMGLNNDGAIVIGERLKNVDAPFPVGVNIAKTEHVGTNEAPDDYRTTYEHVAEGGDFFVVNVSCPNSEGFEELQNRDAMEAILSELQDAGAAPLLVKLSPDLPEPAVEDALDLVTELDLDGVVATNTTTERPASLRSPNAVETGGLSGKPIENQATEMVRFVAERVDVPVVGVGGVSTAEGAYRKIRAGASLVQLYTGLVYRGP... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37214
Sequence Length: 350
Pathway: Pyrimidine ... |
Q17WU9 | MLYSLFKKYLFRLDAEEVHEKVCKILKILSRSPFFCNLIHAQFGYTNPKLENEILGLHFPNPLGLAAGFDKNASMIRALTAFGFGYLEAGTLTNTAQSGNEKPRLFRHIEEESLQNAMGFNNYGAVLGVRAFERFAPYKTPIGINLGKNKHIEQDNALEDYKAVLIKCLNIGDYYTFNLSSPNTPNLRDLQNKAFVSELFCMAKEMTKKPLFLKIAPDLEIDAMLEITNSAIEAGANGIIATNTTIDKSLVFAPKETGGLSGKCLTQKSREIFKELAKAFFNKTILVSVGGISDAKEAYERIKMGASLLQIYSAFIYNGP... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39064
Sequence Length: 351
Pathway: Pyrimidine ... |
O25655 | MLYSLVKKYLFSLDAEDAHEKVCKILRMLSSSPFLCNLIDSQWGYQNPKLENEILGLHFPNPLGLAAGFDKNASMLRALMAFGFGYLEAGTLTNEAQVGNERPRLFRHIEEESLQNAMGFNNYGAILGVRSFKRFAPYKTPIGINLGKNKHIEQAHALEDYKAVLSKCLNIGDYYTFNLSSPNTPNLRDLQNKAFVHELFCMAKEMTHKPLFLKIAPDLETDDMLEIVNSAIGAGAHGIIATNTTIDKSLVFAPKEMGGLSGKCLTKKSREIFKELAKAFFNKSVLVSVGGISDAKEAYERIKMGASLLQIYSAFIYNGP... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39002
Sequence Length: 351
Pathway: Pyrimidine ... |
Q02127 | MAWRHLKKRAQDAVIILGGGGLLFASYLMATGDERFYAEHLMPTLQGLLDPESAHRLAVRFTSLGLLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVNLGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQERDGLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGALRSETGGLSGKPLRDLSTQTIREMY... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. Required for UMP biosynthesis via de novo pathway.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
PTM: The uncleaved transit peptide is required for mitochondria... |
Q5SK69 | MHRFLFALDPEAAHGLALGLLALWSERGPLLEVPARLLRVEDPRLRVEAFGVSFPNPLGLAAGMDKDARALGAWWALGFGFAEVGTLTPRPQVGNPKPRLFRLVEDRALINRMGFNNRGAEEAARRLKRSRQRGLPLPIGVNLGKNRDTPLGRAAEDYLKALRLLEPFGDYFVLNVSSPNTPGLRALQEGPFLDELLARLRPATKKPLLLKVAPDLSPKALDEVLALAKKHRLQGLVAVNTTLAREGLKSPWAKEAGGLSGRPLKGRALEVLRHLAEGAEGLALVSVGGVETPLDLWERLKAGASLVQVYTGFVYGGPLF... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37662
Sequence Length: 346
Pathway: Pyrimidine ... |
Q4D3W2 | MMCLKLNLLDHVFANPFMNAAGVLCSTEEDLRCMTASSSGALVSKSCTSAPRDGNPEPRYMAFPLGSINSMGLPNLGFDFYLKYASDLHDYSKKPLFLSISGLSVEENVAMVRRLAPVAQEKGVLLELNLSCPNVPGKPQVAYDFEAMRTYLQQVSLAYGLPFGVKMPPYFDIAHFDTAAAVLNEFPLVKFVTCVNSVGNGLVIDAESESVVIKPKQGFGGLGGKYILPTALANVNAFYRRCPDKLVFGCGGVYSGEDAFLHILAGASMVQVGTALQEEGPGIFTRLEDELLEIMARKGYRTLEEFRGRVKTIE | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor. Molecular oxygen can replace fumarate in vitro.
Catalytic Activity: (S)-dihydroorotate + fumarate = orotate + succinate
Sequence Mass (Da): 34167
Sequence Length: 314
Pathway: Pyrim... |
A1WJ81 | MPLLPYALTRPFLFGLDAEAAHELIIDLLARGQRTPLQWAWCNQTVDDPIELAGLRFPNRVGLAAGLDKNARCIDALGAMGFGFVEAGTVTPQAQPGNPRPRMFRLPEARALINRLGFNNAGLQAFVHNLQQSRLRAAGSALRLGLNIGKNASTPMAQASSDYLACLEGVYPHADYVALNISSPNTQNLRTLQGDAALDHLLGAIAERRATLAARHGRRVPVFVKIAPDLDEAQLSLMAATLQRHGIDGVIATNTTIDRAVVQGQRHAQESGGLSGAPVLQASNQVIGQLRAALGKGFPIIGVGGIMSAEDAVSKIRAGA... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38028
Sequence Length: 360
Pathway: Pyrimidine ... |
Q8D370 | MIYKIINFILSKKDHEEKKDLLLKIMKFFNKTPLNFLIKNKFPNNNISCMGLNFKNILGLAAGLDKNGDYIKLFSDIGFGFIELGTVTLKPQHGEKKPRLFCFPNVYGIINRMGFNNNGIENLIENIKNEKNVKSILGINIGKNKDTLIEKAKDDYLICINKAYYYSDYISINISSPNTKDLRKLQFGELFSDLLKSIKEEQNKLNKIYNKYVPILIKISPDINNSEIIQISDCLLSYNIDGVIATNTTVNKDIIMRCCNNCEKGGLSGAPLNENSTRIIKKLSKELKGKIPIIGSGGIISVKSAKEKIKAGASLIQIYS... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37951
Sequence Length: 337
Pathway: Pyrimidine ... |
P58856 | MKWGINMLNREIINALLDIKAVELRVDKENWFTWASGIKSPIYCDNRLTMSYPKIRKQIAEGFVKKINELYPNVDYIVGTATAGIPHAAWISDIMDLPMLYVRGSAKDHGKTNQIEGKFEKGKKVVVIEDLISTGKSSVLAAQALQEEGLEVLGVIAIFSYNLNKAKEKFDEAKIPFSTLTNYDVLLELAKETGLIGDKENQILIDWRNNL | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 23776
Sequence Length: 2... |
A9GUD3 | MSAAGASERERLVALLRERSFEQKRVVLASGRESDFFIDCKQSVLTAEGHALVGSLMFEALGALPRCEAVAGVELGGCPLASAVSLTSFLRGRPLPALYVRKEVKDHGSRRLVEGDRGLVPGMPVAILEDVITTGGSTLKAVEKLRTAGASVVGVIALVDRLEGGAEAIRAAGLPVVAICTRRDFIPDNPPG | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 20144
Sequence Length: 1... |
Q1GTA2 | MTDDQILAEFRAADALLQGHFLLSSGRHSEYYLQCARVLMDTERAGRLAAALAAKLPRELKQAIDLVVSPAMGGVIIGHEMGRALGKPAIFVERPTGTFELRRGFTIDPGAKVLMVEDVVTTGLSSREAMEAVRAAGGEVVAEAALVDRSAGSNIDLGVPFYPLVAINFPTYAADELPPELAGTEAIKPGSRSVAA | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 20719
Sequence Length: 1... |
P65916 | MAKEIAKSLLDIEAVTLSPNDLYTWSSGIKSPIYCDNRVTLGYPLVRGAIRDGLINLIKEHFPEVEVISGTATAGIPHAAFIAEKLKLPMNYVRSSNKSHGKQNQIEGAKSEGKKVVVIEDLISTGGSSVTAVEALKQAGAEVLGVVAIFTYGLKKADDTFSNIQLPFYTLSDYNELIEVAENEGKISSEDIQTLVEWRDNLA | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 22057
Sequence Length: 2... |
P57358 | MLNPNIFHMPKIIIALDFCNKKSAMKLVNLLNPSIFYLKIGKEMFTILGCKFVKELHQLGFNIFLDLKFHDIPNTVFNATKAAADLGIWMLSVHASGGKEMLISAKKALKSFKKAPLLIAVTALTSFKEEALKEIGINISLTEYILKLSKLSNDCGLDGIVCPGKEAKKIKFLFGNKYKIITPGIRIAKDLLYDQNNIITPKEAKEYKIDYIVIGRSITMSKNPIKKLDLIIKSMQ | Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 26480
Sequence Length: 236
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
Q89AL6 | MHLKSNFKNINIIIALDFFDENKAMKFIYNLNPTIYALKIGNIMFTLFGVRFIKILQKLGFKIFLDLKFYDIPNTIFGAIQAVANLNIWMVSIHISGGIQMLKSARLALKPFKNKPLLMGVTILTSLDKTDMSKLGIQISLSKYILSLAKIAHKCNLDGIICSGTEISNIKKHINVKNFKILTPGIRLNGCSSNDQKNVTTPMLAKQYNVDYIIIGRIVTSSQNPLKTLELIRSQI | Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 26565
Sequence Length: 236
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
B9MS23 | MLNFSDRLIESIKKKNSVLIAGIDTSIENIPDYFIKRFYDKEKSEIDNLKTILFEYIRRIIDAVEENVVGVKFQAAFFEQYSYHGFEVLHKLCEYTKNKKLVVIFDGKRNDISSSAKGYSNAYLGETPVFGKKMRFFEFDAITTNPYLGQDGIKPFVEDCERFKKGLFVLVKTSNPSSADFQDLMVEDKYLFEVVAEKVYEWGKNCIGKEGYSDVGAVVGATQPEAAKRIREILPNSFFLVPGIGVQGGKIEDLKYFVDSNNMGIIVNSSRDIIYAYKNYVHSDFEKSSYLASKNIKESINAAIS | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 34715
Sequence Length: 305
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
P58883 | MFVDRLIESVKAKKTPVVVGLDPRIEMIPDFIKEEAFRRKGNGVEGIAEAMYLFNKGIIDAVYDLIPAVKIQVAFYEAYGIEGFKAFFRTAEYAKSLGLIVIADVKRGDIQDVAKMYSKAYLQNPLFDAITVNPYMGEDSMVPYLEDVEKFGKGIFVLVKTSNRSSKDVQDIETKKGGYVYQEVAKMISRLSKVIVGKYGYSSIGAVVGATYPFEAKILREEMPRCYFLVPGYGAQGATAEDVVNCFDEEGYGAIINSSRGVIYAYRSDFWKEAYSEYEYGQAAREEVILMTGMINNALVKRKYIAS | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 34399
Sequence Length: 307
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
B2RME4 | MTTKELFDRICRKRSFLCVGLDTDVKKIPPHLLNEDDPILAFNKAIIDATAEYCVAFKPNMAFYESMGSFGAHSFEKTIEYIRERYPDQFIIADAKRGDIGNTSDMYARSFFEHLKVDALTVSPYMGEDSISPFLSYAGKFTVLLALTSNKGSQDFQMMRDADGEYLFERVIRISQTWDNAGQLMYVVGATQASMLKDIREIVPDAFLLVPGVGAQGGSLEDVAEYGMNAHCGLLVNASRSIIYADNTEGFAAKAAGEAAAMQRQMEIALRAKGLI | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 30558
Sequence Length: 276
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
Q9WYG7 | MTPVLSLDMEDPIRFIDENGSFEVVKVGHNLAIHGKKIFDELAKRNLKIILDLKFCDIPSTVERSIKSWDHPAIIGFTVHSCAGYESVERALSATDKHVFVVVKLTSMEGSLEDYMDRIEKLNKLGCDFVLPGPWAKALREKIKGKILVPGIRMEVKADDQKDVVTLEEMKGIANFAVLGREIYLSENPREKIKRIKEMRL | Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 22809
Sequence Length: 201
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
B9L1A9 | MSFRERLEQTIAQNHSLLCIGLDPDLERFPTGIPRDPEGIVVFNRAIIEATADLVCAYKPNLAFYLQYGAAGIAALATTRQLIPPHIPVILDAKLGDIASTSAAYARAVFETLGFDALTVHPYLGSEALEPFLSTSDRGVFVLVRTSNPGASEIQDLPVGEAGEPLYLWLAERARAWNQRSGNVGLVVGATYPVDLALVRQRCPDLPILAPGIGAQGGDLERAVCAGLTEATAPLLVTVSRSILYADASARFAESARAAARRVRDTIERIRKEVAGQAGHR | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 30141
Sequence Length: 281
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
P96076 | MDFLEALSRPPLVLGVDPRPTLHGPEPLAHIRRYTLELLEALAPRLAAAKFQLAFFEALGPEGTALLWELASASRVMGLPVIFDGKRGDIGSTAEAYARAYLEAFPGSALTVNPYLGLDALKPFFQAASRTGGGVFVLAKTSNPGSGFLQDLLVEGKPLYLHLAEALEREGERYREGPWSRVGMVVGATYPEAVARVRERAPHAPLLLPGVGAQGGRPLKGEGLLFAASRALYYPGGRPDLKAALEAAEALLKALVE | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 27436
Sequence Length: 257
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
Q8DLT3 | MFNSQAAVASKIIVALDVPNLEVAIATIHRLPQVQFWKVGLELFCASGPMILDVLKDQGKRIFLDLKLHDIPNTVAAAARAIAPYGVDFVTIHTATGLTGLKTAQAALGESATQLIGVTLLTSIGADTLQQELQIPLDPATYVECMANLAHQAGLAGIVCSPQEAARVKQRWGENFLRICPGIRPLGSATGDQARSLTPNAAFAAGASYLVIGRPILQAADPAAAFDDLCSSLV | Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 24566
Sequence Length: 234
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
Q3SK77 | MTHKIIVALDFPAGAPALALADRLDPARCRLKVGKELFTAAGPDLVRALVARGFEVFLDLKFHDIPNTVAAACRAAAGLGVWMLNVHAAGGRRMMDAAREALESLPPGDGAADTPQRPLLIAVTVLTSMSAGDLAETGVADTPAEQVMRLARLAHACALDGVVCSAQEAAGLRAALGADFRLVTPGIRPAGAAAADQRRVMTPVEALRAGATDLVIGRPITGAGDPLAALAAIQADIEENLGRAF | Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 25177
Sequence Length: 245
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
B3E1T2 | MTRDEAKNKIIFALDVDNLKDIDCWAEKLSRKVGMFKVGKELFTSAGPAAVEAVKKHAGEVFLDLKYHDIPNTVAQAMLAAGRLGVKLANLHALGGPEMMEKASQAVRKEFSENERPRLLAVTILTSSTQDTLKAVGIEHPVEEMVVRLAKLAKESGMDGVVASPLEIEAIRAACGPDFLIVTPGVRPSFAAVDDQKRIMTPAEAVKAGADYLVIGRPIAKAADPIQAAELIVDEIVAGVQ | Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 25821
Sequence Length: 241
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC... |
P15188 | MSSITLQSYASRAAKQPNPAAKALLECMERKQTNLCVSIDVTNKQDLLDVCEAVGRNVCLVKTHIDIVEDFDMDLVHQLTQLSEKHDFLIFEDRKFADIGNTVSLQYSAGVHKIASWSHITNAHLVPGPSVISGLAKVGQPLGRGLLLLAEMSSEGALTKGDYTQACVDEAHKDTTGFVCGFIAMSRVDERERANTHRDLLILTPGVGLDVKGDGLGQQYRTPDQVIRESGCDVIIVGRGIYGALTTEEGKADKKAAFAKVSEQGERYKTAGWDAYLKRIGQK | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 30864
Sequence Length: 283
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
A1WGU4 | MNFTDMLRAATARHGSLLCVGLDPEPARFPAGMQGDARKIYDFCAAVVDATADLVCAFKPQIAYFAAHGAEAQLERLMQHMRSNAPQVPVILDAKRGDIGATAEQYAKEAFERYGADAVTLSPFMGFDSIAPYLAYRGKGAFLLCRTSNPGGDDLQNQRLASVAGQPLLYEHLASLAQGPWNRNGQLGLVVGATYPQEIERVRSLAPTLPLLIPGVGAQGGDAAAAVRAGLRSDAPIIVNSSRTILYAGAGADFAGAARAQALRMRALLQAARR | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 29041
Sequence Length: 274
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
O29987 | MKYIVVTGGVMSGLGKGITAASIGRLFVDMGYRVIPIKIDPYINIDAGTMNPFQHGEVYVLKDGTEVDLDLGHYERFIGEEVTGDHNITTGKIYKRVIEKERKGDYLGQTVQIIPHVTDEIKSWIRRVAKESNAEICLVEIGGTVGDIEGMPFLEAIRQMHNEEKEEDFALVHVTLVPLDAGGEQKTKPTQHSVKELRELGLHPDVIVGRCSERLKPATKKKIALFCDVPEEAVISNEDAEDIYEVPLIFKREKLDEYLMRKLNLRAKESRKEWEEMVKRMKTLYEEASIAIVGKYVDVRDAYLSIKEALKHGGIEAGCK... | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate... |
G0HV10 | MPTEPETDYDPELGRKFIFVTGGVMSGLGKGITAASTGRLLKNAGFDVTAVKIDPYLNVDAGTMNPFQHGEVYVLKDGGEVDLDLGNYERFLDIDMTFDHNVTTGKTYQHVIEKERSGDYLGRTVQIIPHITDDIKRRIREAAEGNDVCIIEVGGTVGDIEGMPYLEALRQFAHEEDEDDILFTHVTLVPYSKNGEQKTKPTQHSVKELRSIGLQPDILVGRCSDKLDIDTKEKIALFCDVPTEAVFSNPDVDDIYHVPLMVEEEGLDQYVMEELDIATEALPEDERENRWRDLVTQNTEGEVDIALVGKYDLEDAYMSV... | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate... |
O25116 | MDRAKFIFVTGGVLSSLGKGISSSSIATLLQHCNYQVSILKIDPYINIDPGTMSPLEHGEVFVTSDGAETDLDIGHYERFLNRNLTRLNNFTTGQIFSSVIENERKGEYLGKTIQIVPHVTDEIKRRIKSAAKGLDFLIVEVGGTVGDMEGMFYLEAIRQLKLELGNEKVINVHVTLIPYIQTTNELKTKPTQHSVQELRRLGVTPQIILARSPKPLDKELKNKIALSCDVEQDSVIVATDTKSIYACPILFLQEGILTPIARRFNLNKLHPKMAAWNTLVEKIIAPKHKVKIGFVGKYLSLKESYKSLIEALIHAGAHL... | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate... |
Q4FM39 | MARYIFVTGGVVSSLGKGLSSASLAYLLQSRGYKVRIRKLDPYLNVDPGTMSPFQHGEVFVTDDGAETDLDLGHYERFSGVSAKKSDNITTGKIYSDVLRKERKGEYLGKTVQVIPHITDRIKQFIKHDSSKEDFVICEIGGIVGDIESLPFVEAIRQFANDVGKKNALFIHLTLVPYLKASDEIKTKPTQHSVKELRSIGIQPDIIICRSERPIPLDHRKKISLFCNVDIKNVIETVDVRTIYEAPMSFFKEKLDLQVLNYFKLKSKKPANLNPWKKITKIILHNKKQVNIAIIGKYVELKDAYKSLDEALTHGGIDNK... | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate... |
Q6L1K7 | MHYIVITGGVISGLGKGTITSSLSYLLKNSGFKVTNIKIDPYINYDAGTMNPYQHGEVFVLDDGSEVDLDLGNYERFLDTDLTGNNNITTGKIYKSVIERERHGDYLGKTVQIIPHITNEIKERIKRASSGYDIALIEVGGTVGDIESMPFIEAVRQLRSTDDVIYSHVTLVPEINGEQKTKPTQHSVKELRSLGISPDILFCRSEKPLGKDVIEKISLFTDVPASGIISMYNVKNVYMIPEIMMRQGILEYIKKRTGTSNHNLDYTWSNFVENIKNPAESVDIAIVGKYIELQDAYISHKEAFSHVTGNTGISVNIHWV... | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate... |
Q9PQK7 | MEIDLMKHIQKTKFIFVTGGVYSSLGKGVSASSIGRILVELGYSVAMQKLDPYLNIDPTYLSPLQHGEVFVTKDGKEADLDLGTYERFINADLNKYASVTSGKIYYEILTKERENGFDGKTVQTIPHVTSAVIDYIKKIKDSLKTDFIIVEIGGTIGDIESLPFIEAISQFKTIYGVNNVMFIHCSPLIYIEKVGELKTKPTQHSVKTLRSLGINLDLLLLRTNQKLDEVTIKKLAWSCGLDIDMIFAAYDVESVYLLPNVLFEQGIHKTILDFFSLPLKNDNINSWIDFTDKITTFKKHNLVIGLVGKYVELPDAYKSV... | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate... |
Q73HS5 | MKEAKFIFVTGGVVSSLGKGLVASSVGALLQAHGFKIRIRKLDPYLNIDPGTMNPTQHGEVFVTEDGAETDLDLGHYERFTGIKATKDDNITTGKIYHELLKKERRGDYLGKTVQVIPHVTDLIKSFIFNGTEGLDFVICEIGGTVGDIESQPFLEAIRQVNYTLGKQRVILIHLTLIPYLAAAQELKTKPTQHSVRELNSAGLQPDIILCRSEKEIFDNQREKIAKLCNVSLSNVIPAPDVSHIYELPVLYSQCGLDTQILEHFHLSKPKPSLTEWDQIVHSIRHPTQEVTVSIVGKYTEFPDAYKSLVEALNHGAISN... | Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate... |
Q7NI44 | MKYRRVLLKLSGEALMGDREFGIDPEVVKSLAGEIARVVEAGTELAVVVGGGNIFRGVKASSSGMDRATADYVGMLATVMNALTLQDALEQQFQVQTRLLSAIEMKEVAEPFIRRRAMRHLEKGRVVIFGAGSGNPFFTTDTTAALRAAEIDAQVIFKATRVDGIYDSDPKFNPQAVRFEKITFHEVLVQNLRVMDSTAIALCRENNIPILVFNVFEKNSIYRAVQGEAVGTYVC | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 25853
Sequence Length: 235
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.22
|
Q5FPZ5 | MMTENREQSPSYKRVLLKVSGEALMGDGPSGVDPVMVDMVAADIADVVASGVEVCLVVGGGNIFRGLAAAAKGMDRAQGDYAGMLATVINALMLQNALERRGMETRVMTAIQMAAIAEPYIRRRAVRHMEKGRVVIFAAGTGNPFFTTDTAAALRANEMECDALFKGTQVDGVYSADPRRNPDAERYDQLTYLEVLARDLNVMDAAAISLARENKLPIVVFNMHAPGSFGAVMRGEGLFTKIIEAD | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 26464
Sequence Length: 246
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.22
|
P43890 | MSQPIYKRILLKLSGEALQGEDGLGIDPAILDRMAVEIKELVEMGVEVSVVLGGGNLFRGAKLAKAGMNRVVGDHMGMLATVMNGLAMRDSLFRADVNAKLMSAFQLNGICDTYNWSEAIKMLREKRVVIFSAGTGNPFFTTDSTACLRGIEIEADVVLKATKVDGVYDCDPAKNPDAKLYKNLSYAEVIDKELKVMDLSAFTLARDHGMPIRVFNMGKPGALRQVVTGTEEGTTIC | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 25726
Sequence Length: 237
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.22
|
B9LSL4 | MRVVVSIGGSVLAPDLDPDRVAAYAEAIERLAADGCEVGVVVGGGGVAREYIETARELGANEVELDQLGIGTTRLNARLLIAALAGGANLSPATGYDEAAAALRRGEVSVMGGVTPGQTTDAVAAAFAESVDADLLVYATSANGVYDADPNVDDDATQFGSMSPAELVDIVLPMSRNAGASAPVDLLAAKLIDRAGIRSIVLDGTNPEVVVDAVLRGDHTGTDVIPTGSEEPIYWTGSSDA | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 24465
Sequence Length: 241
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.22
|
Q7UTH1 | MPDIAPSSQPEGDLRYRRVILKLSGESLAESGKRGISDNELLAIAKQIKSAHESGCQIAIVNGGGNILRGASFSGANASVQEATAHYMGMLATVINSLALQDALDSIGLQTRVMSALPVDRVAEQFIRRRAIRHLEKGRVIILSGGIGSPFVTTDTAAAQRALEIEADVILKATRVDGVYSDDPEKNPHAVLYEQLSYNEVIQKKLRVMDATAIALCNEHRKPILVFNFKQDGNIVRAVRGESVGTWIGDPQDTQTNQR | Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Mass (Da): 28085
Sequence Length: 259
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.22
|
O14949 | MGREFGNLTRMRHVISYSLSPFEQRAYPHVFTKGIPNVLRRIRESFFRVVPQFVVFYLIYTWGTEEFERSKRKNPAAYENDK | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
P48503 | MRPTQTMLGGGGGAPIGKHNHYLGGWGNFGGMKQRGIISYGISPNRQNPLAGTAHDAVFNTFRRVSSQFLYWAPSLVAGYYIMNWAIERNHYLNSKAGRAEFAGQEE | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
P50523 | MGGAAGGKTYLGWWGHLGGPKQKGIITYSLSPFQQRPMAGFFKTSTQNMFRRVMTEGLYVAIPFGIAYYIYCWGKERNEFLNSKHGRHLVEE | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
P08525 | MGPPSGKTYMGWWGHMGGPKQKGITSYAVSPYAQKPLQGIFHNAVFNSFRRFKSQFLYVLIPAGIYWYWWKNGNEYNEFLYSKAGREELERVNV | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
Q9LXJ2 | MEYAARRNQKGAFEGFYKLIMRRNSVYVTFIIAGAFFGERAVDYGVHKLWERNNVGKRYEDISVLGQRPVEE | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
P00130 | MVAPTLTARLYSLLFRRTSTFALTIVVGALFFERAFDQGADAIYEHINEGKLWKHIKHKYENKE | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
Q54QR8 | MSNALTNIFYKYVARRNSTWMAGAILGAFVLDSTVSGAVNTFFDSVNKGKLWKDVYAERVKKGISQ | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
Q9XY35 | MKVIYNTLFKRTSTYAVAIIASAFFFERALDVTSVAIFEGINKGKLWKDIKGKYE | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
Q9UDW1 | MAAATLTSKLYSLLFRRTSTFALTIIVGVMFFERAFDQGADAIYDHINEGKLWKHIKHKYENK | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
Q6CJX2 | MSFASTLYKTVFKRNSVFVGTVFASAFVFQAAFDTGVTSWYENHNKGKLWKDIKGGIMNGGEEDEEDDE | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
Q8R1I1 | MSSPTIPSRLYSLLFRRTSTFALTIAVGALFFERAFDQGADAIYEHINEGKLWKHIKHKYENKE | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
Q7SGT7 | MSALYNLIFRNNTAFVGAVFAGAFAFELAYDNGMDKVWDKINKGRQWKDIRHKYVEAEE | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
O74433 | MASSTIYNIFFRRNSSFYATIFVSAFFAKIGFDVFTDSVWKRANAGLTWDEVKPRFLNKDEDAEDDE | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
P46270 | MESAARRSGGGVLEGFYRLVMRRTPVYVTFVIAGALLGERAVDYGVKTLWEKNNVGKRYEDISVLGQRPVDE | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
P22289 | MSFSSLYKTFFKRNAVFVGTIFAGAFVFQTVFDTAITSWYENHNKGKLWKDVKARIAAGDGDDDDE | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
O94710 | MLCLVYNSILCKQRRISLKVLQQFRCWNISKTFLSYRTLTALAIETSCDDTSVSVVRTSDSSSHCQNEIICLNTHRTISKYEAYGGIHPTIVIHEHQKNLAKVIQRTISDAARSGITDFDLIAVTRGPGMIGPLAVGLNTAKGLAVGLQKPLLAVHHMQAHALAVQLEKSIDFPYLNILVSGGHTMLVYSNSLLNHEIIVTTSDIAVGDYLDKCAKYLGIPWDNEMPAAALEQFASPEINSTSYSLKPPIPLNTREKVHSASFSFSGLESYACRIIRKTPLNLSEKKFFAYQLQYAAFQHICQKTLLALKRLDLSKVKYL... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP)... |
P43122 | MISIKGTGRFLLDNYRIWQRRAFNRPIQLRKGYKVLAIETSCDDTCVSVLDRFSKSAAPNVLANLKDTLDSIDEGGIIPTKAHIHHQARIGPLTERALIESNAREGIDLICVTRGPGMPGSLSGGLDFAKGLAVAWNKPLIGVHHMLGHLLIPRMGTNGKVPQFPFVSLLVSGGHTTFVLSRAIDDHEILCDTIDIAVGDSLDKCGRELGFKGTMIAREMEKFINQDINDQDFALKLEMPSPLKNSASKRNMLSFSFSAFITALRTNLTKLGKTEIQELPEREIRSIAYQVQESVFDHIINKLKHVLKSQPEKFKNVREF... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP)... |
Q2TAL8 | MNNSLENTISFEEYIRVKARSVPQHRMKEFLDSLASKGPEALQEFQQTATTTMVYQQGGNCIYTDSTEVAGSLLELACPVTTSVQPQTQQEQQIQVQQPQQVQVQVQVQQSPQQVSAQLSPQLTVHQPTEQPIQVQVQIQGQAPQSAAPSIQTPSLQSPSPSQLQAAQIQVQHVQAAQQIQAAEIPEEHIPHQQIQAQLVAGQSLAGGQQIQIQTVGALSPPPSQQGSPREGERRVGTASVLQPVKKRKVDMPITVSYAISGQPVATVLAIPQGQQQSYVSLRPDLLTVDSAHLYSATGTITSPTGETWTIPVYSAQPRG... | Function: Transcriptional regulator that acts as a mediator of the integrated stress response (ISR) through transcriptional control of protein homeostasis under conditions of ER stress . Controls the outcome of the unfolded protein response (UPR) which is an ER-stress response pathway . ER stress induces QRICH1 transla... |
Q9SFB7 | MYEKIIILSVFLLTFLPSCFSSYPFNHRDDLFMSSNVYYETNRQHQHGHNTRNSHLKNRHGYAPRSSPRSFNVNTFGAKANGNDDSKAFMKAWEAACSSTGIVYIVAPKNRDYMLKAVTFSGPCKSSLIIFKIYGRIEAWENPSDYKERRHWIVFENVNNLRVEGGGRIDGNGHIWWPKSCKINPQLPCLGAPTAVTFVECNNLRVSNIRLENAQQMHLTFQDCKNVKALNLMVTSPADSPNTDGIHVSGTQNILIQDSIVRTGDDCISIVSGSENVRATGITCGPGHGISIGSLGEDNSEAYVSNVVVNKATLIGTTNG... | Function: Polygalacturonase required for cell type-specific pectin degradation to separate microspores. Involved in anther dehiscence and floral organ abscission.
Catalytic Activity: (1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.
Sequence Mass (Da): 48572
Sequence... |
O49432 | MELRKSQVAMPVFLAIMSLMVSQVVFAEKDSGSMSPHDRALAEMQALKASLVRRNLPALVSPPPTPPQAVPGPRVYQVISYGADPTGKLDSTDAILKAMEEAFDGPNHGVLMQGINDLGGARIDLQGGSYLISRPLRFPSAGAGNLLISGGTLRASNDFPVDRYLIELKDESSKLQYIFEYITLRDLLIDCNYRGGAIAVINSLRTSIDNCYITRFGDTNGILVKSGHETYIRNSFLGQHITAGGDRGERSFSGTAINLMGNDNAVTDTVIFSARIGVMVSGQANLLSGVHCYNKATGFGGTGIYLRLPGLTQNRIVNSY... | Function: Polygalacturonase required for degrading the pollen mother cell wall during microspore development.
Catalytic Activity: (1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.
Sequence Mass (Da): 51659
Sequence Length: 481
Subcellular Location: Secreted
EC: 3.2.1... |
P52076 | MRILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTARDALAERVEGLRLGADDYLCKPFALIEVAARLEALMRRTNGQASNELRHGNVMLDPGKRIATLAGEPLTLKPKEFALLELLMRNAGRVLSRKLIEEKLYTWDEEVTSNAVEVHVHHLRRKLGSDFIRTVHGIGYTLGEK | Function: Member of a two-component regulatory system QseB/QseC. Activates the flagella regulon by activating transcription of FlhDC. Currently it is not known whether this effect is direct or not.
PTM: Phosphorylated by QseC.
Sequence Mass (Da): 24678
Sequence Length: 219
Subcellular Location: Cytoplasm
|
P45337 | MRILLIEDDNLIGNGLQIGLTKLGFAVDWFTDGKTGMAALTSAPYDAVVLDLTLPKLDGLEVLQQWRSNHQDVPVLILTARDTLDERVKGLQSGADDYLCKPFALAEVAARLQALIRRRYGYHHSVIEQAGVKLDQNQRSVWLNNQPISLTSREYKLLELFMLNKDRVLSRSSIEEKLSSWDEEISSGALDVHIYNLRQKLGKQFIRTVHGVGYALGQVEK | Function: Member of a two-component regulatory system QseB/QseC.
PTM: Phosphorylated by QseC.
Sequence Mass (Da): 24903
Sequence Length: 221
Subcellular Location: Cytoplasm
|
P40719 | MKFTQRLSLRVRLTLIFLILASVTWLLSSFVAWKQTTDNVDELFDTQLMLFAKRLSTLDLNEINAADRMAQTPNRLKHGHVDDDALTFAIFTHDGRMVLNDGDNGEDIPYSYQREGFADGQLVGEDDPWRFVWMTSPDGKYRIVVGQEWEYREDMALAIVAGQLIPWLVALPIMLIIMMVLLGRELAPLNKLALALRMRDPDSEKPLNATGVPSEVRPLVESLNQLFARTHAMMVRERRFTSDAAHELRSPLTALKVQTEVAQLSDDDPQARKKALLQLHSGIDRATRLVDQLLTLSRLDSLDNLQDVAEIPLEDLLQSS... | Function: Member of a two-component regulatory system QseB/QseC. Activates the flagella regulon by activating transcription of FlhDC. May activate QseB by phosphorylation.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (D... |
P45336 | MKNRSLTLRLISVLCLTALFVWLGSTLVAWWQVRHDVNKVFDAQQVLFAERLANSDLSTILLESSTTLNKNSQSVLKKSYDDDALAFAIFSKTGKLLFSDGRNGKDFIFNYKTGFYNANIYDDDDKWRIFWRMAANGELVIAVGQELDYREDLIEEMILGQMWIWFASLPILIIVLGWLIHKELRPIKRLSQEVQTRKSGDVSLLNTEGLPVEILPLVKNLNQFFDRTSAMLQRERRFTSDAAHELRSPLAALRIQIEVAQLAGDDVALREQALLHLTQGIDRASQLIEQLLTLSRLDNLQALETLQLLDWEAIVQSLIS... | Function: Member of a two-component regulatory system QseB/QseC. May activate QseB by phosphorylation (By similarity).
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51271
Sequence Length: 451
Subcellular Location: ... |
Q6LU70 | MQVSDFHFDLPNELIARYPQPERTASRLLQLTGETGNIQHKGFKDVLDLAESGDLFVFNNTRVIPARIFGRKASGGKIEVLVERILDDKSILAHVRASKSPKPGNELLLGENDDYQAEMIARHDTLFEIRFNSDKTVLEILEEVGHMPLPPYIDRPDEDADKERYQTVYNAKPGAVAAPTAGLHFDDKLMAALKAKGVNFAFVTLHVGAGTFQPVRVDNIDDHHMHSEYVEVPQDVVDAVNATKANGGRIIAVGTTSVRSLESAAQDAVKKGTELVPFFGDTEIFIFPGYEFQLVDVLVTNFHLPESTLIMLVSAFAGYE... | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Ma... |
A6KZK0 | MKLSQFKFKLPEDKIALHPAKYRDESRLMVVHKSTGKIEHKVFKDILDYFDDKDVFIFNDTKVFPARLYGNKEKTGARIEVFLLRELNEELRLWDVLVDPARKIRIGNKLYFGDDDSMVAEVIDNTTSRGRTLRFLYDGSHDEFKKALYALGEAPLPSFIRRPVEEEDAERFQTIFAKNEGAVTAPTAGLHFSRELMKRMEIKGIDFAFVTMHAGLGNFREIDVEDLTKHKMDSEQMYVNADACRIVNNAKDEGKNICAVGTTVMRTIETAVGTDGHLKEFDGWTNKFIFPPYDFSVANSMVTNFHLPLSTLLMLVAAYG... | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Ma... |
A2BV65 | MNFEIYNEEIDHKLEAYDYCLDESLIAGKPSKVRHESRLMIVRDSSLKEDYSTNKYTKDLLAELREGDLVVINDTKVMKARLKVELENGQLVELLVLEKSDQSTWLCLAKPAKKLKINKQLNLKSPFAKDIKLKISGIDDETGGRFIKFPENINDLISMNKLLDIFGEIPIPPYIKSSEEESFHENSYQTEYACNPGAVAAPTAGLHLSKSLISNLKKKGILVMPITLHVGYGTFKPIDQEDLSDLKLHKEWVSVSKKVVEEIKRIKKTDRRVIAIGTTSVRALESCYSYAMKDFIPIAKYVDLVIKPGYKFKAVDGLLT... | Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
Sequence Ma... |
Q24ZT5 | MGKNKVVLLFSGGIDSTVLLFWLLSRNYEIFPLFINYGQKSYEGELEAINKILKDLNTKNNLLTLNMPELQLVGSGALVGEYPKNISSHNEWYASEFFPNRNMILLSIAATYGYKLQISKIAIGVVGDSYQDTTRTFLEAMEMTLAQSIARYELIAPFAGHPRQKVIEEAYRLQVPLKSTFSCNAMGNRHCLLCTSCYEREKAIQLHEQCGKERAEKSDF | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 24953
Sequence Length: 2... |
Q96ZD9 | MKALLLMSGGLDSSSAAYYYTRRGLDFDCLFINYGQRSARMQLRSSKIICEKLNKKLLVADIRKIRELFISDIWLKPHEPITHRNLVIIPIAIAFAKEKGYEEIIIASVKEDCEYEQNRIEIIKELKNLGEILKVKVSTPFAGMPKSFLLKLGVSAGLDPSLTYSCLLGHKYHCGQCSQCLKRKEAFKSANIQDPTKYLNLS | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 22936
Sequence Length: 2... |
Q24VU8 | MKKAVVLLSGGLDSTTCMSVAHKAGYELYPLSFDYGQRHQRELEAAKAVAQYYKVKEHRLIKIEHVGGSALTDASIQVPDYTEDGQIPVTYVPARNILFLSYALGYGEVMGAEAIFIGISSVDYSGYPDCRPEFLQAFQKVVDVGTKAGVSGQTIAIKAPLLYLSKAETIQLAAENGAPLHHTTSCYRGGEKACGTCDSCTLRLKGFAEAGIKDPIDYVNQGDRSCFSTPLED | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 25203
Sequence Length: 2... |
Q2IUE0 | MARKKVLVLHSGGMDSTTCLLQAKAEGHDVASLGIDYGQRLLVEMMFAEGQCEKYSIPRHVINVNWQKAERQIPLNRSVEEMAHSVSPAFLPGRNIVFLGLGHAHAAGIGADELQIGLNCVDFSGYPDCTTQFYDSYCTMLNIGNPGGPKLVAPLLKMSKPEIARLASTLGLQRNDTWSCYRPQIREGSIVACGECDACKLHEFAWQELK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 23096
Sequence Length: 2... |
A6WGA4 | MDRPAVVLLSGGLDSTTVLAIAKSQGFTPYALSFAYGQRHAVELDAARRVATALGAAGHVIATIDLTVFGGSALTADIAVPKHDTVEDLQADIPITYVPARNTIFLSYALAYAEVVGAGDIFIGVNALDYSGYPDCRPEYVDAFQAMGRLATRAGVQGTELTIHAPLMQMTKADIVRAGLALGVDYGMTSSCYDPDAAGHPCGHCDSCLLRLNGFAEAGSTDPLPYRGA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 23929
Sequence Length: 2... |
Q1IHK6 | MKVQRGDTGKAVVVLSGGMDSTVCATLAVREYGAENIGALHVSYGQRTAAREKQAFAAVAERLGIQTRLAVETPFFRAIGGSALTDANIAVPDAGELIGHEIPVTYVPFRNAHLLAMAVSWAEVLGASKIYIGAVAQDSSGYPDCRPEFYEAYNLAVRRGTKAGDIEVVTPLIALRKHEIVSLGLELGAPFDLTWSCYSREDCACGVCDSCVLRLRAFEGAGAVDPVPYAPRLAGHD | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 25187
Sequence Length: 2... |
C1D6L0 | MDSLRDPEHALVVLSGGQDSTTCLYWALSRFAQVSAISFDYGQRHRVELDAARTIAAMAGVGHTIIPINTFSALGGNALTDQQMSPDTGPDAETLLPNTFVPGRNLVFLTFAAAWAWPRGIRHIVTGVAQTDYSGYPDCRENTLRALELAINLGMESRMRLHMPLMFLSKADTVTLARTVGAMPALAFSHTCYAGAVPPCGQCAACVLRAKGFAEAGIPDPLLNRLAGV | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 24505
Sequence Length: 2... |
Q5ZRJ5 | MKKAVVLLSGGLDSTTCLALAKSQGFACYALSFSYGQRHSAELCAATRIAKHMGAADHKIVTLDIALFGGSALTDASIEVPEFKESPEIPVTYVPARNTIFLAMALGYAESIGARDIFIGASSVDYSHYPDCRPEFIESFQSLANLATKAGIEGDRFTINAPLQYLSKVQTIQLGTELGVDYGLTVSCYQANEAGEACGQCDSCTFRKRGFKSAGVDDPTRYQKCVHI | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 24477
Sequence Length: 2... |
B1Y8J4 | MNRDSRTALVLFSGGQDSTTCLAWALTRFAHVETLAFDYGQRHRIELDCRLTVLAQLREQFPDWAERLGADHLLDLSLLAQISDTALTTEREIELQANGLPNTFVPGRNLLFLGMAATLAYRRSASVLVGGMCETDYSGYPDCRDNTLKALQVALSLGLAAPMTIETPLMFLTKAQTWTLAEDLGGAPLVELITEHTHTCYLGERGQRHAWGHGCGHCPACELRHAGHAAWLGGR | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 25818
Sequence Length: 2... |
Q72VK9 | MNSSSNEKNKDLNRKNFSSKTDSSNNKAVVLLSGGLDSTTCLYQAIADGKEIQALSFDYGQRHKIELSYAKKVTRKLGIPHTIQKLKPELFLGSSLTQKSLHVPKNSLRKEEIPNTYVPGRNILFLSFAVSLAEGTGSDSIYIGVNSMDYSGYPDCRPEFIKMFEMAIQLGTKKGSQGPSIKILTPLQNLSKKEIVLLGNQLKVPFHLTFSCYDPKNGKACGKCDACLLRKKGFQETGVSEK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 26720
Sequence Length: 2... |
A0L4R8 | MPTIMSAVVLLSGGLDSATVLRMAHATGQRIHALSFRYGQRHTMELEMARKQALSLPGVAHRIMDLQLSLFGGSALTADIPVPKGGVDENTIPVTYVPARNMVFLSLALAWAESLGAQHLYIGVNAVDYSGYPDCRPEFIQSFQQTANLATKAGVEGHPFTVHTPLINLTKAQIIQQGLALGVDYGLTRSCYDPDAQGAGCGLCDACRLRLQGFAEAGVPDPAPYQGP | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 24307
Sequence Length: 2... |
Q0I671 | MTDSTAIALLSGGLDSATAAALAIKSGFRVIGLSFDYGQRHRRELDAAVEIAKALNLAEHHTINVDLAMWGGSSLTDHAQTLPTSGVETSIIPNTYVPGRNTVFIAIGLSLAEARGADRLVLGVNAVDYSGYPDCRPDYLEAFQDLADLSSRAGREGHGPKLWAPLVEWSKQQIAEEALHLGIPIERTWSCYSGGDVPCGVCDSCRIRDEALLAAGRPDLCSPGRP | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 24072
Sequence Length: 2... |
Q55468 | MTKTAVVLLSGGLDSATVAAIAKREGYRVIALSFNYGQRHDRELRAAADIVQALGIPEHFSINLDLAQWGGSSLTDRQQTLPQTGVEPDIIPSTYVPGRNTVFIALGLSLAEAKGAEAVFLGINAIDYSGYPDCRPEYLATYQQLAALSSKVGVEGRPIQLLAPLIELSKVDIVHKALELGVPIAQTWSCYAGGEEPCGRCDSCRLRDQALIEAGHPELASAKGRLWREKVD | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 24972
Sequence Length: 2... |
Q9HJL6 | MERKKAVVLLSGGLDSSTVLAYAISLGYEVHAISFDYGQRHSREMNSSEELAKYYGVDRKIVHVDLRSIGKSALTDDIEVPSRDLESIPEEIPVTYVPARNTIFLSIAAAYAESIGSTDIFIGANAIDYSGYPDCRPEYFNAMEKALTLGTEIGLRKGMHINVPLQYLTKADIIRMGLKLGVPYEKTWSCYKGGEKACGECDSCLLRLKGFMEAGSEDPLEYEKYPTFYKDYIEKRKK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Mass (Da): 26646
Sequence Length: 2... |
Q8R9P3 | MTDKYKERRFDIYGYEKIDKEVLESIEYEYPEKNTIVEYITDEFSSVCPWTGLPDNAKLTIRYIPHKKLVELKSLKYYLTSYRNVGILQEHAINRILDDLVEFLQPKFMEIIGEFQERGGIATRIIARYEKEEY | Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
Sequence Mass (Da): 16088
Sequence Length: 134
Pathway: tRNA modification; tRNA-queuosine ... |
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