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stringlengths 6
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stringlengths 11
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stringlengths 108
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Q2GH90 | MYKQSWELLGNGQHADLTVAYINARIIDPESKLDIRGSLLTKGDKIIDFGPDLFANGIPSTIDEVIDCNNNILLPGLIDIHVHFREPGQEHKETINTGSKSAAAGGITTVVCQPNTIPTISSVITAKYIKMRALESAYVNIEFYASITKSDNSLSDMALLKEVGAVGFTDDGMPVMNALTMRQALSYSSMLDTVIAQHAEDLNISNNGCINEGIISYELGLKGIPDISESIIVNRDIALMKNIKNVHYHILHVSSQESLHIIKQAKSQGLKVTCEVTPHHFTLTERDIMTHGSLAKMNPPLRTENDRLSMIEGLKSGIIDCIATDHAPHDINAKELPLDTAAFGIVGLETMLPISLELYHNGTMPLIDLLATLTYKPADIIKVPRGRIKKDYVADLIILDLDHEWVVDISKFASKSKNSPFHNRKVKGKVLRTIVSGKTTYKAEIII | 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 pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
EC: 3.5.2.3
|
B2KCN5 | MKYLIKNAHVIDPANKIDGLKDILIENGKIAAVENKIEDNAAKIIDAKGLTAMPGFVDMHTHLREPGQEGKETIFTGTKAALKGGFTTVCMMPNTNPAMDSKNNLAIAQDIIRKTANVNVEIMGAITKNRAGKELSNFAELKQAGAIALSDDGSGVEDDAVMQAAFKESVKQDILLISHSEDSKLSAGGVMNEGLISTKLGLKPISNASEYEMVKREIQLAKGLDAKIHIAHVSTKESCEIIAKAKKQGVMVTAEATPHHFTLTDKACESFSGNTKMNPPLRSEADVEALKQALKDGTIDAIATDHAPHAVHEKEVEFDLAYFGIIGLETAFPLAYDVLVKSGLIDMAKLVGLMSLNPSKILGLKKGTLTPGADADITIVDLNKQWVYSKEEVQSLSCNSPFIGKNLQGYIEYTFVGGELKLENGTLKVKDA | 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 pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
EC: 3.5.2.3
|
Q74DP4 | MNLLIKGGRVIDPSQGIDEVLDILVENGAIKELGKGLAAPAGAGVVDAAGLIVTPGLIDMHVHLRDPGLEYKEDIVTGTRAAAAGGFTSVACMPNTKPVNDNKAVTSYIVAKAKAEGLVNVFPVGSITQGSKGDALAEMGDLKEAGCVAVSDDGRPVTSSELMRRALEYAKGMGIMVISHAEDLSLVGEGVMNEGFVSTELGLKGIPWAAEDAATARDVYLAEFTNSPLHIAHVSTMGSLRIIRNAKARGVKVTCETAPHYFSLTDDAVRGYNTNAKMNPPLRTADDLAAVKEALKDGTIDAIATDHAPHHLDEKDVEFNVALNGIIGLETSLPLSLKLVEEGVLTLPALVEKMACNPAAILGIDRGTLRQGAVADITVIDPAAVWTVEAGALASKSKNSPFLGWEMKGAAAYTIVGGTVVHSRG | 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 pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
EC: 3.5.2.3
|
Q9KXR3 | MSKTLIRGAKVLGGEPQDVLIDGTVVEAVGTNLSAEGAEVVEADGKVLLPGLVDLHTHLREPGREDSETVLTGTRAAASGGYTNVFAMANTFPVADTAGVVEQVWRLGQESGYCDVQPIGAVTVGLEGAKLAELGAMHESAAGVTVFSDDGKCVHDAVIMRRALEYVKAFNGVVAQHAQEPRLTEGAQMNEGVVSAELGLGGWPAVAEESVIARDVLLAEHVGSRVHICHLSTAGSVEIVRWAKSRGIDVTAEVTPHHLLLTDELVRSYNPVYKVNPPLRTERDVMALREALADGTIDIVATDHAPHPHEDKDCEWAAAAMGMVGLETALSVVQETMVDTGLLDWAGVADRMSFKPAKIGQATGHGRPVSAGEPANLTLVDAAYRGQVDPAGFASRSRNTPYEGRELPGRVTHTWLRGKATLVDGKLT | 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 pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
EC: 3.5.2.3
|
Q8DPQ5 | MLLIKNGRVMDPKSGLDQVCDVLVQDGKIIKIAPEITEEGAETIDATGHVVAPGLVDIHVHFREPGQTHKEDIHTGALAAAAGGFTTVVMMANTSPTISDVETLQAVLQSAAKEKINVKTVATITKNFNGKNLTDFKALLEAGAVGFSDDGIPLESSKIVKEAMEEAKKLNTFISLHEEDPGLNGVLGFNENIAREHFHICGATGVAEYAMMARDVMIAYATKAHVHIQHLSKEESVKVVEFAQGLGAEVTAEVAPQHFSKTEALLLTQGSNAKMNPPLRLESDRRAVIEGLKSGVITVIATDHAPHHVDEKNVEDITKAPSGMTGLETSLSLGLTYLVEAGELSLMELLEKMTYNPAKLYNFEAGYLAENGPADITIFDAKADRLVDSHFASKAANSPFIGETLKGQVKYTICKGQIVYQA | 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 pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
EC: 3.5.2.3
|
O08357 | MWIKGKAYYEGEIKEICINFDRSIKEIRANCKPDMTFTNEELILPASVDLHVHVRGAQLSYKETVATATSEAVYGGVGVIVDMPNTVPYINTPERIKERLREFQLYSRTDYGIYSGVSKEVEEIDKLPIAGYKIYPEDLEKEETRYVLEKSKKLKILHPEMPFVSKIERSLRRSYWMETAAINLVKGNMHITHITNFETLQLAKSMGFTTDITAHHLVVDGERDCISKVNPPIRDYVTRLKLFLKGLFEVDCIASDHAPHSKEEKRMNFDLCPPGIAGVSFSTPYIYSLMFKGLISIDRAVSLLSGNPSRILNIPTGKIKEGYRANFTVIKRENWRYTTKFSKVTETPMDGFSLDAKVTNVIVEGKLAFDGENVYPIRGVNIFDSSSRS | 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 pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
EC: 3.5.2.3
|
B2V5I6 | MILIKNGHIVDPQNNLNDKFDILIEKGEIKKIEKNIQPFAGCEVIDAEGKIITPSFTDIHVHFRDPGQTYKEDIESGSKAAVAGGYTTVVCMPNTIPAIDDVPIVRYIIEKGEEIGLCRVLPSAAITKGRKGKELTEMALLKDAGAVYFTDDGAPVMDSFIMRKAMEYAGSLGTFVADHCEDLNLSQNGVAHEGEIAAALGLPPLPPEAEDTMVARDCILSIQTGMPVHICHISTKLSVEIVAWAKAMGAKVTAEVTPHHLYLTDEEFLDFSCIAKVSPPLRTHEDIEATRWALASGIIDFVATDHAPHAHYEKMQELQACPPGMLGLQFALPIVLELVKKDYFDLNRMVEVMSIQPAKKIGLKPPQIKEGEIAELTIFDPFETWEVNKETILSKSKNTPLLGRKLTGKVKYTFFKGKIVYRD | 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 pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
EC: 3.5.2.3
|
Q2LVI3 | MKILLKGGRVIDPAQNLDGQMDLLLENGKIAAIAEAVGSVPEDTRLLDLKGMILLPGLVDMHTHLREPGYEYKETIRSGSEAAAVGGFTSIACMPNTLPVNDNRTVTEYILKRAKECDTVHVYPVAAVSRNSEGKILAEFGDLKEAGAIAFSDDGKPVMNSILMRRALEYASSLDRIIISHCEDLNLSAGGLMNEGKISTELGLPGIPTLAEDVMVARDLLLAEFSGAALHIAHVSSAGAVRMIRDAKKRGVRVTAETTPHYFTLTDEAVTNFNTNTKVSPPLRSREDLQAVREGLRDGTLDAIVTDHAPHALTDKEVEFEYAANGISGLETALALSLTLVDDGLLTLSELVRKMSVNPAKILNIPKGTLRPGADADITVLNPGKTWVVDPSNWRSQGKNTPFFGWTLKGKVIMTLVQGRIVYQED | 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 pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
EC: 3.5.2.3
|
A0LK22 | MKKGKADPCNYLFRRARVIDPARDLDAVADVLVVDGILTDIKPNIDLPSDRLAHFAVIDASEKWIVPGLIDMHVHLREPGEEYKETIATGTMAAVAGGYTAVACMPNTKPVNDCAAVTEYILERAREQGHCRVLPVGAVSSGLEGRSLAEFGELKGSGAVAVTDDGRPVANSMLMRRALEYAKNFDLPVISHAEDPALSEGGLMNEGPTSTLLGLHGIPKAAEEVMVARDLALAELTGARLHIAHVSTAGAVRMIGEAKSRGVPVTAETAPHYFTLTDDRLMTFDTLYKVNPPIRGPADVEAIKRGLADGTIDAVATDHAPHSSIEKDTEFEYAANGIIGLESALPLILELVREKTLTPSQAVAKVSCNPARILGLPLGTLLLNQRACMTYLDPEFYFVLDCTTFRSKSRNCPFHGQPTRGRALMTFFNGKVAFSRLSK | 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 pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
EC: 3.5.2.3
|
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; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
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; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
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; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
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; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
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; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
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; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
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; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
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; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
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; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
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; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
Q2SCG9 | MSYQLARQFLFRLPAEASHNISLKMLKMADNAGMLGMFMPQMYSRPVELMGITFPNAVGLAAGLDKNGDYIDGLSKLGFGFIEVGTVTPKPQDGNPPPRLFRLEERSAIINRMGFNNYGVDYMTERLRKKKYGGVIGVNVGKNKDTPAEEAASDYIACINKVYPYASYITINISSPNTPGLRALQFGDSLRSMLQEIKDCQERMNQQHGRYVPFVVKIAPDMSDDEVHMVARTLLDYNMDGAIATNTTLSREGVESLAHGKEQGGLSGAPLTKRSTHVVKELCVALEGRIPVIASGGVMSAQDAVDKVRAGAKLVQVYSGLIYRGPVLVREAAEAIGGLDG | 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 metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
A1WTJ3 | MYALIRQLLFRLEPEQAHRVSMQLARLGLRIAAVPGVRSLPAVPRRVMGIDFPNPVGLAAGFDKDGEYMDVLEQLGFGFLELGTVTPRAQPGNPQPRVFRIPEHEALINRMGFNNQGAEPLVRRLEVSRHRGVVGINIGKNRDTPPERAVEDYAQALGMVYGVADYVAVNLSSPNTPGLRDLQHEGALRNLIDRLQTERKRLAELHDKRVPLVVKIAPDWEAGELDATLDILLERRVDGIVATNTTLGRTGVEQTPQARESGGLSGAPLREQAEWVLEQVAARRDRRTALIAAGGIMSGEDVTRRLDLGADLVQLYTGMIYRGPGLVQEAVRAAARHAGQPA | 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 metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
Q5UYF1 | MRPYDIAKPFLFSLPAETANKSVHRLLETVDGTRVADVMADRYTVADERLAVEAFGHTFDNPVGVAAGFDKNATIPETLASLGFGFAEVGGVTAEPQAGNARPRMFRLKADEAIINRMGLNNDGAIVIGERLKNVDAPFPVGVNIAKTEHVGTNEAPDDYRTTYEHVAEGGDFFVVNVSCPNSEGFEELQNRDAMEAILSELQDAGAAPLLVKLSPDLPEPAVEDALDLVTELDLDGVVATNTTTERPASLRSPNAVETGGLSGKPIENQATEMVRFVAERVDVPVVGVGGVSTAEGAYRKIRAGASLVQLYTGLVYRGPSIAREINSGLRDLLAEDGFDSVEDAVGADL | 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 metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
Q17WU9 | MLYSLFKKYLFRLDAEEVHEKVCKILKILSRSPFFCNLIHAQFGYTNPKLENEILGLHFPNPLGLAAGFDKNASMIRALTAFGFGYLEAGTLTNTAQSGNEKPRLFRHIEEESLQNAMGFNNYGAVLGVRAFERFAPYKTPIGINLGKNKHIEQDNALEDYKAVLIKCLNIGDYYTFNLSSPNTPNLRDLQNKAFVSELFCMAKEMTKKPLFLKIAPDLEIDAMLEITNSAIEAGANGIIATNTTIDKSLVFAPKETGGLSGKCLTQKSREIFKELAKAFFNKTILVSVGGISDAKEAYERIKMGASLLQIYSAFIYNGPNLCQNILKDLVKLLQKDGFLSVKEVIGADLR | 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 metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
O25655 | MLYSLVKKYLFSLDAEDAHEKVCKILRMLSSSPFLCNLIDSQWGYQNPKLENEILGLHFPNPLGLAAGFDKNASMLRALMAFGFGYLEAGTLTNEAQVGNERPRLFRHIEEESLQNAMGFNNYGAILGVRSFKRFAPYKTPIGINLGKNKHIEQAHALEDYKAVLSKCLNIGDYYTFNLSSPNTPNLRDLQNKAFVHELFCMAKEMTHKPLFLKIAPDLETDDMLEIVNSAIGAGAHGIIATNTTIDKSLVFAPKEMGGLSGKCLTKKSREIFKELAKAFFNKSVLVSVGGISDAKEAYERIKMGASLLQIYSAFIYNGPNLCQNILKDLVKLLQKDGFLSVKEAIGADLR | 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 metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
Q02127 | MAWRHLKKRAQDAVIILGGGGLLFASYLMATGDERFYAEHLMPTLQGLLDPESAHRLAVRFTSLGLLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVNLGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQERDGLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFGGVTDAIGADHRR | 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 mitochondrial targeting and proper membrane integration.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 42867
Sequence Length: 395
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Mitochondrion inner membrane
EC: 1.3.5.2
|
Q5SK69 | MHRFLFALDPEAAHGLALGLLALWSERGPLLEVPARLLRVEDPRLRVEAFGVSFPNPLGLAAGMDKDARALGAWWALGFGFAEVGTLTPRPQVGNPKPRLFRLVEDRALINRMGFNNRGAEEAARRLKRSRQRGLPLPIGVNLGKNRDTPLGRAAEDYLKALRLLEPFGDYFVLNVSSPNTPGLRALQEGPFLDELLARLRPATKKPLLLKVAPDLSPKALDEVLALAKKHRLQGLVAVNTTLAREGLKSPWAKEAGGLSGRPLKGRALEVLRHLAEGAEGLALVSVGGVETPLDLWERLKAGASLVQVYTGFVYGGPLFPRRLLLGLLRLMEAEGVSSLGELRRA | 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 metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
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: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.
Subcellular Location: Cytoplasm
EC: 1.3.98.1
|
A1WJ81 | MPLLPYALTRPFLFGLDAEAAHELIIDLLARGQRTPLQWAWCNQTVDDPIELAGLRFPNRVGLAAGLDKNARCIDALGAMGFGFVEAGTVTPQAQPGNPRPRMFRLPEARALINRLGFNNAGLQAFVHNLQQSRLRAAGSALRLGLNIGKNASTPMAQASSDYLACLEGVYPHADYVALNISSPNTQNLRTLQGDAALDHLLGAIAERRATLAARHGRRVPVFVKIAPDLDEAQLSLMAATLQRHGIDGVIATNTTIDRAVVQGQRHAQESGGLSGAPVLQASNQVIGQLRAALGKGFPIIGVGGIMSAEDAVSKIRAGADLVQIYTGLIYEGPALVVQAARAIKAMGGCGPVIALPNRS | 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 metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
Q8D370 | MIYKIINFILSKKDHEEKKDLLLKIMKFFNKTPLNFLIKNKFPNNNISCMGLNFKNILGLAAGLDKNGDYIKLFSDIGFGFIELGTVTLKPQHGEKKPRLFCFPNVYGIINRMGFNNNGIENLIENIKNEKNVKSILGINIGKNKDTLIEKAKDDYLICINKAYYYSDYISINISSPNTKDLRKLQFGELFSDLLKSIKEEQNKLNKIYNKYVPILIKISPDINNSEIIQISDCLLSYNIDGVIATNTTVNKDIIMRCCNNCEKGGLSGAPLNENSTRIIKKLSKELKGKIPIIGSGGIISVKSAKEKIKAGASLIQIYSGLVFFGLKIIKKLIKSF | 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 metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
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: 211
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
EC: 2.4.2.10
|
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: 192
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
EC: 2.4.2.10
|
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: 196
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
EC: 2.4.2.10
|
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: 203
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
EC: 2.4.2.10
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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: 4.1.1.23
|
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: 4.1.1.23
|
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
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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
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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
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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: 4.1.1.23
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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
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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
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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: 4.1.1.23
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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: 4.1.1.23
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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: 4.1.1.23
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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
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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
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O29987 | MKYIVVTGGVMSGLGKGITAASIGRLFVDMGYRVIPIKIDPYINIDAGTMNPFQHGEVYVLKDGTEVDLDLGHYERFIGEEVTGDHNITTGKIYKRVIEKERKGDYLGQTVQIIPHVTDEIKSWIRRVAKESNAEICLVEIGGTVGDIEGMPFLEAIRQMHNEEKEEDFALVHVTLVPLDAGGEQKTKPTQHSVKELRELGLHPDVIVGRCSERLKPATKKKIALFCDVPEEAVISNEDAEDIYEVPLIFKREKLDEYLMRKLNLRAKESRKEWEEMVKRMKTLYEEASIAIVGKYVDVRDAYLSIKEALKHGGIEAGCKVNIVWVDSEDLENVDDFTLDVDGILVPGGFGARGAEGKIRAIEYARENGVPFLGICFGFQLAVIEFARNVVGFSEANSTELDENTPHPVIDLLPEQKGIDEMGGTMRLGDIEVTIKPGTIAHKLYGSEKVVERHRHRYEVNPEYIEKIESKGLVFSAYSDGGRRMEIAELPDHPFFFATQFHPEFKSRPYRPSPPFVGFVRAALKYRREEEI | 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
Sequence Mass (Da): 59971
Sequence Length: 532
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
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G0HV10 | MPTEPETDYDPELGRKFIFVTGGVMSGLGKGITAASTGRLLKNAGFDVTAVKIDPYLNVDAGTMNPFQHGEVYVLKDGGEVDLDLGNYERFLDIDMTFDHNVTTGKTYQHVIEKERSGDYLGRTVQIIPHITDDIKRRIREAAEGNDVCIIEVGGTVGDIEGMPYLEALRQFAHEEDEDDILFTHVTLVPYSKNGEQKTKPTQHSVKELRSIGLQPDILVGRCSDKLDIDTKEKIALFCDVPTEAVFSNPDVDDIYHVPLMVEEEGLDQYVMEELDIATEALPEDERENRWRDLVTQNTEGEVDIALVGKYDLEDAYMSVHEALKHAGLEKNVDVNVQWVNSEKMNDHHADRMREADAIVVPGGFGARGTEGKIEAIRYARENDIPFLGLCLGFQMAVVEYARNVLDLDDAHSAELDEDTPHPVIDILPEQYEIEDMGGTMRLGAHETEIDANTLAATLYGGESCTERHRHRYEVNPEYIDDLEAAGLKFSGYAENRMEILELAPEDHPYFIGTQFHPEFRSRPTRASPPFVGLLEAVLGDDPHTVTTEEVSH | 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
Sequence Mass (Da): 61893
Sequence Length: 553
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.2
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O25116 | MDRAKFIFVTGGVLSSLGKGISSSSIATLLQHCNYQVSILKIDPYINIDPGTMSPLEHGEVFVTSDGAETDLDIGHYERFLNRNLTRLNNFTTGQIFSSVIENERKGEYLGKTIQIVPHVTDEIKRRIKSAAKGLDFLIVEVGGTVGDMEGMFYLEAIRQLKLELGNEKVINVHVTLIPYIQTTNELKTKPTQHSVQELRRLGVTPQIILARSPKPLDKELKNKIALSCDVEQDSVIVATDTKSIYACPILFLQEGILTPIARRFNLNKLHPKMAAWNTLVEKIIAPKHKVKIGFVGKYLSLKESYKSLIEALIHAGAHLDTQVNIEWLDSENFNEKTDLEGVDAILVPGGFGERGIEGKICAIQRARLEKLPFLGICLGMQLAIVEFCRNVLGLKGANSTEFNQRCEYPVVYLIGDFMDQNHQKQVRTYNSPLGGTMRLGEYECEIMPNSLLEKAYKKPSIKERHRHRYEINPKYRQEWENKGLKVVGFGSNHLIEAIELEDHPFFVGVQFHPEFTSRLQSPNPIILDFIKSALSKS | 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
Sequence Mass (Da): 60616
Sequence Length: 538
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
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Q4FM39 | MARYIFVTGGVVSSLGKGLSSASLAYLLQSRGYKVRIRKLDPYLNVDPGTMSPFQHGEVFVTDDGAETDLDLGHYERFSGVSAKKSDNITTGKIYSDVLRKERKGEYLGKTVQVIPHITDRIKQFIKHDSSKEDFVICEIGGIVGDIESLPFVEAIRQFANDVGKKNALFIHLTLVPYLKASDEIKTKPTQHSVKELRSIGIQPDIIICRSERPIPLDHRKKISLFCNVDIKNVIETVDVRTIYEAPMSFFKEKLDLQVLNYFKLKSKKPANLNPWKKITKIILHNKKQVNIAIIGKYVELKDAYKSLDEALTHGGIDNKVKVNLVRIDSEKLKISEIKKKLKNISGILIPGGFGKRGTDGKIEAIKHARLNKIPFLGICYGMQMAIIEFARNQLNLKNATSSEFDKKGLPIIGLINEWTKDGKKIKGTDKDLGGTMRLGSYDAKLKDNSKISKIYKSKLIKERHRHRYEVNIAFKDKFEKKGMIFSGLSPDNKLPEIIELKNHPWFIGVQFHPEFKSRPLAPHPLFSSFIKAAKNHK | 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
Sequence Mass (Da): 60881
Sequence Length: 538
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
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Q6L1K7 | MHYIVITGGVISGLGKGTITSSLSYLLKNSGFKVTNIKIDPYINYDAGTMNPYQHGEVFVLDDGSEVDLDLGNYERFLDTDLTGNNNITTGKIYKSVIERERHGDYLGKTVQIIPHITNEIKERIKRASSGYDIALIEVGGTVGDIESMPFIEAVRQLRSTDDVIYSHVTLVPEINGEQKTKPTQHSVKELRSLGISPDILFCRSEKPLGKDVIEKISLFTDVPASGIISMYNVKNVYMIPEIMMRQGILEYIKKRTGTSNHNLDYTWSNFVENIKNPAESVDIAIVGKYIELQDAYISHKEAFSHVTGNTGISVNIHWVDADKLLNSTHDLKNVDGILVPGGFGYRGVEGKIIAARYARENRIPYLGICLGFQVSVIEISRSLLGLKGANSTEFDNNTDYPVIDILPEQSNVSDLGGTMRLGSKKVLIKDGTIAKNIYKSDIIYERHRHRYEVNPDYIERLEDSGVIFSGTDDEKIRMEILELSDRDNYIATQYHAEFKSRPLNPSKVHMHLVLKALEYRRNIYERNTSGISR | 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
Sequence Mass (Da): 60050
Sequence Length: 534
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
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Q9PQK7 | MEIDLMKHIQKTKFIFVTGGVYSSLGKGVSASSIGRILVELGYSVAMQKLDPYLNIDPTYLSPLQHGEVFVTKDGKEADLDLGTYERFINADLNKYASVTSGKIYYEILTKERENGFDGKTVQTIPHVTSAVIDYIKKIKDSLKTDFIIVEIGGTIGDIESLPFIEAISQFKTIYGVNNVMFIHCSPLIYIEKVGELKTKPTQHSVKTLRSLGINLDLLLLRTNQKLDEVTIKKLAWSCGLDIDMIFAAYDVESVYLLPNVLFEQGIHKTILDFFSLPLKNDNINSWIDFTDKITTFKKHNLVIGLVGKYVELPDAYKSVLASLELAAIELNIDLKIKYIQPQNLNENNINEELKKINGIVIPSIAGSIKGWPGALLAASYARKNNIPFLAVGTGVNIGIGEFINNVLKLPIEFINLGNGDFSFLKDAFVKNEIENYRIGEYCSNIQANTITSQIYLKQNQLNERHRHHFEFNNHYINNYFLNQNWKIGAISVDNNYIDVLEYTKNHFYVLTIFNPEYTSKPSKANPYFINLLKMSLKIKES | 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
Sequence Mass (Da): 61347
Sequence Length: 542
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
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Q73HS5 | MKEAKFIFVTGGVVSSLGKGLVASSVGALLQAHGFKIRIRKLDPYLNIDPGTMNPTQHGEVFVTEDGAETDLDLGHYERFTGIKATKDDNITTGKIYHELLKKERRGDYLGKTVQVIPHVTDLIKSFIFNGTEGLDFVICEIGGTVGDIESQPFLEAIRQVNYTLGKQRVILIHLTLIPYLAAAQELKTKPTQHSVRELNSAGLQPDIILCRSEKEIFDNQREKIAKLCNVSLSNVIPAPDVSHIYELPVLYSQCGLDTQILEHFHLSKPKPSLTEWDQIVHSIRHPTQEVTVSIVGKYTEFPDAYKSLVEALNHGAISNKVKVKINWVNSREKEEKPIGEKLQNSHAILVPGGFGDDGVEGKILAINYARTNNIPFFGICLGMQLAIIEFARNVVKLEDAHSEEFRNCKHPIVKLAGDQDDDLGGTMRLGAYKCNINANSKMMDAYSNTTISERHRHRYIINSDYKDDLEKNGLLCSGISEDGTCIEAVELESHPWFIGVQFHPEFQSKPFSPHPLFVSFVKAAIDKK | 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
Sequence Mass (Da): 59028
Sequence Length: 529
Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
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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
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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
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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
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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
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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
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9906
Sequence Length: 82
Subcellular Location: Mitochondrion inner membrane
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 11776
Sequence Length: 107
Subcellular Location: Mitochondrion inner membrane
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 10467
Sequence Length: 92
Subcellular Location: Mitochondrion inner membrane
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 10975
Sequence Length: 94
Subcellular Location: Mitochondrion inner membrane
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8449
Sequence Length: 72
Subcellular Location: Mitochondrion inner membrane
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7458
Sequence Length: 64
Subcellular Location: Mitochondrion inner membrane
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7337
Sequence Length: 66
Subcellular Location: Mitochondrion inner membrane
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6294
Sequence Length: 55
Subcellular Location: Mitochondrion inner membrane
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7308
Sequence Length: 63
Subcellular Location: Mitochondrion inner membrane
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7750
Sequence Length: 69
Subcellular Location: Mitochondrion inner membrane
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7446
Sequence Length: 64
Subcellular Location: Mitochondrion inner membrane
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6861
Sequence Length: 59
Subcellular Location: Mitochondrion inner membrane
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7800
Sequence Length: 67
Subcellular Location: Mitochondrion inner membrane
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8048
Sequence Length: 72
Subcellular Location: Mitochondrion inner membrane
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7476
Sequence Length: 66
Subcellular Location: Mitochondrion inner membrane
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O94710 | MLCLVYNSILCKQRRISLKVLQQFRCWNISKTFLSYRTLTALAIETSCDDTSVSVVRTSDSSSHCQNEIICLNTHRTISKYEAYGGIHPTIVIHEHQKNLAKVIQRTISDAARSGITDFDLIAVTRGPGMIGPLAVGLNTAKGLAVGLQKPLLAVHHMQAHALAVQLEKSIDFPYLNILVSGGHTMLVYSNSLLNHEIIVTTSDIAVGDYLDKCAKYLGIPWDNEMPAAALEQFASPEINSTSYSLKPPIPLNTREKVHSASFSFSGLESYACRIIRKTPLNLSEKKFFAYQLQYAAFQHICQKTLLALKRLDLSKVKYLVCSGGVARNELLKKMLNDTLMVLQFEHQPTDIKLVYPSPDICSDNAAMIGYTAIQMFKAGYTSSFDVEPIRKWPINQILTVEGWLTKKNKKV | 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) to the N6 group of A37. Involved in mitochondrial genome maintenance.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 45973
Sequence Length: 412
Subcellular Location: Mitochondrion
EC: 2.3.1.234
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P43122 | MISIKGTGRFLLDNYRIWQRRAFNRPIQLRKGYKVLAIETSCDDTCVSVLDRFSKSAAPNVLANLKDTLDSIDEGGIIPTKAHIHHQARIGPLTERALIESNAREGIDLICVTRGPGMPGSLSGGLDFAKGLAVAWNKPLIGVHHMLGHLLIPRMGTNGKVPQFPFVSLLVSGGHTTFVLSRAIDDHEILCDTIDIAVGDSLDKCGRELGFKGTMIAREMEKFINQDINDQDFALKLEMPSPLKNSASKRNMLSFSFSAFITALRTNLTKLGKTEIQELPEREIRSIAYQVQESVFDHIINKLKHVLKSQPEKFKNVREFVCSGGVSSNQRLRTKLETELGTLNSTSFFNFYYPPMDLCSDNSIMIGWAGIEIWESLRLVSDLDICPIRQWPLNDLLSVDGWRTDQL | 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) to the N6 group of A37. Involved in mitochondrial genome maintenance.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 45543
Sequence Length: 407
Subcellular Location: Mitochondrion
EC: 2.3.1.234
|
Q2TAL8 | MNNSLENTISFEEYIRVKARSVPQHRMKEFLDSLASKGPEALQEFQQTATTTMVYQQGGNCIYTDSTEVAGSLLELACPVTTSVQPQTQQEQQIQVQQPQQVQVQVQVQQSPQQVSAQLSPQLTVHQPTEQPIQVQVQIQGQAPQSAAPSIQTPSLQSPSPSQLQAAQIQVQHVQAAQQIQAAEIPEEHIPHQQIQAQLVAGQSLAGGQQIQIQTVGALSPPPSQQGSPREGERRVGTASVLQPVKKRKVDMPITVSYAISGQPVATVLAIPQGQQQSYVSLRPDLLTVDSAHLYSATGTITSPTGETWTIPVYSAQPRGDPQQQSITHIAIPQEAYNAVHVSGSPTALAAVKLEDDKEKMVGTTSVVKNSHEEVVQTLANSLFPAQFMNGNIHIPVAVQAVAGTYQNTAQTVHIWDPQQQPQQQTPQEQTPPPQQQQQQLQVTCSAQTVQVAEVEPQSQPQPSPELLLPNSLKPEEGLEVWKNWAQTKNAELEKDAQNRLAPIGRRQLLRFQEDLISSAVAELNYGLCLMTREARNGEGEPYDPDVLYYIFLCIQKYLFENGRVDDIFSDLYYVRFTEWLHEVLKDVQPRVTPLGYVLPSHVTEEMLWECKQLGAHSPSTLLTTLMFFNTKYFLLKTVDQHMKLAFSKVLRQTKKNPSNPKDKSTSIRYLKALGIHQTGQKVTDDMYAEQTENPENPLRCPIKLYDFYLFKCPQSVKGRNDTFYLTPEPVVAPNSPIWYSVQPISREQMGQMLTRILVIREIQEAIAVANASTMH | 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 translation by a ribosome translation re-initiation mechanism in response to EIF2S1/eIF-2-alpha phosphorylation, and stress-induced QRICH1 regulates a transcriptional program associated with protein translation, protein secretion-mediated proteotoxicity and cell death during the terminal UPR . May cooperate with ATF4 transcription factor signaling to regulate ER homeostasis which is critical for cell viability . Up-regulates CASP3/caspase-3 activity in epithelial cells under ER stress. Central regulator of proteotoxicity associated with ER stress-mediated inflammatory diseases in the intestines and liver . Involved in chondrocyte hypertrophy, a process required for normal longitudinal bone growth .
Sequence Mass (Da): 86436
Sequence Length: 776
Domain: The CARD domain may be involved in the regulation of caspase activity in the context of programmed cell death.
Subcellular Location: Nucleus
|
Q9SFB7 | MYEKIIILSVFLLTFLPSCFSSYPFNHRDDLFMSSNVYYETNRQHQHGHNTRNSHLKNRHGYAPRSSPRSFNVNTFGAKANGNDDSKAFMKAWEAACSSTGIVYIVAPKNRDYMLKAVTFSGPCKSSLIIFKIYGRIEAWENPSDYKERRHWIVFENVNNLRVEGGGRIDGNGHIWWPKSCKINPQLPCLGAPTAVTFVECNNLRVSNIRLENAQQMHLTFQDCKNVKALNLMVTSPADSPNTDGIHVSGTQNILIQDSIVRTGDDCISIVSGSENVRATGITCGPGHGISIGSLGEDNSEAYVSNVVVNKATLIGTTNGVRIKTWQGGHGMAKNIIFQDIIMKNVTNPIIINQDYCDRVEACPEQKSAVQVSNVLYKNIQGTSSRPIAVKFVCSKNIPCRGISMQNVKLVDQTQQDVSKASCSNVKLDTRGNVSPLCT | 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 Length: 439
Subcellular Location: Secreted
EC: 3.2.1.15
|
O49432 | MELRKSQVAMPVFLAIMSLMVSQVVFAEKDSGSMSPHDRALAEMQALKASLVRRNLPALVSPPPTPPQAVPGPRVYQVISYGADPTGKLDSTDAILKAMEEAFDGPNHGVLMQGINDLGGARIDLQGGSYLISRPLRFPSAGAGNLLISGGTLRASNDFPVDRYLIELKDESSKLQYIFEYITLRDLLIDCNYRGGAIAVINSLRTSIDNCYITRFGDTNGILVKSGHETYIRNSFLGQHITAGGDRGERSFSGTAINLMGNDNAVTDTVIFSARIGVMVSGQANLLSGVHCYNKATGFGGTGIYLRLPGLTQNRIVNSYLDYTGIVAEDPVQLQISGTFFLGDAFILLKSIAGYIRGVSIVDNMFSGSGHGVQIVQLDQRNTAFDDVGQVVVDRNSVNGMVEKSTVARGSVDGNGTSWTVDFNPVLLFPDLINHVQYTLVASEAGVFPLHALRNVSDNRVVVETNAPVTGTVYVTVNQGV | 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: 3.2.1.15
|
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 | MKFTQRLSLRVRLTLIFLILASVTWLLSSFVAWKQTTDNVDELFDTQLMLFAKRLSTLDLNEINAADRMAQTPNRLKHGHVDDDALTFAIFTHDGRMVLNDGDNGEDIPYSYQREGFADGQLVGEDDPWRFVWMTSPDGKYRIVVGQEWEYREDMALAIVAGQLIPWLVALPIMLIIMMVLLGRELAPLNKLALALRMRDPDSEKPLNATGVPSEVRPLVESLNQLFARTHAMMVRERRFTSDAAHELRSPLTALKVQTEVAQLSDDDPQARKKALLQLHSGIDRATRLVDQLLTLSRLDSLDNLQDVAEIPLEDLLQSSVMDIYHTAQQAKIDVRLTLNAHSIKRTGQPLLLSLLVRNLLDNAVRYSPQGSVVDVTLNADNFIVRDNGPGVTPEALARIGERFYRPPGQTATGSGLGLSIVQRIAKLHGMNVEFGNAEQGGFEAKVSW | 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 (Da): 50282
Sequence Length: 449
Subcellular Location: Cell inner membrane
EC: 2.7.13.3
|
P45336 | MKNRSLTLRLISVLCLTALFVWLGSTLVAWWQVRHDVNKVFDAQQVLFAERLANSDLSTILLESSTTLNKNSQSVLKKSYDDDALAFAIFSKTGKLLFSDGRNGKDFIFNYKTGFYNANIYDDDDKWRIFWRMAANGELVIAVGQELDYREDLIEEMILGQMWIWFASLPILIIVLGWLIHKELRPIKRLSQEVQTRKSGDVSLLNTEGLPVEILPLVKNLNQFFDRTSAMLQRERRFTSDAAHELRSPLAALRIQIEVAQLAGDDVALREQALLHLTQGIDRASQLIEQLLTLSRLDNLQALETLQLLDWEAIVQSLISERYFVAEKRKITLVFEKESEPKQKQGQSILVSLMLRNLLDNAIKYCPEDTIVSVKISSSQIIIEDNGGGVEPEDLKKLGQRFYRPAGQNEKGSGLGLSIVMRIAELHGFKVRLENVVKEGRRIGLKAIISL | 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: Cell inner membrane
EC: 2.7.13.3
|
Q6LU70 | MQVSDFHFDLPNELIARYPQPERTASRLLQLTGETGNIQHKGFKDVLDLAESGDLFVFNNTRVIPARIFGRKASGGKIEVLVERILDDKSILAHVRASKSPKPGNELLLGENDDYQAEMIARHDTLFEIRFNSDKTVLEILEEVGHMPLPPYIDRPDEDADKERYQTVYNAKPGAVAAPTAGLHFDDKLMAALKAKGVNFAFVTLHVGAGTFQPVRVDNIDDHHMHSEYVEVPQDVVDAVNATKANGGRIIAVGTTSVRSLESAAQDAVKKGTELVPFFGDTEIFIFPGYEFQLVDVLVTNFHLPESTLIMLVSAFAGYEHTMNAYLQAVDNKYRFFSYGDSMFITRRNNV | 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 Mass (Da): 39148
Sequence Length: 351
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.4.99.17
|
A6KZK0 | MKLSQFKFKLPEDKIALHPAKYRDESRLMVVHKSTGKIEHKVFKDILDYFDDKDVFIFNDTKVFPARLYGNKEKTGARIEVFLLRELNEELRLWDVLVDPARKIRIGNKLYFGDDDSMVAEVIDNTTSRGRTLRFLYDGSHDEFKKALYALGEAPLPSFIRRPVEEEDAERFQTIFAKNEGAVTAPTAGLHFSRELMKRMEIKGIDFAFVTMHAGLGNFREIDVEDLTKHKMDSEQMYVNADACRIVNNAKDEGKNICAVGTTVMRTIETAVGTDGHLKEFDGWTNKFIFPPYDFSVANSMVTNFHLPLSTLLMLVAAYGGYDLVMEAYHTALKEDYRFGTYGDAMLILDK | 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 Mass (Da): 40180
Sequence Length: 351
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.4.99.17
|
A2BV65 | MNFEIYNEEIDHKLEAYDYCLDESLIAGKPSKVRHESRLMIVRDSSLKEDYSTNKYTKDLLAELREGDLVVINDTKVMKARLKVELENGQLVELLVLEKSDQSTWLCLAKPAKKLKINKQLNLKSPFAKDIKLKISGIDDETGGRFIKFPENINDLISMNKLLDIFGEIPIPPYIKSSEEESFHENSYQTEYACNPGAVAAPTAGLHLSKSLISNLKKKGILVMPITLHVGYGTFKPIDQEDLSDLKLHKEWVSVSKKVVEEIKRIKKTDRRVIAIGTTSVRALESCYSYAMKDFIPIAKYVDLVIKPGYKFKAVDGLLTNFHLPKSSLLLLVSAMIGRERLLDLYKKATKEKFRFFSYGDAMYISPDSFLEK | 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 Mass (Da): 42471
Sequence Length: 373
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.4.99.17
|
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: 220
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 202
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 233
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 210
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 229
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 237
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 229
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 228
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 235
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 242
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 228
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 226
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 232
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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: 238
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 6.3.4.20
|
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 biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.7.1.13
|
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