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Database: UniProt
Entry: G0V7T7_NAUCC
LinkDB: G0V7T7_NAUCC
Original site: G0V7T7_NAUCC 
ID   G0V7T7_NAUCC            Unreviewed;      2213 AA.
AC   G0V7T7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   13-SEP-2023, entry version 61.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCC67535.1};
GN   Name=NCAS0A09770 {ECO:0000313|EMBL:CCC67535.1};
GN   OrderedLocusNames=NCAS_0A09770 {ECO:0000313|EMBL:CCC67535.1};
OS   Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS   1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC67535.1, ECO:0000313|Proteomes:UP000001640};
RN   [1] {ECO:0000313|EMBL:CCC67535.1, ECO:0000313|Proteomes:UP000001640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC   {ECO:0000313|Proteomes:UP000001640};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain:CBS 4309;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Genome sequence of Naumovozyma castellii.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC         carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:456216; EC=6.3.5.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001777};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC         aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58228; EC=2.1.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001363};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004812}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00004852}.
CC   -!- SIMILARITY: In the central section; belongs to the metallo-dependent
CC       hydrolases superfamily. DHOase family. CAD subfamily.
CC       {ECO:0000256|ARBA:ARBA00008454}.
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DR   EMBL; HE576752; CCC67535.1; -; Genomic_DNA.
DR   RefSeq; XP_003673916.1; XM_003673868.1.
DR   STRING; 1064592.G0V7T7; -.
DR   MEROPS; C26.956; -.
DR   GeneID; 11529210; -.
DR   KEGG; ncs:NCAS_0A09770; -.
DR   eggNOG; KOG0370; Eukaryota.
DR   HOGENOM; CLU_000513_2_1_1; -.
DR   InParanoid; G0V7T7; -.
DR   OMA; FTGDLRY; -.
DR   OrthoDB; 309at2759; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001640; Chromosome 1.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   CDD; cd01423; MGS_CPS_I_III; 1.
DR   Gene3D; 3.40.50.20; -; 2.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR   Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR   Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR   HAMAP; MF_00001; Asp_carb_tr; 1.
DR   HAMAP; MF_01209; CPSase_S_chain; 1.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR002082; Asp_carbamoyltransf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR   InterPro; IPR006274; CarbamoylP_synth_ssu.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR035686; CPSase_GATase1.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   NCBIfam; TIGR00670; asp_carb_tr; 1.
DR   NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR   NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR   PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF02142; MGS; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00101; ATCASE.
DR   PRINTS; PR00098; CPSASE.
DR   PRINTS; PR00099; CPSGATASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR   SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR   SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
DR   PROSITE; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51855; MGS; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001640};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          557..749
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1094..1285
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1351..1502
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   ACT_SITE        297
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        381
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        383
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   2213 AA;  244635 MW;  17AC42C1D5C5050C CRC64;
     MSSVIPISPI TPSMESTGDR LITLELKDGI TLQGYSFGAE KSCAGELVFQ TGMVGYPESI
     TDPSYEGQIL VITFPLVGNY GVPDFNLEDE FVKELPRYFE SNRIHIAGLV IAHYTEKYSH
     WLAKSSLGKW LQDEGIPAVY GVDTRALTKH LRDSGSMLGR LALQKTSSSS NNWPSSFDIP
     EWVDPNVENL VATVSTKEPK LYLPPTDNEN ITIQKGPDGK TLRILAIDVG MKYNQIRCFI
     KRGVELKVVP WDYDFTKEEY DGLFISNGPG DPSVLKELTQ RLASVVDSKK TPIFGICLGH
     QLLARSTGAS TLKLKFGNRG HNIPCTSTIS GRCYITSQNH GFAVDVDTLT SGWEPLFYNA
     NDGSNEGIYH SELPYFSVQF HPESTPGPRD TEFLFDVFIN SVKEFKSTGV LKSVEFPGGK
     VEDNLRAHPR VEAKKVLVLG SGGLSIGQAG EFDYSGSQAI KALKEEGIYT ILINPNIATI
     QTSKGLADKV YFLPVTAEFV RKVILHERPD AIYVTFGGQT ALSVGIEMKD EFESLGVKVL
     GTQIDTIITT EDRELFANAI DEINEKCAKS HAANSVEEAL TAVKDIGFPV IVRAAYALGG
     LGSGFANNEQ ELIDLCNVAF ASSPQVLVER SMKGWKEIEY EVVRDAFDNC VTVCNMENFD
     PLGIHTGDSI VVAPSQTLSD EEYNMLRNTA VNVIRHLGVV GECNIQYALN PFSKEYCIIE
     VNARLSRSSA LASKATGYPL AYTAAKLGLN IPLNEVINSV TKSTCACFEP SLDYCVVKMP
     RWDLKKFTRV STELSSSMKS VGEVMSIGRT FEEAIQKAIR STEYANLGFN ETDLEIDIDY
     ELANPTDLRV FAIANAFSKL NYSIEKVWEL TKIDKWFLSK LYDLIQFGKK VTAVGAIEGF
     PSATLREAKQ LGFDDRQIAK FLNSNEVAIR RLRKDHGITP FVKQIDTVAA EFPAHTNYLY
     MTYNASSHDL SFDEHGVMVL GSGVYRIGSS VEFDWCAVTA VRTLRANKIK TIMINYNPET
     VSTDYDEADR LYFETINLER ILDIYEIENS SGVVVSMGGQ TSNNIAMSLH RENVKILGTS
     PEMIDSAENR YKFSRMLDQI GVDQPAWKEL TSMDEAESFA EKVGYPVLVR PSYVLSGAAM
     NTVYSKNDLA SYLNQAVEVS RDYPVVITKY IENAKEIEMD AVARNGELVM HVVSEHVENA
     GVHSGDATLI VPPQDLAKET VDRIVVATAK IGKALKITGP YNIQFIAKDN EIKVIECNVR
     ASRSFPFISK VVGVNLIELA TKAVMGLPFE PYPVEKLPDD YVAVKVPQFS FPRLAGADPV
     LGVEMASTGE VASFGHSKYE AYLKALKATG FKLPKKNILL SIGSYKEKKE LLPCVQKLYN
     MGFKLFATAG TADFISENGI PVQYLEVLNE DDEEKKEYSL TQHLANNEID LYINLPSANR
     YRRPASYVSN GYRTRRMAVD YSVPLVTNVK CAKLLIEALS RHIALDVSER DAQTSHRTVT
     IPGLINVTGY VPNASNVIKG PAELKETTRL CLESGFTFSQ IMPRSASGPT ITDSHSLKAA
     LSTAKDSSYT DFSLTVAGTS NNAEMIGSTS DQVSALFLPF HELKNKVSTV AELLKTWPIE
     KQVIAEAKTA DLASVLLLAS LQNRSIHITG VSNKEDLALI MTVKEKDPSV TCDVCIHSLF
     VTQEDYPEGV FLPTEEDQQF FWDNLDSIDA FSIGVLPTML AHVTGNKVDI GSGIKDALPL
     LLSAVEDGRL TIDDIVLRLH DNPIKIFNLP EQKAVVEIDL DYSFNNRKRW SPYTKGGLNG
     GIERVLVNDE TVVLSGDLIA IQPTGISVVK AQGSGPVSAN IEAPLGTSTA NKRKFSVFGE
     RPSFANVDEA EKYMDQPIEQ KLMSSRPPKE LVVPGALENL IRGNNPFLGR NILSVKQFSR
     SDLHVLFGVA EELRAAVARE GVLDLMKGHV MTTIFYEPST RTCSSFIAAM ERLGGRVVNI
     NPSVSSVKKG ETLQDTVRTL ACYSDAIVMR HPDEMSVHIA AKYSPVPIIN GGNGSREHPT
     QAFLDLFTIR EEIGTVNGIT VTFLGDLKHG RTVHSLCRLL LHYQVRINLV SPTELRIPEG
     LRKELKDAGL LGVESTELTP EIISKSDVLY CTRVQQERFK TQEDYEKFKN AYIIDNKVLA
     HAKENMAVMH PLPRVNEIKE EVDYDHRAAY FREMKYGLFV RMALLAMVMG VDI
//
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