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
//