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Database: UniProt
Entry: P07259
LinkDB: P07259
Original site: P07259 
ID   PYR1_YEAST              Reviewed;        2214 AA.
AC   P07259; A2TBN0; D6VW55; Q06HN1;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 5.
DT   13-FEB-2019, entry version 220.
DE   RecName: Full=Protein URA2;
DE   Includes:
DE     RecName: Full=Glutamine-dependent carbamoyl-phosphate synthase;
DE              EC=6.3.5.5;
DE   Includes:
DE     RecName: Full=Aspartate carbamoyltransferase;
DE              EC=2.1.3.2;
GN   Name=URA2; OrderedLocusNames=YJL130C; ORFNames=J0686;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX   PubMed=2570735; DOI=10.1016/0378-1119(89)90092-9;
RA   Souciet J.-L., Nagy M., le Gouar M., Lacroute F., Potier S.;
RT   "Organization of the yeast URA2 gene: identification of a defective
RT   dihydroorotase-like domain in the multifunctional carbamoylphosphate
RT   synthetase-aspartate transcarbamylase complex.";
RL   Gene 79:59-70(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N.,
RA   Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H.,
RA   Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A.,
RA   Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P.,
RA   Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L.,
RA   Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V.,
RA   Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M.,
RA   Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W.,
RA   Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M.,
RA   Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A.,
RA   Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M.,
RA   Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [3]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 123.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-510.
RC   STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX   PubMed=3039294; DOI=10.1007/BF00331595;
RA   Souciet J.-L., Potier S., Hubert J.-C., Lacroute F.;
RT   "Nucleotide sequence of the pyrimidine specific carbamoyl phosphate
RT   synthetase, a part of the yeast multifunctional protein encoded by the
RT   URA2 gene.";
RL   Mol. Gen. Genet. 207:314-319(1987).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-276.
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8948101;
RX   DOI=10.1002/(SICI)1097-0061(199611)12:14<1471::AID-YEA30>3.0.CO;2-4;
RA   Cziepluch C., Kordes E., Pujol A., Jauniaux J.-C.;
RT   "Sequencing analysis of a 40.2 kb fragment of yeast chromosome X
RT   reveals 19 open reading frames including URA2 (5' end), TRK1, PBS2,
RT   SPT10, GCD14, RPE1, PHO86, NCA3, ASF1, CCT7, GZF3, two tRNA genes,
RT   three remnant delta elements and a Ty4 transposon.";
RL   Yeast 12:1471-1474(1996).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-119.
RC   STRAIN=ATCC 201390 / BY4743;
RX   PubMed=17351133; DOI=10.1101/gr.6049107;
RA   Zhang Z., Hesselberth J.R., Fields S.;
RT   "Genome-wide identification of spliced introns using a tiling
RT   microarray.";
RL   Genome Res. 17:503-509(2007).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-117.
RC   STRAIN=ATCC 201390 / BY4743;
RX   PubMed=17244705; DOI=10.1073/pnas.0610354104;
RA   Juneau K., Palm C., Miranda M., Davis R.W.;
RT   "High-density yeast-tiling array reveals previously undiscovered
RT   introns and extensive regulation of meiotic splicing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 175-2214.
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8813765;
RX   DOI=10.1002/(SICI)1097-0061(19960630)12:8<787::AID-YEA954>3.3.CO;2-W;
RA   Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.;
RT   "Sequence analysis of a 40.7 kb segment from the left arm of yeast
RT   chromosome X reveals 14 known genes and 13 new open reading frames
RT   including homologues of genes clustered on the right arm of chromosome
RT   XI.";
RL   Yeast 12:787-797(1996).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 838-877.
RX   PubMed=9150260; DOI=10.1007/s004380050415;
RA   Akada R., Yamamoto J., Yamashita I.;
RT   "Screening and identification of yeast sequences that cause growth
RT   inhibition when overexpressed.";
RL   Mol. Gen. Genet. 254:267-274(1997).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1268-2214.
RX   PubMed=2498313;
RA   Nagy M., le Gouar M., Potier S., Souciet J.-L., Herve G.;
RT   "The primary structure of the aspartate transcarbamylase region of the
RT   URA2 gene product in Saccharomyces cerevisiae. Features involved in
RT   activity and nuclear localization.";
RL   J. Biol. Chem. 264:8366-8374(1989).
RN   [11]
RP   PROTEIN SEQUENCE OF 1855-1874, AND PHOSPHORYLATION AT SER-1857.
RX   PubMed=1977585; DOI=10.1111/j.1432-1033.1990.tb19376.x;
RA   Denis-Duphil M., Lecaer J.-P., Hardie D.G., Carrey E.A.;
RT   "Yeast carbamoyl-phosphate-synthetase--aspartate-transcarbamylase
RT   multidomain protein is phosphorylated in vitro by cAMP-dependent
RT   protein kinase.";
RL   Eur. J. Biochem. 193:581-587(1990).
RN   [12]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11015727;
RX   DOI=10.1002/1097-0061(200010)16:14<1299::AID-YEA593>3.0.CO;2-6;
RA   Benoist P., Feau P., Pliss A., Vorisek J., Antonelli R., Raska I.,
RA   Denis-Duphil M.;
RT   "The yeast Ura2 protein that catalyses the first two steps of
RT   pyrimidines biosynthesis accumulates not in the nucleus but in the
RT   cytoplasm, as shown by immunocytochemistry and Ura2-green fluorescent
RT   protein mapping.";
RL   Yeast 16:1299-1312(2000).
RN   [13]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [14]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1857, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1857, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass
RT   spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1857, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
RN   [19]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [20]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1853, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
CC   -!- FUNCTION: This protein is a "fusion" protein encoding three
CC       enzymatic activities of the pyrimidine pathway (GATase, CPSase,
CC       and ATCase).
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   -!- 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   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11015727,
CC       ECO:0000269|PubMed:14562095}.
CC   -!- DOMAIN: The DHOase domain is defective.
CC   -!- MISCELLANEOUS: GATase (glutamine amidotransferase) and CPSase
CC       (carbamoyl phosphate synthase) form together the glutamine-
CC       dependent CPSase (GD-CPSase) (EC 6.3.5.5).
CC   -!- MISCELLANEOUS: In eukaryotes EC 6.3.5.5 is synthesized by two
CC       pathway-specific (arginine and pyrimidine) genes under separate
CC       control.
CC   -!- MISCELLANEOUS: Present with 11000 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: In the central section; belongs to the metallo-
CC       dependent hydrolases superfamily. DHOase family. CAD subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABI95879.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; M27174; AAA68280.1; -; Genomic_DNA.
DR   EMBL; Z49405; CAA89425.1; -; Genomic_DNA.
DR   EMBL; X05553; CAA29068.1; -; Genomic_DNA.
DR   EMBL; DQ881452; ABI95879.1; ALT_INIT; mRNA.
DR   EMBL; EF123133; ABM97477.1; -; mRNA.
DR   EMBL; X87371; CAA60825.1; -; Genomic_DNA.
DR   EMBL; D28139; BAA05680.1; -; Genomic_DNA.
DR   EMBL; J04711; AAA35198.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08671.2; -; Genomic_DNA.
DR   PIR; S56911; QZBYU2.
DR   RefSeq; NP_012405.2; NM_001181563.2.
DR   SMR; P07259; -.
DR   BioGrid; 33626; 174.
DR   DIP; DIP-7215N; -.
DR   IntAct; P07259; 463.
DR   MINT; P07259; -.
DR   STRING; 4932.YJL130C; -.
DR   MEROPS; C26.956; -.
DR   CarbonylDB; P07259; -.
DR   iPTMnet; P07259; -.
DR   MaxQB; P07259; -.
DR   PaxDb; P07259; -.
DR   PRIDE; P07259; -.
DR   EnsemblFungi; YJL130C_mRNA; YJL130C_mRNA; YJL130C.
DR   GeneID; 853311; -.
DR   KEGG; sce:YJL130C; -.
DR   EuPathDB; FungiDB:YJL130C; -.
DR   SGD; S000003666; URA2.
DR   GeneTree; ENSGT00940000157241; -.
DR   HOGENOM; HOG000234584; -.
DR   InParanoid; P07259; -.
DR   KO; K11541; -.
DR   OMA; FTNANDH; -.
DR   BioCyc; MetaCyc:YJL130C-MONOMER; -.
DR   BioCyc; YEAST:YJL130C-MONOMER; -.
DR   BRENDA; 6.3.5.5; 984.
DR   Reactome; R-SCE-500753; Pyrimidine biosynthesis.
DR   Reactome; R-SCE-70635; Urea cycle.
DR   UniPathway; UPA00070; UER00115.
DR   UniPathway; UPA00070; UER00116.
DR   PRO; PR:P07259; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IDA:SGD.
DR   GO; GO:0004151; F:dihydroorotase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IDA:SGD.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IDA:SGD.
DR   GO; GO:0045984; P:negative regulation of pyrimidine nucleobase metabolic process; IDA:SGD.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR   GO; GO:0006228; P:UTP biosynthetic process; IBA:GO_Central.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.1370; -; 2.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.50.30.20; -; 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   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   SMART; SM01096; CPSase_L_D3; 1.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF48108; SSF48108; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   SUPFAM; SSF52021; SSF52021; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52335; SSF52335; 1.
DR   SUPFAM; SSF52440; SSF52440; 2.
DR   SUPFAM; SSF53671; SSF53671; 1.
DR   TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR   TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR   TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
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   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Isopeptide bond; Ligase;
KW   Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW   Pyrimidine biosynthesis; Reference proteome; Repeat; Transferase;
KW   Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22814378}.
FT   CHAIN         2   2214       Protein URA2.
FT                                /FTId=PRO_0000199511.
FT   DOMAIN      228    413       Glutamine amidotransferase type-1.
FT   DOMAIN      562    754       ATP-grasp 1.
FT   DOMAIN     1099   1290       ATP-grasp 2.
FT   DOMAIN     1356   1508       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   REGION        2    400       GATase (Glutamine amidotransferase).
FT   REGION      401    440       Linker.
FT   REGION      441   1482       CPSase (Carbamoyl-phosphate synthase).
FT   REGION     1483   1492       Linker.
FT   REGION     1493   1821       Defective DHOase domain.
FT   REGION     1822   1909       Linker.
FT   REGION     1910   2214       ATCase (Aspartate transcarbamylase).
FT   ACT_SITE    302    302       For GATase activity. {ECO:0000250}.
FT   ACT_SITE    386    386       For GATase activity. {ECO:0000250}.
FT   ACT_SITE    388    388       For GATase activity. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000244|PubMed:22814378}.
FT   MOD_RES    1857   1857       Phosphoserine; by PKA.
FT                                {ECO:0000244|PubMed:17287358,
FT                                ECO:0000244|PubMed:17330950,
FT                                ECO:0000244|PubMed:19779198,
FT                                ECO:0000269|PubMed:1977585}.
FT   CROSSLNK   1853   1853       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000244|PubMed:22106047}.
FT   CONFLICT     86     86       H -> D (in Ref. 4; CAA29068).
FT                                {ECO:0000305}.
FT   CONFLICT    123    123       A -> R (in Ref. 2; CAA89425).
FT                                {ECO:0000305}.
FT   CONFLICT    250    257       ELKVVPWN -> RIESCSMD (in Ref. 4;
FT                                CAA29068). {ECO:0000305}.
FT   CONFLICT    270    270       I -> Y (in Ref. 4; CAA29068).
FT                                {ECO:0000305}.
FT   CONFLICT    313    314       GA -> VQ (in Ref. 4; CAA29068).
FT                                {ECO:0000305}.
FT   CONFLICT    372    373       GI -> RF (in Ref. 4; CAA29068).
FT                                {ECO:0000305}.
FT   CONFLICT    394    402       RDTEFLFDV -> EIQNSCLT (in Ref. 4;
FT                                CAA29068). {ECO:0000305}.
FT   CONFLICT    431    433       KAH -> QGT (in Ref. 4; CAA29068).
FT                                {ECO:0000305}.
FT   CONFLICT    482    482       I -> T (in Ref. 4; CAA29068).
FT                                {ECO:0000305}.
FT   CONFLICT    485    485       I -> N (in Ref. 4; CAA29068).
FT                                {ECO:0000305}.
FT   CONFLICT    492    492       A -> G (in Ref. 4; CAA29068).
FT                                {ECO:0000305}.
FT   CONFLICT    501    510       TAEFVRKVIL -> NAAKQRDVDR (in Ref. 4;
FT                                CAA29068). {ECO:0000305}.
FT   CONFLICT   1411   1412       EV -> S (in Ref. 10; AAA35198).
FT                                {ECO:0000305}.
FT   CONFLICT   1582   1582       I -> M (in Ref. 10; AAA35198).
FT                                {ECO:0000305}.
FT   CONFLICT   1588   1588       N -> K (in Ref. 10; AAA35198).
FT                                {ECO:0000305}.
FT   CONFLICT   1592   1592       V -> G (in Ref. 10; AAA35198).
FT                                {ECO:0000305}.
FT   CONFLICT   1595   1595       S -> A (in Ref. 10; AAA35198).
FT                                {ECO:0000305}.
FT   CONFLICT   1872   1872       Missing (in Ref. 11; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT   1937   1937       A -> R (in Ref. 1; AAA68280 and 10;
FT                                AAA35198). {ECO:0000305}.
FT   CONFLICT   1997   1997       T -> I (in Ref. 10; AAA35198).
FT                                {ECO:0000305}.
FT   CONFLICT   2039   2039       H -> L (in Ref. 10; AAA35198).
FT                                {ECO:0000305}.
FT   CONFLICT   2158   2165       KILAHAKE -> VRSWHTQQK (in Ref. 10;
FT                                AAA35198). {ECO:0000305}.
SQ   SEQUENCE   2214 AA;  245041 MW;  D5A47F4E42A9B1A7 CRC64;
     MATIAPTAPI TPPMESTGDR LVTLELKDGT VLQGYSFGAE KSVAGELVFQ TGMVGYPESV
     TDPSYEGQIL VITYPLVGNY GVPDMHLRDE LVEELPRYFE SNRIHIAGLV ISHYTDEYSH
     YLAKSSLGKW LQNEGIPAVY GVDTRSLTKH LRDAGSMLGR LSLEKSGSDR TISRSSSWRS
     AFDVPEWVDP NVQNLVSKVS INEPKLYVPP ADNKHIELQT GPDGKVLRIL AIDVGMKYNQ
     IRCFIKRGVE LKVVPWNYDF TKEDYDGLFI SNGPGDPSVL DDLSQRLSNV LEAKKTPVFG
     ICLGHQLIAR AAGASTLKLK FGNRGHNIPC TSTISGRCYI TSQNHGFAVD VDTLTSGWKP
     LFVNANDDSN EGIYHSELPY FSVQFHPEST PGPRDTEFLF DVFIQAVKEF KYTQVLKPIA
     FPGGLLEDNV KAHPRIEAKK VLVLGSGGLS IGQAGEFDYS GSQAIKALKE EGIYTILINP
     NIATIQTSKG LADKVYFVPV TAEFVRKVIL HERPDAIYVT FGGQTALSVG IAMKDEFEAL
     GVKVLGTPID TIITTEDREL FSNAIDEINE KCAKSQAANS VDEALAAVKE IGFPVIVRAA
     YALGGLGSGF ANNEKELVDL CNVAFSSSPQ VLVEKSMKGW KEVEYEVVRD AFDNCITVCN
     MENFDPLGIH TGDSIVVAPS QTLSDEDYNM LRTTAVNVIR HLGVVGECNI QYALNPVSKD
     YCIIEVNARL SRSSALASKA TGYPLAYTAA KLGLNIPLNE VKNSVTKSTC ACFEPSLDYC
     VVKMPRWDLK KFTRVSTELS SSMKSVGEVM SIGRTFEEAI QKAIRSTEYA NLGFNETDLD
     IDIDYELNNP TDMRVFAIAN AFAKKGYSVD KVWEMTRIDK WFLNKLHDLV QFAEKISSFG
     TKEELPSLVL RQAKQLGFDD RQIARFLDSN EVAIRRLRKE YGITPFVKQI DTVAAEFPAY
     TNYLYMTYNA DSHDLSFDDH GVMVLGSGVY RIGSSVEFDW CAVTAVRTLR ANNIKTIMVN
     YNPETVSTDY DEADRLYFET INLERVLDIY EIENSSGVVV SMGGQTSNNI AMTLHRENVK
     ILGTSPDMID SAENRYKFSR MLDQIGVDQP AWKELTSMDE AESFAEKVGY PVLVRPSYVL
     SGAAMNTVYS KNDLESYLNQ AVEVSRDYPV VITKYIENAK EIEMDAVARN GELVMHVVSE
     HVENAGVHSG DATLIVPPQD LAPETVDRIV VATAKIGKAL KITGPYNIQF IAKDNEIKVI
     ECNVRASRSF PFISKVVGVN LIELATKAIM GLPLTPYPVE KLPDDYVAVK VPQFSFPRLA
     GADPVLGVEM ASTGEVATFG HSKYEAYLKS LLATGFKLPK KNILLSIGSY KEKQELLSSV
     QKLYNMGYKL FATSGTADFL SEHGIAVQYL EVLNKDDDDQ KSEYSLTQHL ANNEIDLYIN
     LPSANRFRRP ASYVSKGYKT RRLAVDYSVP LVTNVKCAKL LIEAISRNIT LDVSERDAQT
     SHRTITLPGL INIATYVPNA SHVIKGPAEL KETTRLFLES GFTYCQLMPR SISGPVITDV
     ASLKAANSVS QDSSYTDFSF TIAGTAHNAH SVTQSASKVT ALFLPLRELK NKITAVAELL
     NQWPTEKQVI AEAKTADLAS VLLLTSLQNR SIHITGVSNK EDLALIMTVK AKDPRVTCDV
     NIYSLFIAQD DYPEAVFLPT KEDQEFFWNN LDSIDAFSVG ALPVALANVT GNKVDVGMGI
     KDSLPLLLAA VEEGKLTIDD IVLRLHDNPA KIFNIPTQDS VVEIDLDYSF RRNKRWSPFN
     KDMNGGIERV VYNGETLVLS GELVSPGAKG KCIVNPSPAS ITASAELQST SAKRRFSITE
     EAIADNLDAA EDAIPEQPLE QKLMSSRPPR ELVAPGAIQN LIRSNNPFRG RHILSIKQFK
     RSDFHVLFAV AQELRAAVAR EGVLDLMKGH VITTIFFEPS TRTCSSFIAA MERLGGRIVN
     VNPLVSSVKK GETLQDTIRT LACYSDAIVM RHSEEMSVHI AAKYSPVPII NGGNGSREHP
     TQAFLDLFTI REEIGTVNGI TVTFMGDLKH GRTVHSLCRL LMHYQVRINL VSPPELRLPE
     GLREELRKAG LLGVESIELT PHIISKTDVL YCTRVQEERF NSPEEYARLK DTYIVDNKIL
     AHAKENMAIM HPLPRVNEIK EEVDYDHRAA YFRQMKYGLF VRMALLAMVM GVDM
//
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