PYR1_YEAST
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 03-AUG-2022, entry version 238.
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; Saccharomycetes;
OC 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; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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 URA2
RT 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 reveals 19
RT open reading frames including URA2 (5' end), TRK1, PBS2, SPT10, GCD14,
RT RPE1, PHO86, NCA3, ASF1, CCT7, GZF3, two tRNA genes, three remnant delta
RT 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 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 introns
RT 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>3.0.co;2-4;
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; DOI=10.1016/s0021-9258(18)83191-x;
RA Nagy M., le Gouar M., Potier S., Souciet J.-L., Herve G.;
RT "The primary structure of the aspartate transcarbamylase region of the URA2
RT gene product in Saccharomyces cerevisiae. Features involved in activity and
RT 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 protein
RT 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 pyrimidines
RT biosynthesis accumulates not in the nucleus but in the cytoplasm, as shown
RT by immunocytochemistry and Ura2-green fluorescent 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., Dephoure N.,
RA 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 BY
RP 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 BY
RP 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 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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1857, AND IDENTIFICATION BY
RP 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 insights
RT 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 SPECTROMETRY
RP [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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT 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 BY
RP 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 enzymatic
CC activities of the pyrimidine pathway (GATase, CPSase, 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 pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (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-dependent
CC CPSase (GD-CPSase) (EC 6.3.5.5).
CC -!- MISCELLANEOUS: In eukaryotes EC 6.3.5.5 is synthesized by two pathway-
CC specific (arginine and pyrimidine) genes under separate 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-dependent
CC hydrolases superfamily. DHOase family. CAD subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABI95879.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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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 AlphaFoldDB; P07259; -.
DR SMR; P07259; -.
DR BioGRID; 33626; 208.
DR DIP; DIP-7215N; -.
DR IntAct; P07259; 463.
DR MINT; P07259; -.
DR STRING; 4932.YJL130C; -.
DR MEROPS; C26.956; -.
DR MEROPS; S08.056; -.
DR CarbonylDB; P07259; -.
DR iPTMnet; P07259; -.
DR MaxQB; P07259; -.
DR PaxDb; P07259; -.
DR PRIDE; P07259; -.
DR EnsemblFungi; YJL130C_mRNA; YJL130C; YJL130C.
DR GeneID; 853311; -.
DR KEGG; sce:YJL130C; -.
DR SGD; S000003666; URA2.
DR VEuPathDB; FungiDB:YJL130C; -.
DR eggNOG; KOG0370; Eukaryota.
DR GeneTree; ENSGT00940000157241; -.
DR HOGENOM; CLU_000513_2_0_1; -.
DR InParanoid; P07259; -.
DR OMA; IPCTSML; -.
DR BioCyc; MetaCyc:YJL130C-MON; -.
DR BioCyc; YEAST:YJL130C-MON; -.
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 RNAct; P07259; protein.
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; 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; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Ligase; Multifunctional enzyme; Nucleotide-binding;
KW Phosphoprotein; Pyrimidine biosynthesis; Reference proteome; Repeat;
KW Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..2214
FT /note="Protein URA2"
FT /id="PRO_0000199511"
FT DOMAIN 228..413
FT /note="Glutamine amidotransferase type-1"
FT DOMAIN 562..754
FT /note="ATP-grasp 1"
FT DOMAIN 1099..1290
FT /note="ATP-grasp 2"
FT DOMAIN 1356..1508
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 2..400
FT /note="GATase (Glutamine amidotransferase)"
FT REGION 401..440
FT /note="Linker"
FT REGION 441..1482
FT /note="CPSase (Carbamoyl-phosphate synthase)"
FT REGION 1483..1492
FT /note="Linker"
FT REGION 1493..1821
FT /note="Defective DHOase domain"
FT REGION 1822..1909
FT /note="Linker"
FT REGION 1910..2214
FT /note="ATCase (Aspartate transcarbamylase)"
FT ACT_SITE 302
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 386
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 388
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 1857
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:1977585,
FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 1853
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 86
FT /note="H -> D (in Ref. 4; CAA29068)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="A -> R (in Ref. 2; CAA89425)"
FT /evidence="ECO:0000305"
FT CONFLICT 250..257
FT /note="ELKVVPWN -> RIESCSMD (in Ref. 4; CAA29068)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="I -> Y (in Ref. 4; CAA29068)"
FT /evidence="ECO:0000305"
FT CONFLICT 313..314
FT /note="GA -> VQ (in Ref. 4; CAA29068)"
FT /evidence="ECO:0000305"
FT CONFLICT 372..373
FT /note="GI -> RF (in Ref. 4; CAA29068)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..402
FT /note="RDTEFLFDV -> EIQNSCLT (in Ref. 4; CAA29068)"
FT /evidence="ECO:0000305"
FT CONFLICT 431..433
FT /note="KAH -> QGT (in Ref. 4; CAA29068)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="I -> T (in Ref. 4; CAA29068)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="I -> N (in Ref. 4; CAA29068)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="A -> G (in Ref. 4; CAA29068)"
FT /evidence="ECO:0000305"
FT CONFLICT 501..510
FT /note="TAEFVRKVIL -> NAAKQRDVDR (in Ref. 4; CAA29068)"
FT /evidence="ECO:0000305"
FT CONFLICT 1411..1412
FT /note="EV -> S (in Ref. 10; AAA35198)"
FT /evidence="ECO:0000305"
FT CONFLICT 1582
FT /note="I -> M (in Ref. 10; AAA35198)"
FT /evidence="ECO:0000305"
FT CONFLICT 1588
FT /note="N -> K (in Ref. 10; AAA35198)"
FT /evidence="ECO:0000305"
FT CONFLICT 1592
FT /note="V -> G (in Ref. 10; AAA35198)"
FT /evidence="ECO:0000305"
FT CONFLICT 1595
FT /note="S -> A (in Ref. 10; AAA35198)"
FT /evidence="ECO:0000305"
FT CONFLICT 1872
FT /note="Missing (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1937
FT /note="A -> R (in Ref. 1; AAA68280 and 10; AAA35198)"
FT /evidence="ECO:0000305"
FT CONFLICT 1997
FT /note="T -> I (in Ref. 10; AAA35198)"
FT /evidence="ECO:0000305"
FT CONFLICT 2039
FT /note="H -> L (in Ref. 10; AAA35198)"
FT /evidence="ECO:0000305"
FT CONFLICT 2158..2165
FT /note="KILAHAKE -> VRSWHTQQK (in Ref. 10; AAA35198)"
FT /evidence="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
