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Database: UniProt
Entry: P05990
LinkDB: P05990
Original site: P05990 
ID   PYR1_DROME              Reviewed;        2224 AA.
AC   P05990; B5X540; O97163; Q26376; Q7KUX4; Q8SXM0; Q9VXD5;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 3.
DT   16-JAN-2019, entry version 204.
DE   RecName: Full=CAD protein;
DE   AltName: Full=Protein rudimentary;
DE   Includes:
DE     RecName: Full=Glutamine-dependent carbamoyl-phosphate synthase;
DE              EC=6.3.5.5 {ECO:0000269|PubMed:10080891};
DE   Includes:
DE     RecName: Full=Aspartate carbamoyltransferase;
DE              EC=2.1.3.2 {ECO:0000250|UniProtKB:P27708};
DE   Includes:
DE     RecName: Full=Dihydroorotase;
DE              EC=3.5.2.3 {ECO:0000250|UniProtKB:P27708};
GN   Name=r; ORFNames=CG18572;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2884325; DOI=10.1016/0022-2836(87)90621-8;
RA   Freund J.-N., Jarry B.P.;
RT   "The rudimentary gene of Drosophila melanogaster encodes four enzymic
RT   functions.";
RL   J. Mol. Biol. 193:1-13(1987).
RN   [2]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3023623; DOI=10.1016/0022-2836(86)90378-5;
RA   Freund J.-N., Zerges W., Schedl P., Jarry B.P.;
RT   "Molecular organization of the rudimentary gene of Drosophila
RT   melanogaster.";
RL   J. Mol. Biol. 189:25-36(1986).
RN   [3]
RP   ERRATUM.
RA   Freund J.-N., Zerges W., Schedl P., Jarry B.P.;
RL   J. Mol. Biol. 191:727-727(1986).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA   Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C.,
RA   Celniker S.E.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-130.
RX   PubMed=1329025; DOI=10.1093/nar/20.17.4639;
RA   Zerges W., Udvardy A., Schedl P.;
RT   "Molecular characterization of the 5' end of the rudimentary gene in
RT   Drosophila and analysis of three P element insertions.";
RL   Nucleic Acids Res. 20:4639-4647(1992).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-2224.
RC   STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 898-1649, CPSASE ACTIVITY, AND
RP   MUTAGENESIS OF GLU-1167.
RX   PubMed=10080891; DOI=10.1006/jmbi.1999.2618;
RA   Simmons A.J., Rawls J.M., Piskur J., Davidson J.N.;
RT   "A mutation that uncouples allosteric regulation of carbamyl phosphate
RT   synthetase in Drosophila.";
RL   J. Mol. Biol. 287:277-285(1999).
RN   [10]
RP   SEQUENCE REVISION TO 2066-2146.
RX   PubMed=7932764; DOI=10.1006/jmbi.1994.1663;
RA   Davidson J.N., Kern C.B.;
RT   "Revision in sequence of CAD aspartate transcarbamylase domain of
RT   Drosophila.";
RL   J. Mol. Biol. 243:364-366(1994).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1883; SER-1885; SER-1892
RP   AND SER-1894, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: This protein is a "fusion" protein encoding four
CC       enzymatic activities of the pyrimidine pathway (GATase, CPSase,
CC       ATCase and DHOase).
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:0000269|PubMed:10080891};
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:0000250|UniProtKB:P27708};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-
CC         aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814;
CC         EC=3.5.2.3; Evidence={ECO:0000250|UniProtKB:P27708};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P27708};
CC       Note=Binds 1 zinc ion per subunit (for dihydroorotase activity).
CC       {ECO:0000250|UniProtKB:P27708};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC       Note=Binds 4 magnesium or manganese ions per subunit.
CC       {ECO:0000255|PROSITE-ProRule:PRU00409};
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   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: GATase (glutamine amidotransferase) and CPSase
CC       (carbamoyl phosphate synthase) together form the glutamine-
CC       dependent CPSase (GD-CPSase) (EC 6.3.5.5).
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=AAA28873.1; Type=Miscellaneous discrepancy; Note=Various problems, including DNA not present in the genome.; Evidence={ECO:0000305};
CC       Sequence=AAL90298.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=CAA27509.1; Type=Miscellaneous discrepancy; Note=Various problems, including DNA not present in the genome.; Evidence={ECO:0000305};
CC       Sequence=CAA27510.1; Type=Miscellaneous discrepancy; Note=Various problems, including DNA not present in the genome.; Evidence={ECO:0000305};
CC       Sequence=CAA27511.1; Type=Miscellaneous discrepancy; Note=Various problems, including DNA not present in the genome.; Evidence={ECO:0000305};
CC       Sequence=CAA27513.1; Type=Miscellaneous discrepancy; Note=Various problems, including DNA not present in the genome.; Evidence={ECO:0000305};
CC       Sequence=CAA28502.1; Type=Miscellaneous discrepancy; Note=Various problems, including DNA not present in the genome.; Evidence={ECO:0000305};
DR   EMBL; X04813; CAA28502.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X03875; CAA27509.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X03876; CAA27510.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X03877; CAA27511.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X03878; CAA27512.1; -; Genomic_DNA.
DR   EMBL; X03879; CAA27513.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AE014298; AAF48639.3; -; Genomic_DNA.
DR   EMBL; AE014298; AAS65389.2; -; Genomic_DNA.
DR   EMBL; BT046159; ACI46547.1; -; mRNA.
DR   EMBL; M37783; AAA28873.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY089560; AAL90298.1; ALT_INIT; mRNA.
DR   EMBL; AF129814; AAD18071.1; -; mRNA.
DR   EMBL; S74010; AAB32204.1; -; mRNA.
DR   PIR; A29106; QZFF.
DR   RefSeq; NP_001285343.1; NM_001298414.1.
DR   RefSeq; NP_523377.1; NM_078653.2.
DR   RefSeq; NP_996488.2; NM_206765.3.
DR   UniGene; Dm.4956; -.
DR   ProteinModelPortal; P05990; -.
DR   SMR; P05990; -.
DR   BioGrid; 58976; 39.
DR   IntAct; P05990; 8.
DR   MINT; P05990; -.
DR   STRING; 7227.FBpp0088675; -.
DR   MEROPS; M38.972; -.
DR   iPTMnet; P05990; -.
DR   PaxDb; P05990; -.
DR   PRIDE; P05990; -.
DR   EnsemblMetazoa; FBtr0089734; FBpp0088675; FBgn0003189.
DR   EnsemblMetazoa; FBtr0340155; FBpp0309141; FBgn0003189.
DR   EnsemblMetazoa; FBtr0340156; FBpp0309142; FBgn0003189.
DR   GeneID; 32640; -.
DR   KEGG; dme:Dmel_CG18572; -.
DR   CTD; 32640; -.
DR   FlyBase; FBgn0003189; r.
DR   eggNOG; KOG0370; Eukaryota.
DR   eggNOG; COG0458; LUCA.
DR   eggNOG; COG0505; LUCA.
DR   eggNOG; COG0540; LUCA.
DR   InParanoid; P05990; -.
DR   KO; K11540; -.
DR   OMA; FTNANDH; -.
DR   OrthoDB; 273358at2759; -.
DR   PhylomeDB; P05990; -.
DR   BRENDA; 6.3.5.5; 1994.
DR   Reactome; R-DME-500753; Pyrimidine biosynthesis.
DR   UniPathway; UPA00070; UER00115.
DR   UniPathway; UPA00070; UER00116.
DR   UniPathway; UPA00070; UER00117.
DR   ChiTaRS; r; fly.
DR   GenomeRNAi; 32640; -.
DR   PRO; PR:P05990; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0003189; Expressed in 6 organ(s), highest expression level in embryo.
DR   ExpressionAtlas; P05990; baseline and differential.
DR   Genevisible; P05990; DM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IDA:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IC:FlyBase.
DR   GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IBA:GO_Central.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IDA:FlyBase.
DR   GO; GO:0004151; F:dihydroorotase activity; IDA:FlyBase.
DR   GO; GO:0070406; F:glutamine binding; IC:FlyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IMP:FlyBase.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0070409; P:carbamoyl phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IMP:FlyBase.
DR   GO; GO:0051414; P:response to cortisol; IBA:GO_Central.
DR   GO; GO:0033574; P:response to testosterone; IBA:GO_Central.
DR   GO; GO:0000050; P:urea cycle; 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; IPR006680; Amidohydro-rel.
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; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
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; PF01979; Amidohydro_1; 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   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; SSF51338; SSF51338; 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; 1.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51855; MGS; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; Glutamine amidotransferase;
KW   Hydrolase; Ligase; Magnesium; Manganese; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW   Pyrimidine biosynthesis; Reference proteome; Repeat; Transferase;
KW   Zinc.
FT   CHAIN         1   2224       CAD protein.
FT                                /FTId=PRO_0000199505.
FT   DOMAIN      195    380       Glutamine amidotransferase type-1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00605}.
FT   DOMAIN      529    721       ATP-grasp 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN     1066   1257       ATP-grasp 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN     1322   1477       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     555    610       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND    1092   1149       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   REGION        1    369       GATase (Glutamine amidotransferase).
FT                                {ECO:0000250|UniProtKB:P08955}.
FT   REGION      370    415       Linker. {ECO:0000250|UniProtKB:P08955}.
FT   REGION      416   1470       CPSase (Carbamoyl-phosphate synthase).
FT                                {ECO:0000250|UniProtKB:P08955}.
FT   REGION     1471   1484       Linker. {ECO:0000250|UniProtKB:P08955}.
FT   REGION     1485   1800       DHOase (dihydroorotase).
FT                                {ECO:0000250|UniProtKB:P08955}.
FT   REGION     1801   1912       Linker. {ECO:0000250|UniProtKB:P08955}.
FT   REGION     1913   2224       ATCase (Aspartate transcarbamylase).
FT                                {ECO:0000250|UniProtKB:P08955}.
FT   ACT_SITE    269    269       Nucleophile; for GATase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00605}.
FT   ACT_SITE    353    353       For GATase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00605}.
FT   ACT_SITE    355    355       For GATase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00605}.
FT   METAL       678    678       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       692    692       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       692    692       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       694    694       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL      1216   1216       Magnesium or manganese 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL      1228   1228       Magnesium or manganese 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL      1228   1228       Magnesium or manganese 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL      1230   1230       Magnesium or manganese 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL      1486   1486       Zinc 1; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1486   1486       Zinc 2; via pros nitrogen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1488   1488       Zinc 1; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1571   1571       Zinc 1; via carbamate group.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1571   1571       Zinc 3; via carbamate group.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1605   1605       Zinc 3; via pros nitrogen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1628   1628       Zinc 2. {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1629   1629       Zinc 3; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1652   1652       Zinc 2. {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1701   1701       Zinc 1. {ECO:0000250|UniProtKB:P27708}.
FT   BINDING    1490   1490       N-carbamoyl-L-aspartate.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   BINDING    1520   1520       N-carbamoyl-L-aspartate.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   BINDING    1676   1676       N-carbamoyl-L-aspartate; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   BINDING    1701   1701       N-carbamoyl-L-aspartate.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   BINDING    1705   1705       N-carbamoyl-L-aspartate.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   MOD_RES    1571   1571       N6-carboxylysine.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   MOD_RES    1883   1883       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1885   1885       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1892   1892       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1894   1894       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MUTAGEN    1167   1167       E->K: Severely diminishes UTP inhibition
FT                                of CPSase; in Su(b).
FT                                {ECO:0000269|PubMed:10080891}.
FT   CONFLICT     34     34       F -> V (in Ref. 2; CAA27509).
FT                                {ECO:0000305}.
FT   CONFLICT     58     58       G -> A (in Ref. 2; CAA27509).
FT                                {ECO:0000305}.
FT   CONFLICT    172    173       RN -> QD (in Ref. 2; CAA27509).
FT                                {ECO:0000305}.
FT   CONFLICT    220    221       LL -> FV (in Ref. 2; CAA27509).
FT                                {ECO:0000305}.
FT   CONFLICT    288    288       Y -> I (in Ref. 2; CAA27509).
FT                                {ECO:0000305}.
FT   CONFLICT    394    394       P -> L (in Ref. 2; CAA27509).
FT                                {ECO:0000305}.
FT   CONFLICT   2192   2192       S -> L (in Ref. 2; CAA27513).
FT                                {ECO:0000305}.
FT   CONFLICT   2222   2224       TAL -> RRS (in Ref. 2; CAA27513).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2224 AA;  246672 MW;  F89DEAD44FEFAEC6 CRC64;
     MASTDCYLAL EDGTVLPGYS FGYVPSENES KVGFGGEVVF QTGMVGYTEA LTDRSYSGQI
     LVLTYPLIGN YGVPAPDEDE HGLPLHFEWM KGVVQATALV VGEVAEEAFH WRKWKTLPDW
     LKQHKVPGIQ DIDTRALTKK LREQGSMLGK IVYEKPPVEG LPKSSFVDPN VRNLAKECSV
     KERQVYGNPN GKGPRIAILD CGLKLNQLRC LLQRGASVTL LPWSARLEDE QFDALFLSNG
     PGNPESCDQI VQQVRKVIEE GQKPVFGICL GHQLLAKAIG CSTYKMKYGN RGHNLPCLHR
     ATGRCLMTSQ NHGYAVDLEQ LPDGWSELFV NANDGTNEGI VHASKPYFSV QFHPEHHAGP
     QDTEFLFDVF MESIQQKDLT IPQLIEQRLR PTTPAIDSAP VMPRKVLILG SGGLSIGQAG
     EFDYSGSQAI KAMRESNIQT VLINPNIATV QTSKGMADKC YFLPLTPHYV EQVIKSERPN
     GVLLTFGGQT ALNCGVQLER AGVFSKYNVR ILGTPIQSII ETEDRKLFAE RVNEIGEQVA
     PSEAVYSVAQ ALDAASRLGY PVMARAAFSL GGLGSGFANN EEELQSLAQQ ALAHSSQLIV
     DKSLKGWKEV EYEVVRDAYN NCITVCNMEN FDPLGIHTGE SIVVAPSQTL SDREYQMLRS
     TALKVIRHFG VVGECNIQYA LCPHSEQYYI IEVNARLSRS SALASKATGY PLAYVAAKLA
     LGLPLPDIKN SVTGNTTACF EPSLDYCVVK IPRWDLAKFV RVSKHIGSSM KSVGEVMAIG
     RNFEEAFQKA LRMVDSDVLG FDPDVVPLNK EQLAEQLSEP TDRRPFVIAA ALQLGMSLRE
     LHQLTNIDYW FLEKLERIIL LQSLLTRNGS RTDAALLLKA KRFGFSDKQI AKYIKSTELA
     VRHQRQEFGI RPHVKQIDTV AGEWPASTNY LYHTYNGSEH DVDFPGGHTI VVGSGVYRIG
     SSVEFDWCAV GCLRELRKLQ RPTIMINYNP ETVSTDYDMC DRLYFEEISF EVVMDIYEME
     NSEGIILSMG GQLPNNIAMD LHRQQAKVLG TSPESIDCAE NRFKFSRMLD RKGILQPRWK
     ELTNLQSAIE FCEEVGYPCL VRPSYVLSGA AMNVAYSNQD LETYLNAASE VSREHPVVIS
     KFLTEAKEID VDAVASDGRI LCMAVSEHVE NAGVHSGDAT LVTPPQDLNA ETLEAIKRIT
     CDLASVLDVT GPFNMQLIAK NNELKVIECN VRVSRSFPFV SKTLDHDFVA TATRAIVGLD
     VEPLDVLHGV GKVGVKVPQF SFSRLAGADV QLGVEMASTG EVACFGDNRY EAYLKAMMST
     GFQIPKNAVL LSIGSFKHKM ELLPSIRDLA KMGYKLYASM GTGDFYAEHG VNVESVQWTF
     DKTTPDDING ELRHLAEFLA NKQFDLVINL PMSGGGARRV SSFMTHGYRT RRLAVDYSIP
     LVTDVKCTKL LVESMRMNGG KPPMKTHTDC MTSRRIVKLP GFIDVHVHLR EPGATHKEDF
     ASGTAAALAG GVTLVCAMPN TNPSIVDRET FTQFQELAKA GARCDYALYV GASDDNWAQV
     NELASHACGL KMYLNDTFGT LKLSDMTSWQ RHLSHWPKRS PIVCHAERQS TAAVIMLAHL
     LDRSVHICHV ARKEEIQLIR SAKEKGVKVT CEVCPHHLFL STKDVERLGH GMSEVRPLLC
     SPEDQEALWE NIDYIDVFAT DHAPHTLAEK RSERPPPGFP GVETILPLLL QAVHEGRLTM
     EDIKRKFHRN PKIIFNLPDQ AQTYVEVDLD EEWTITGNEM KSKSGWTPFE GTKVKGRVHR
     VVLRGEVAFV DGQVLVQPGF GQNVRPKQSP LASEASQDLL PSDNDANDTF TRLLTSEGPG
     GGVHGISTKV HFVDGANFLR PNSPSPRIRL DSASNTTLRE YLQRTTNSNP VAHSLMGKHI
     LAVDMFNKDH LNDIFNLAQL LKLRGTKDRP VDELLPGKIM ASVFYEVSTR TQCSFAAAML
     RLGGRVISMD NITSSVKKGE SLEDSIKVVS SYADVVVLRH PSPGAVARAA TFSRKPLINA
     GDGVGEHPTQ ALLDIFTIRE EFGTVNGLTI TMVGDLKNGR TVHSLARLLT LYNVNLQYVA
     PNSLQMPDEV VQFVHQRGVK QLFARDLKNV LPDTDVLYMT RIQRERFDNV EDYEKCCGHL
     VLTPEHMMRA KKRSIVLHPL PRLNEISREI DSDPRAAYFR QAEYGMYIRM ALLAMVVGGR
     NTAL
//
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