PYR1_DROME
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 03-AUG-2022, entry version 220.
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; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC 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 OF PUBMED:3023623.
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., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., 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., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., 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., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA 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., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT 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., 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., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA 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 MUTAGENESIS OF
RP 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 AND
RP 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 enzymatic
CC activities of the pyrimidine pathway (GATase, CPSase, ATCase and
CC 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-aspartate;
CC Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
CC 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 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 -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (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-dependent
CC CPSase (GD-CPSase) (EC 6.3.5.5).
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=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=Truncated N-terminus.; 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};
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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 AlphaFoldDB; P05990; -.
DR SMR; P05990; -.
DR BioGRID; 58976; 39.
DR IntAct; P05990; 8.
DR MINT; P05990; -.
DR STRING; 7227.FBpp0088675; -.
DR MEROPS; C26.952; -.
DR MEROPS; C26.956; -.
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 VEuPathDB; VectorBase:FBgn0003189; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_2_1_1; -.
DR InParanoid; P05990; -.
DR OMA; IPCTSML; -.
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 BioGRID-ORCS; 32640; 1 hit in 3 CRISPR screens.
DR ChiTaRS; r; fly.
DR GenomeRNAi; 32640; -.
DR PRO; PR:P05990; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003189; Expressed in eye disc (Drosophila) and 21 other tissues.
DR ExpressionAtlas; P05990; baseline and differential.
DR Genevisible; P05990; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IC:FlyBase.
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:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IMP:FlyBase.
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; 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; 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; Cytoplasm; Glutamine amidotransferase; Hydrolase; Ligase;
KW Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Phosphoprotein; Pyrimidine biosynthesis;
KW Reference proteome; Repeat; Transferase; Zinc.
FT CHAIN 1..2224
FT /note="CAD protein"
FT /id="PRO_0000199505"
FT DOMAIN 195..380
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT DOMAIN 529..721
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 1066..1257
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 1322..1477
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..369
FT /note="GATase (Glutamine amidotransferase)"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 370..415
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 416..1470
FT /note="CPSase (Carbamoyl-phosphate synthase)"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 1471..1484
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 1485..1800
FT /note="DHOase (dihydroorotase)"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 1801..1912
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 1821..1843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1913..2224
FT /note="ATCase (Aspartate transcarbamylase)"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT COMPBIAS 1822..1843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 269
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 353
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 355
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 555..610
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 678
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 692
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 692
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 694
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1092..1149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1486
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1486
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1488
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1490
FT /ligand="N-carbamoyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:32814"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1520
FT /ligand="N-carbamoyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:32814"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1571
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1571
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1605
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1628
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1629
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1652
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1676
FT /ligand="N-carbamoyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:32814"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1701
FT /ligand="N-carbamoyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:32814"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1701
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1705
FT /ligand="N-carbamoyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:32814"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT MOD_RES 1571
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT MOD_RES 1883
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1885
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1892
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1894
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 1167
FT /note="E->K: Severely diminishes UTP inhibition of CPSase;
FT in Su(b)."
FT /evidence="ECO:0000269|PubMed:10080891"
FT CONFLICT 34
FT /note="F -> V (in Ref. 2; CAA27509)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="G -> A (in Ref. 2; CAA27509)"
FT /evidence="ECO:0000305"
FT CONFLICT 172..173
FT /note="RN -> QD (in Ref. 2; CAA27509)"
FT /evidence="ECO:0000305"
FT CONFLICT 220..221
FT /note="LL -> FV (in Ref. 2; CAA27509)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="Y -> I (in Ref. 2; CAA27509)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="P -> L (in Ref. 2; CAA27509)"
FT /evidence="ECO:0000305"
FT CONFLICT 2192
FT /note="S -> L (in Ref. 2; CAA27513)"
FT /evidence="ECO:0000305"
FT CONFLICT 2222..2224
FT /note="TAL -> RRS (in Ref. 2; CAA27513)"
FT /evidence="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
