ID PYR1_SQUAC Reviewed; 2242 AA. AC Q91437; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 146. DE RecName: Full=Multifunctional protein CAD {ECO:0000305}; DE AltName: Full=Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; DE Includes: DE RecName: Full=Glutamine-dependent carbamoyl-phosphate synthase; DE EC=6.3.5.5 {ECO:0000250|UniProtKB:P27708}; DE Includes: DE RecName: Full=Glutamine amidotransferase; DE Short=GATase; DE Short=GLNase; DE EC=3.5.1.2 {ECO:0000250|UniProtKB:P07259}; DE Includes: DE RecName: Full=Ammonium-dependent carbamoyl phosphate synthase; DE Short=CPS; DE Short=CPSase; DE EC=6.3.4.16 {ECO:0000250|UniProtKB:P07259}; 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=CAD; OS Squalus acanthias (Spiny dogfish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; OC Elasmobranchii; Squalomorphii; Squaliformes; Squalidae; Squalus. OX NCBI_TaxID=7797; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Spleen, and Testis; RX PubMed=7775474; DOI=10.1074/jbc.270.23.14130; RA Hong J., Salo W.L., Anderson P.M.; RT "Nucleotide sequence and tissue-specific expression of the multifunctional RT protein carbamoyl-phosphate synthetase-aspartate transcarbamoylase- RT dihydroorotase (CAD) mRNA in Squalus acanthias."; RL J. Biol. Chem. 270:14130-14139(1995). CC -!- FUNCTION: Multifunctional protein that encodes the first 3 enzymatic CC activities of the de novo pyrimidine pathway: carbamoylphosphate CC synthetase (CPSase; EC 6.3.5.5), aspartate transcarbamylase (ATCase; EC CC 2.1.3.2) and dihydroorotase (DHOase; EC 3.5.2.3). The CPSase-function CC is accomplished in 2 steps, by a glutamine-dependent amidotransferase CC activity (GATase) that binds and cleaves glutamine to produce ammonia, CC followed by an ammonium-dependent carbamoyl phosphate synthetase, which CC reacts with the ammonia, hydrogencarbonate and ATP to form carbamoyl CC phosphate. The endogenously produced carbamoyl phosphate is sequestered CC and channeled to the ATCase active site. ATCase then catalyzes the CC formation of carbamoyl-L-aspartate from L-aspartate and carbamoyl CC phosphate. In the last step, DHOase catalyzes the cyclization of CC carbamoyl aspartate to dihydroorotate. {ECO:0000250|UniProtKB:P27708}. 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:0000250|UniProtKB:P27708}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+); CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; CC Evidence={ECO:0000250|UniProtKB:P07259}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, CC ChEBI:CHEBI:456216; EC=6.3.4.16; CC Evidence={ECO:0000250|UniProtKB:P07259}; 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=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 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|PROSITE- CC ProRule:PRU00409}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:P27708}; CC Note=Binds 3 Zn(2+) ions per subunit (for dihydroorotase activity). CC {ECO:0000250|UniProtKB:P27708}; CC -!- ACTIVITY REGULATION: Allosterically regulated and controlled by CC phosphorylation. 5-phosphoribose 1-diphosphate is an activator while CC UMP is an inhibitor of the CPSase reaction. CC {ECO:0000250|UniProtKB:P27708}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 1/3. CC {ECO:0000250|UniProtKB:P27708}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 2/3. CC {ECO:0000250|UniProtKB:P27708}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 3/3. CC {ECO:0000250|UniProtKB:P27708}. CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P27708}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P27708}. Nucleus CC {ECO:0000250|UniProtKB:P27708}. CC -!- TISSUE SPECIFICITY: Present in the testis but not in the liver. CC {ECO:0000269|PubMed:7775474}. 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). {ECO:0000250|UniProtKB:P07259}. CC -!- SIMILARITY: In the N-terminal section; belongs to the CarA family. CC {ECO:0000305}. CC -!- SIMILARITY: In the 2nd section; belongs to the CarB family. CC {ECO:0000305}. CC -!- SIMILARITY: In the 3rd section; belongs to the metallo-dependent CC hydrolases superfamily. DHOase family. CAD subfamily. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC aspartate/ornithine carbamoyltransferase superfamily. ATCase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U18868; AAA74569.1; -; mRNA. DR PIR; A57541; A57541. DR AlphaFoldDB; Q91437; -. DR SMR; Q91437; -. DR UniPathway; UPA00070; UER00115. DR UniPathway; UPA00070; UER00116. DR UniPathway; UPA00070; UER00117. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC. DR GO; GO:0004151; F:dihydroorotase activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; ISS:UniProtKB. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro. DR CDD; cd01316; CAD_DHOase; 1. DR CDD; cd01744; GATase1_CPSase; 1. DR CDD; cd01423; MGS_CPS_I_III; 1. DR Gene3D; 3.40.50.20; -; 2. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2. DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1. DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1. DR HAMAP; MF_00001; Asp_carb_tr; 1. DR HAMAP; MF_01209; CPSase_S_chain; 1. DR InterPro; 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 NCBIfam; TIGR00670; asp_carb_tr; 1. DR NCBIfam; TIGR01369; CPSaseII_lrg; 1. DR NCBIfam; TIGR01368; CPSaseIIsmall; 1. DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1. DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1. DR Pfam; 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 PRINTS; PR00099; CPSGATASE. DR SMART; SM01096; CPSase_L_D3; 1. DR SMART; SM01097; CPSase_sm_chain; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1. DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1. DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 2. DR PROSITE; PS50975; ATP_GRASP; 2. DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1. DR PROSITE; PS00866; CPSASE_1; 2. DR PROSITE; PS00867; CPSASE_2; 2. DR PROSITE; PS00482; DIHYDROOROTASE_1; 1. DR PROSITE; PS00483; DIHYDROOROTASE_2; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. DR PROSITE; PS51855; MGS; 1. PE 2: Evidence at transcript level; KW Allosteric enzyme; ATP-binding; Cytoplasm; Hydrolase; Ligase; KW Metal-binding; Multifunctional enzyme; Nucleotide-binding; Nucleus; KW Phosphoprotein; Pyrimidine biosynthesis; Repeat; Transferase; Zinc. FT CHAIN 1..2242 FT /note="Multifunctional protein CAD" FT /id="PRO_0000199508" FT DOMAIN 177..363 FT /note="Glutamine amidotransferase type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT DOMAIN 522..714 FT /note="ATP-grasp 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT DOMAIN 1057..1248 FT /note="ATP-grasp 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT DOMAIN 1313..1469 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" FT REGION 1..365 FT /note="GATase (Glutamine amidotransferase)" FT /evidence="ECO:0000250|UniProtKB:P08955" FT REGION 366..397 FT /note="Linker" FT /evidence="ECO:0000250|UniProtKB:P08955" FT REGION 398..1462 FT /note="CPSase (Carbamoyl-phosphate synthase)" FT /evidence="ECO:0000250|UniProtKB:P08955" FT REGION 398..937 FT /note="CPSase A" FT /evidence="ECO:0000250|UniProtKB:P08955" FT REGION 938..1462 FT /note="CPSase B" FT /evidence="ECO:0000250|UniProtKB:P08955" FT REGION 1463..1796 FT /note="DHOase (dihydroorotase)" FT /evidence="ECO:0000250|UniProtKB:P08955" FT REGION 1797..1934 FT /note="Linker" FT /evidence="ECO:0000250|UniProtKB:P08955" FT REGION 1829..1862 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1935..2242 FT /note="ATCase (Aspartate transcarbamylase)" FT /evidence="ECO:0000250|UniProtKB:P08955" FT COMPBIAS 1835..1855 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 252 FT /note="Nucleophile; for GATase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT ACT_SITE 336 FT /note="For GATase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT ACT_SITE 338 FT /note="For GATase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT ACT_SITE 1693 FT /note="For DHOase activity" FT /evidence="ECO:0000250|UniProtKB:P05020" FT BINDING 44 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P0A6F1" FT BINDING 222 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P0A6F1" FT BINDING 224 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P0A6F1" FT BINDING 253 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P0A6F1" FT BINDING 256 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P0A6F1" FT BINDING 294 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P0A6F1" FT BINDING 296 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P0A6F1" FT BINDING 297 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P0A6F1" FT BINDING 518 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 558 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 564 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 565 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 595 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 602 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 628 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 629 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 630 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 671 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 671 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 671 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 685 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 685 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 685 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 685 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 685 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 687 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 687 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 1093 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 1132 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 1134 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 1139 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 1164 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 1165 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 1166 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 1167 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 1207 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 1207 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 1207 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 1219 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P00968" FT BINDING 1219 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 1219 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 1219 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 1219 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 1221 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 1221 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 1478 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P27708" FT BINDING 1478 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P27708" FT BINDING 1480 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P27708" FT BINDING 1482 FT /ligand="(S)-dihydroorotate" FT /ligand_id="ChEBI:CHEBI:30864" FT /evidence="ECO:0000250|UniProtKB:P27708" FT BINDING 1512 FT /ligand="(S)-dihydroorotate" FT /ligand_id="ChEBI:CHEBI:30864" FT /evidence="ECO:0000250|UniProtKB:P27708" FT BINDING 1563 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 1563 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 1597 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P27708" FT BINDING 1620 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P27708" FT BINDING 1621 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P27708" FT BINDING 1644 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P27708" FT BINDING 1668 FT /ligand="(S)-dihydroorotate" FT /ligand_id="ChEBI:CHEBI:30864" FT /evidence="ECO:0000250|UniProtKB:P27708" FT BINDING 1693 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P27708" FT BINDING 1697 FT /ligand="(S)-dihydroorotate" FT /ligand_id="ChEBI:CHEBI:30864" FT /evidence="ECO:0000250|UniProtKB:P27708" FT BINDING 1709 FT /ligand="(S)-dihydroorotate" FT /ligand_id="ChEBI:CHEBI:30864" FT /evidence="ECO:0000250|UniProtKB:P27708" FT BINDING 1992 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000250|UniProtKB:P0A786" FT BINDING 1993 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000250|UniProtKB:P0A786" FT BINDING 2020 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:P0A786" FT BINDING 2041 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000250|UniProtKB:P0A786" FT BINDING 2069 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000250|UniProtKB:P0A786" FT BINDING 2072 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000250|UniProtKB:P0A786" FT BINDING 2102 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:P0A786" FT BINDING 2163 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:P0A786" FT BINDING 2202 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000250|UniProtKB:P0A786" FT BINDING 2203 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000250|UniProtKB:P0A786" FT MOD_RES 1563 FT /note="N6-carboxylysine" FT /evidence="ECO:0000250|UniProtKB:P27708" SQ SEQUENCE 2242 AA; 249393 MW; 99F1986BA41244EA CRC64; MATLFLDDGS SFKGRLFGAS STVSGEVVFQ TGMVGYPEAL TDPSYLSQIL VLTYPLIGNY GIPKDEEDEH GLSKWFESAK IHAAALVIGE NSQNPSHWSS VRSLDQRLKE HGIPALEGID TRSLTKKIRE KGTLLGKLVI DGTDENSLPY DDPNKRHLVK EVSIKEPKVY HPSGNVKIMA VDCGMKYNQI RSLCKRGAAV TVVPWDYLFD SNEFDGLFIS NGPGDPEYCQ QTINNVKKAI SEEKPKPLFG ICLGHQILSL AIGAKTYKMK YGNRGHNQPC IHEGTQRCFY TSQNHGFAVE PCSLPRDWSV LFTNANDQSN EGIIHNSKPL FSVQFHPEHK AGPTDLVDLF DIFLECARDV KLGVNLDKTV KGRVISHYSF KNGTENSKTP PGRIQPHKVL ILGSGGLSIG QAGEFDYSGS QAIKALKEEN VQSVLINPNI ATVQTSKGLA DKVYFLPITP EYVTQVIMNE RPDGILLTFG GQTALNCGVE LQKRGVLEKY HVRVLGTPVS SIEMTEDRKI FVEKMAEINE YVVPSEAAFT LEQAQGAAER LGYPVLVRAA FALGGLGSGF AQNKEELVTL VTQAFAHTSQ ILVDKSLKGW KEIEYEVVRD AYDNCITVCN MENVDPLGIH TGESIVVAPS QTLNDKEYNL LRTTAIKVIR HLGVVGECNI QYALSPESEQ YFIIEVNARL SRSSALASKA TGYPLAYVAA KLALGIPLPV LRNSVTNSTT ANYEPSLDYC VVKVPRWDLS KFLRLSTKIG SSMKSVGEVM AIGRNFEEAF QKALRMVDEN CVGFDHTLKP ASDEELETPT DKRIFVLAAA LRAGYEIDRL YELTKIDKWF LHKMKNIVEY SLKLSELYMK DEVPRHDLLK VKRLGFSDKQ IAMAIQSTEL AVRRLRQEWK ILPVVKQIDT VAAEWPAQTN YLYLTYNGEG HDLDFTKPHV MVIGSGVYRI GSSVEFDWCA VRCIQQLRKM GYKTRMVNYN PETVSTDYDM CDRLYFDEIS FEVVMDIYEL ENPEGIILSM GGQLPNNIAM DLHRQQCRIL GTSPESIDTA ENRFKFSRML DTIGISQPRW KELSDTESSK QFCTKVGYPC LIRPSYVLSG VAMNVAYSDN DLEKFLSSAV AVSKEHPVVI SKFIQEAKEI DVDAVACDGV VIAVAISEHV ENAGVHSGDA TLVTPPQDLN QKTTERIKAI VHAIGQELQA TGPFNLQLIA KDDQLKVIEC NVRVSRSFPF VSKTLGVDMI ALATKVIMGE EVEPVGLMTG TGVVGVKVPQ FSFSRLAGAD VVLGVEMTST GEVACFGENR YEAYLKAMLS TGFKIPKKNI LLSIGSYKNK SELLSTVQSL EQLGYNLYAS LGTADFYTEH GVKIKAVDWP FEDTDNGCPL KERHRNIMDY LEENHFDLVI NLSMRNSGGR RLSSFVTKGY RTRRLAVDYS VPLIIDIKCT KLFVEALRLV GDTPPVKTHI DSMSSHKLIR LPGLIDVHVH LREPGGTHKE DFASGTAAAL AGGVTMVCAM PNTNPAITDQ TSFALVQKLA TAGARCDFAL FLGASSDNAD VLPLISNSAA GLKMYLNDTF STLKMDNVSL WMEHFEKWPK HLPIVVHAER QTVAAILMVA QLYQRPVHIC HVARKEEIQI IRAAKQKGVQ VTCEVAPHHL FLNEEDLESI GHGKGQVRPM LSTKEDVNAL WENLDVIDCF ATDHAPHSVE EKNSDSPPPG YPGLETMLPL LLTAVSEGRL TIDDLVKRLY ENPRKIFSLP VQENTYVEVD LEQEWIIPSY MQFTKSKWTP FEGKKVKGRV RRVVLRGEVA YIDGQVLVPP GYGQDVRAWP LGVPLPPPPT TVKTPEHSKP TQTETVRTRT ASPRRLASSG PAVDARFHLP PRIHRCSDPG LPNAEGEYKE KPVKKFIEQD TVSQDGYIYP PPVSRLLSPQ NLAAQAVPHP YSLLLHPFVG QHILSVKRFT KDQLSHLFNV AHNLRLTVQK DRSLDILKGK VMASMFYEVS TRTSSSFRAA MHRLGGSVIH FSEATSSVQK GESLLDSVQT MSCYVDVVVL RHPEPGAVEL AAKHSRKPII NAGDGVGEHP TQALLDIFTI REELGTVNGM TITMVGDLKH GRTVHSLAYL LTLYRVNLRY VTPRNLRMPP NIIRFLASRG IKQEEFDSLE EALPDTDVLY MTRIQKERFA SEEEYEACFG QFILTPHIMT KGKKKMVVMH PLPRVNEVSV EVDSDPRAAY FRQAENGMYV RMALLATVLG KF //