ID A0A0C4WJR3_9GAMM Unreviewed; 1073 AA. AC A0A0C4WJR3; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 28-FEB-2018, entry version 21. DE RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000256|HAMAP-Rule:MF_01210}; DE EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01210}; DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000256|HAMAP-Rule:MF_01210}; GN Name=carB {ECO:0000256|HAMAP-Rule:MF_01210, GN ECO:0000313|EMBL:AJE20269.1}; GN ORFNames=Achr_7710 {ECO:0000313|EMBL:AJE20269.1}; OS Azotobacter chroococcum NCIMB 8003. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=1328314 {ECO:0000313|EMBL:AJE20269.1, ECO:0000313|Proteomes:UP000068210}; RN [1] {ECO:0000313|EMBL:AJE20269.1, ECO:0000313|Proteomes:UP000068210} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCIMB 8003 {ECO:0000313|EMBL:AJE20269.1, RC ECO:0000313|Proteomes:UP000068210}; RX PubMed=26061173; RA Robson R.L., Jones R., Robson R.M., Schwartz A., Richardson T.H.; RT "Azotobacter Genomes: The Genome of Azotobacter chroococcum NCIMB 8003 RT (ATCC 4412)."; RL PLoS ONE 10:E0127997-E0127997(2015). CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 CC ADP + phosphate + L-glutamate + carbamoyl phosphate. CC {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00383240}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|SAAS:SAAS00981842}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|SAAS:SAAS00611658}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; CC carbamoyl phosphate from bicarbonate: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00981844}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3. CC {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS01000080}. CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain CC promotes the hydrolysis of glutamine to ammonia, which is used by CC the large (or ammonia) chain to synthesize carbamoyl phosphate. CC {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00570548}. CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000256|HAMAP- CC Rule:MF_01210, ECO:0000256|SAAS:SAAS00570556}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01210}. 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; CP010415; AJE20269.1; -; Genomic_DNA. DR RefSeq; WP_039802050.1; NZ_CP010415.1. DR EnsemblBacteria; AJE20269; AJE20269; Achr_7710. DR KEGG; acx:Achr_7710; -. DR KO; K01955; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000068210; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd01424; MGS_CPS_II; 1. DR Gene3D; 1.10.1030.10; -; 1. DR Gene3D; 3.40.50.1380; -; 1. DR HAMAP; MF_01210_A; CPSase_L_chain_A; 1. DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR006275; CarbamoylP_synth_lsu. DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo. DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf. DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd. DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom. DR InterPro; IPR011607; MGS-like_dom. DR InterPro; IPR036914; MGS-like_dom_sf. DR InterPro; IPR033937; MGS_CPS_CarB. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR Pfam; PF02786; CPSase_L_D2; 2. DR Pfam; PF02787; CPSase_L_D3; 1. DR Pfam; PF02142; MGS; 1. DR PRINTS; PR00098; CPSASE. DR SMART; SM01096; CPSase_L_D3; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF48108; SSF48108; 1. DR SUPFAM; SSF52335; SSF52335; 1. DR SUPFAM; SSF52440; SSF52440; 2. DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1. DR PROSITE; PS50975; ATP_GRASP; 2. DR PROSITE; PS00866; CPSASE_1; 2. DR PROSITE; PS00867; CPSASE_2; 2. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210, KW ECO:0000256|SAAS:SAAS00981831}; KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210, KW ECO:0000256|SAAS:SAAS00981841}; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409, KW ECO:0000256|SAAS:SAAS00710217}; KW Complete proteome {ECO:0000313|Proteomes:UP000068210}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01210, KW ECO:0000256|SAAS:SAAS00710245}; KW Magnesium {ECO:0000256|SAAS:SAAS00981805}; KW Manganese {ECO:0000256|SAAS:SAAS00511130}; KW Metal-binding {ECO:0000256|SAAS:SAAS00511109}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409, KW ECO:0000256|SAAS:SAAS00710285}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210, KW ECO:0000256|SAAS:SAAS01000143}; KW Reference proteome {ECO:0000313|Proteomes:UP000068210}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_01210, KW ECO:0000256|SAAS:SAAS00981845}. FT DOMAIN 133 328 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. FT DOMAIN 678 869 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. FT REGION 1 403 Carboxyphosphate synthetic domain. FT {ECO:0000256|HAMAP-Rule:MF_01210}. FT REGION 404 553 Oligomerization domain. FT {ECO:0000256|HAMAP-Rule:MF_01210}. FT REGION 936 1073 Allosteric domain. {ECO:0000256|HAMAP- FT Rule:MF_01210}. SQ SEQUENCE 1073 AA; 117165 MW; 6787466A9E93E391 CRC64; MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALKEE GFRVILVNSN PATIMTDPSM ADATYIEPIK WQTVAKIIEK ERPDALLPTM GGQTALNCAL ALEKHGVLAK FGVEMIGANA DTIDKAEDRS RFDKAMRAIG LECPRSGIAH SMDEAYGVLD KVGFPCIIRP SFTMGGTGGG IAYNREEFEE ICTRGLDLSP TSELLIDESL IGWKEYEMEV VRDKKDNCII VCSIENFDPM GVHTGDSITV APAQTLTDKE YQIMRNASLA VLREIGVETG GSNVQFGINP VDGRMVVIEM NPRVSRSSAL ASKATGFPIA KIAAKLAVGY TLDELSNDIT GGRTPASFEP AIDYVVTKVP RFAFEKFPKA DARLTTQMKS VGEVMAIGRT FQESVQKALR GLEVGVAGFD PKLDLGNPEA ESILKRELIV PGAERIWYVA DAFRAGKSVD DVFALTKIDP WFLVQIEDLV KEEERVKTLG LSSIDRNLMW KLKRKGFSDA RLAKLLGVTE KNLRSHRQKL KVQPVYKRVD TCAAEFATDT AYMYSTYEEE CEANPSSRDK IMVIGGGPNR IGQGIEFDYC CVHAALAMRE DGYETIMVNC NPETVSTDYD TSDRLYFEPV TLEDVLEIVR VEQPKGVIVQ YGGQTPLKIC RALEEAGVPI IGTSPDAIDR AEDRERFQQM VERLNLRQPP NATARSEDEA IAASKVIGYP LVVRPSYVLG GRAMEIVYEE DELKRYMREA VQVSNDSPVL LDHFLNCAIE VDIDAVCDGE DVVIGAIMQH IEQAGVHSGD SACSLPPYSL PAHIQDDIRE QVKKMALELG VIGLMNVQMA VQGEDIYVLE VNPRASRTVP FVSKCIGASL AKVAARVMAG KTLKEIGFTE EIIPPFFSVK EAVFPFAKFP GVDPILGPEM KSTGEVMGVG DSFAEAFAKA QLGASETLPT GGCAFISVRE DDKPFVADVA RNLVALGFEV VATAGTARMI EAAGLPVRRV NKVTEGRPHV VDMIKNDEVT LIINTTEGRQ SIADSFSIRR NALQHKICIT TTIAGGQAIC EALKFGPEKT VRRLQDLHAG INA //