ID A0A1I6YL40_9GAMM Unreviewed; 1081 AA. AC A0A1I6YL40; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 05-DEC-2018, entry version 6. 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 ORFNames=SAMN04487956_10620 {ECO:0000313|EMBL:SFT51196.1}; OS Halomonas saccharevitans. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=416872 {ECO:0000313|EMBL:SFT51196.1, ECO:0000313|Proteomes:UP000199594}; RN [1] {ECO:0000313|EMBL:SFT51196.1, ECO:0000313|Proteomes:UP000199594} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CGMCC 1.6493 {ECO:0000313|EMBL:SFT51196.1, RC ECO:0000313|Proteomes:UP000199594}; RA de Groot N.N.; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. 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:456216, ChEBI:CHEBI:58228, CC ChEBI:CHEBI:58359; EC=6.3.5.5; Evidence={ECO:0000256|HAMAP- CC 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; FPAQ01000006; SFT51196.1; -; Genomic_DNA. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000199594; Unassembled WGS sequence. 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; 1. 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|HAMAP-Rule:MF_01210, ECO:0000256|PROSITE- KW ProRule:PRU00409, ECO:0000256|SAAS:SAAS00710217}; KW Complete proteome {ECO:0000313|Proteomes:UP000199594}; 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|HAMAP-Rule:MF_01210, KW ECO:0000256|PROSITE-ProRule:PRU00409, ECO:0000256|SAAS:SAAS00710285}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210, KW ECO:0000256|SAAS:SAAS01000143}; KW Reference proteome {ECO:0000313|Proteomes:UP000199594}; 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 683 874 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. FT REGION 1 403 Carboxyphosphate synthetic domain. FT {ECO:0000256|HAMAP-Rule:MF_01210}. FT REGION 941 1081 Allosteric domain. {ECO:0000256|HAMAP- FT Rule:MF_01210}. SQ SEQUENCE 1081 AA; 118392 MW; 22A020A2B5B38DD6 CRC64; MPKRTDIKSI LIIGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN PATIMTDPAM ADATYIEPIT WQTVEKIIEA ERPDVILPTM GGQTALNCAL ELDKHGVLAK YGVEMIGANA DAINKAEDRD LFDKAMKNIG LECPKAKVAH SMQEAWEIQA ELGFPTIIRP SYTMGGSGGG VAYNKEEFDE ICQRGFELSN NHELLIDESL LGWKEYEMEV VRDKHDNCII VCAIENFDPM GVHTGDSITV APAQTLTDKE YQIMRDASLA VLREIGVETG GSNVQFGMDP QTGRMVVIEM NPRVSRSSAL ASKATGFPIA KIAAKLAVGY TLDELQNDIT GGRTPASFEP AIDYVVTKIP RFTFEKFPQA NDRLTTQMKS VGEVMAIGRT FQESLHKALR GMETGNDGLD PVFPEQKPGA FTAEAMAHIK GELQAAGAER IFFVADAMRA GMSLEEVFAL TNIDRWFLVQ IEELIRIEAE VATRPLSEFT PRELYRLKRK GFSDARLARL LGVAEKEFRR TRQRAGIRPV YKRVDTCAAE FASDTAYMYS TYEEECEAEV SDKKKIMVLG GGPNRIGQGI EFDYCCVHAA FAMHDDGYET IMVNCNPETV STDYDTSDRL YFEPVTLEDV LEIADKEQPV GVIVQFGGQT PLKLARELEA AGVPIIGTTP DAIDRAEDRE RFQQMIDKLG LKQPPNATAR SFDEAFAKAE AIGYPLVVRP SYVLGGRAME IVYDASELEN YMTHAVKVSN DSPVLLDHFL NAAIEIDIDA VSDGSQVVIG GIMQHIEQAG VHSGDSACAL PPYSLPAEVQ DAMREQVKQM AVELGVKGLM NVQLAWQDDE IYVIEVNPRA SRTVPFVSKC IGTSLAQVAA RCMAGQTLTE QGFEAEIVPH FYSVKEAVFP FNKFPGVDPI LSPEMKSTGE VMGSGDTFAE AFYKAQLGAG EAIPRLEGKR KAFLSVRDPD KAGIIEVARS LVTLGFTLCA TRGTAKALEG TELSVQIVNK VYEGRPHIVD LLKNDEVAYI VNTTEGRQAI NDSSVIRRTA LARKVPYATT LAGANAVCMA LEYGNAITVR RLQELHAGAT Q //