ID A0A1I6YL40_9GAMM Unreviewed; 1081 AA. AC A0A1I6YL40; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 11-DEC-2019, entry version 10. 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:58228, ChEBI:CHEBI:58359, CC ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01210, ECO:0000256|SAAS:SAAS01124510}; 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; carbamoyl CC phosphate from bicarbonate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01210, CC ECO:0000256|SAAS:SAAS00981844}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000256|HAMAP- CC 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 the CC 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 of CC 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 BioCyc; GCF_900116405:BM388_RS04280-MONOMER; -. 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 Ligase {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00710245}; KW Magnesium {ECO:0000256|SAAS:SAAS00981805}; KW Manganese {ECO:0000256|SAAS:SAAS00459951}; KW Metal-binding {ECO:0000256|SAAS:SAAS00086100}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|PROSITE- KW ProRule:PRU00409, ECO:0000256|SAAS:SAAS00710285}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210, KW ECO:0000256|SAAS:SAAS01000143}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00981845}. FT DOMAIN 133..328 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 683..874 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT REGION 1..403 FT /note="Carboxyphosphate synthetic domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210" FT REGION 941..1081 FT /note="Allosteric domain" FT /evidence="ECO:0000256|HAMAP-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 //