ID A0A2H9SGB5_9GAMM Unreviewed; 1079 AA. AC A0A2H9SGB5; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 25-APR-2018, entry version 3. 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=CK424_04040 {ECO:0000313|EMBL:PJD92759.1}; OS Legionella sp. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=459 {ECO:0000313|EMBL:PJD92759.1}; RN [1] {ECO:0000313|EMBL:PJD92759.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BC.3.72 {ECO:0000313|EMBL:PJD92759.1}; RX PubMed=29097994; DOI=.3389/fmicb.2017.02036; RA Zhang Y., Kitajima M., Whittle A.J., Liu W.T.; RT "Benefits of Genomic Insights and CRISPR-Cas Signatures to Monitor RT Potential Pathogens across Drinking Water Production and Distribution RT Systems."; RL Front. Microbiol. 8:2036-2036(2017). 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PJD92759.1}. 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; PEQK01000012; PJD92759.1; -; Genomic_DNA. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. 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; 1. 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, 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 Repeat {ECO:0000256|HAMAP-Rule:MF_01210, KW ECO:0000256|SAAS:SAAS00981845}. FT DOMAIN 133 328 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. FT DOMAIN 676 867 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. FT REGION 1 403 Carboxyphosphate synthetic domain. FT {ECO:0000256|HAMAP-Rule:MF_01210}. FT REGION 935 1079 Allosteric domain. {ECO:0000256|HAMAP- FT Rule:MF_01210}. SQ SEQUENCE 1079 AA; 118946 MW; 13A306C3BD61B2E6 CRC64; MPKRTDIQSI LILGAGPIVI GQACEFDYSG TQAVRALKRE GYRVILINSN PATIMTDPEL ADATYIEPVL WPEVAAVIKK ERPDALLPTM GGQTALNCAL DLVREGVLEA YGVELIGASE DAIDKAENRD KFRTLMQEIG LDMPRSMIAH SLDEAMVALG VLGFPAIIRP SFTMGGTGGG IAYNLEEFES ICLRGLDLSP TRELLIDESV LGWKEYEMEV VRDRHDNCII VCSIENLDPM GVHTGDSITV APAQTLTDKE YQRMRDAAIK VLRAVGVDTG GSNVQFAVNP EDGRLLVVEM NPRVSRSSAL ASKATGFPIA KIAALLAVGY TLDELKNDIT DGKTPASFEP TLDYVVTKMP RFNFDKFPQT SKTLTTQMKS VGEVMAIGAN FQESLQKAIR GLEIDRYGLH PLFADQEMSV LRGYLQEPTP DRLWYIADAF RLGMSLEEIH KESRVDPWFL AQIQELVAFE ELVLGKTLEH LDEKTLRLLK QRGFSDVYLA RLLGCHEREV RQHRLSLGIK PVYQRIDSCA AEFSSDTAYL YSCYQSVCES RPDFSRPKIM ILGGGPNRIG QGIEFDYCCV HAAFALRDAG YETIMVNCNP ETVSTDVETT DRLYFDPVTL EDVLAVYDLE KPIGVIVDYG GQTPLKLAQE LANHGVPILG TSPDAIDEAE DRERFQQLVT RLGLHQPANG TVRSESEAIA LAQRIGYPLV VRPSYVLGGR AMEIVYHETD LRRYLEHAVR VSNDSPVLLD KFLEDAIEVD IDAVCDGEDV LIGAIMEHIE QAGIHSGDSA CTLPPFSLSV VVQQDLKEQL QLMAKALHVV GLVNAQFAIQ GDDIYVLEVN PRASRTVPFV SKATGLPLAK IAARCKVGLS LKQQGLLHIQ QVPGFYSVKL PVFPFIKFSG VDSILGPEMK STGEVMGIAK RFGQAYAKAQ RGAGCDIVNR RRAFLSVRDT DKSRIGEIAK RLIALGFDIV ATRGTTAVIQ AAGIACERVF KVAEGRPHVV DHIKNHEIDF IVNTTEGKQA IADSFDIRRS ALQYKVSYTT TLSGAEAACL AMKYEERDTV TRLQDLHERF SYAKTSNDG //