ID CARB_XYLFT Reviewed; 1080 AA. AC Q87EB8; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2003, sequence version 1. DT 08-NOV-2023, entry version 128. DE RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000255|HAMAP-Rule:MF_01210}; DE EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01210}; DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000255|HAMAP-Rule:MF_01210}; GN Name=carB {ECO:0000255|HAMAP-Rule:MF_01210}; OrderedLocusNames=PD_0399; OS Xylella fastidiosa (strain Temecula1 / ATCC 700964). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=183190; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Temecula1 / ATCC 700964; RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003; RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y., RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A., RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S., RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H., RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L., RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L., RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S., RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F., RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G., RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A., RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L., RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.; RT "Comparative analyses of the complete genome sequences of Pierce's disease RT and citrus variegated chlorosis strains of Xylella fastidiosa."; RL J. Bacteriol. 185:1018-1026(2003). 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:0000255|HAMAP- CC Rule:MF_01210}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl CC phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01210}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP- CC Rule:MF_01210}. 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:0000255|HAMAP-Rule:MF_01210}. CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP- CC 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; AE009442; AAO28279.1; -; Genomic_DNA. DR RefSeq; WP_004085673.1; NC_004556.1. DR AlphaFoldDB; Q87EB8; -. DR SMR; Q87EB8; -. DR EnsemblBacteria; AAO28279; AAO28279; PD_0399. DR GeneID; 58015949; -. DR KEGG; xft:PD_0399; -. DR HOGENOM; CLU_000513_1_2_6; -. DR OMA; IEPAGIH; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000002516; 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; 3.40.50.20; -; 2. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2. DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1. DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 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 NCBIfam; TIGR01369; CPSaseII_lrg; 1. DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1. DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1. 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; Carbamoyl phosphate synthetase, large subunit connection domain; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2. DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 2. DR PROSITE; PS50975; ATP_GRASP; 2. DR PROSITE; PS00866; CPSASE_1; 1. DR PROSITE; PS00867; CPSASE_2; 2. DR PROSITE; PS51855; MGS; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Ligase; KW Magnesium; Manganese; Metal-binding; Nucleotide-binding; KW Pyrimidine biosynthesis; Reference proteome; Repeat. FT CHAIN 1..1080 FT /note="Carbamoyl-phosphate synthase large chain" FT /id="PRO_0000145068" FT DOMAIN 133..328 FT /note="ATP-grasp 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT DOMAIN 679..876 FT /note="ATP-grasp 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT DOMAIN 943..1080 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" FT REGION 1..403 FT /note="Carboxyphosphate synthetic domain" FT REGION 404..554 FT /note="Oligomerization domain" FT REGION 555..942 FT /note="Carbamoyl phosphate synthetic domain" FT REGION 943..1080 FT /note="Allosteric domain" FT BINDING 159..216 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 285 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 299 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 299 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 301 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 705..762 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 830 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 847 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 847 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 849 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" SQ SEQUENCE 1080 AA; 117355 MW; 1DBD0B48DC356DC1 CRC64; MPKRTDLRTI LIIGAGPIVI GQACEFDYSG AQACKALRAE GFRVVLVNSN PATIMTDPDM ADAVYIEPIH WRTVEKIITK EKPDALLPTM GGQTALNCAL DLADHGVLEK YGVELIGAKR EAIRMAEDRE LFRVAMQEIG LECPKAEVAK SLERALEIQA KVGFPTIIRP SFTLGGTGGG IAYNRQEFEE IIKRGLELSP VHEVLVEESV LGWKEFEMEV VRDASDNCII VCSIENLDPM GVHTGDSITV APAQTLSDKE YQRLRDASIA VLRKIGVDTG GSNVQFGIDP QTGRVVVIEM NPRVSRSSAL ASKATGFPIA KIAAKLAVGY TLDELKNEIT GGKTPASFEP SIDYVVTKIP RFAFEKFPQA DARLTTQMKS VGEVMAMGRT FAESLQKAVR GLETGKVGLE PTGLDLSSED DLVVLKRELK APGAERLFYV ADAFRAGFAV ADVYALSYID PWFLDQIEEI VAAEGRLVTD GLGSIDGARL RQLKRIGFSD ARIAQLTGTN EVAVRTLRRV LKVKPVYKRV DSCAGEFATG TAYLYSTYEE ECEAAPSDRR KIMILGGGPN RIGQGIEFDY CCVHAALALR EDGFETIMVN CNPETVSTDY DTSDRLYFEP LTLEDVLEIV EVEHPVGVIV QYGGQTPLKL AKALEANGVP VIGTSPESID LAEDRERFQR LVQQLGLRQP PNCTARTADE ALVLAREIGY PLVVRPSYVL GGRAMEIVYS EADLARYVRD AVKVSNDSPV LLDRFLDNAV EVDVDIIADP EGQVLIGGVM EHIEEAGVHS GDSSCSLPPY SLSAATQDDL RRQVIRLAQA LNVIGLMNTQ FAIQSNDDGS DIVYLLEVNP RASRTVPFVS KATGVPLAKI AARCMTGKTL AEQSVTCEVV PAYYAVKEAI FPFAKLQGVD PILGPEMRST GEVMGVGRSF AAAFARAQEA GDIRAPQPGR AFVSVRDPDK KRVLPVVLAL VERGFGVVAT AGTYAWLQQN GVACEVVNKV AEGRPHIVDL IKNGEIVYII NTTEGRAAIA DSFSIRREAL QHCVTYSTTI AGAKALVNSL EFRGTGPVWS LQELHKELQV //