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 24-JAN-2024, entry version 129. DE RecName: Full=Carbamoyl phosphate synthase large chain {ECO:0000255|HAMAP-Rule:MF_01210}; DE EC=6.3.4.16 {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 -!- FUNCTION: Large subunit of the glutamine-dependent carbamoyl phosphate CC synthetase (CPSase). CPSase catalyzes the formation of carbamoyl CC phosphate from the ammonia moiety of glutamine, carbonate, and CC phosphate donated by ATP, constituting the first step of 2 biosynthetic CC pathways, one leading to arginine and/or urea and the other to CC pyrimidine nucleotides. The large subunit (synthetase) binds the CC substrates ammonia (free or transferred from glutamine from the small CC subunit), hydrogencarbonate and ATP and carries out an ATP-coupled CC ligase reaction, activating hydrogencarbonate by forming carboxy CC phosphate which reacts with ammonia to form carbamoyl phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01210}. 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 -!- CATALYTIC ACTIVITY: [Carbamoyl phosphate synthase large chain]: CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, CC ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01210}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01210}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01210}; CC Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01210}; 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. Tetramer of CC heterodimers (alpha,beta)4. {ECO:0000255|HAMAP-Rule:MF_01210}. CC -!- DOMAIN: The large subunit is composed of 2 ATP-grasp domains that are CC involved in binding the 2 ATP molecules needed for carbamoyl phosphate CC synthesis. The N-terminal ATP-grasp domain (referred to as the CC carboxyphosphate synthetic component) catalyzes the ATP-dependent CC phosphorylation of hydrogencarbonate to carboxyphosphate and the CC subsequent nucleophilic attack by ammonia to form a carbamate CC intermediate. The C-terminal ATP-grasp domain (referred to as the CC carbamoyl phosphate synthetic component) then catalyzes the CC phosphorylation of carbamate with the second ATP to form the end CC product carbamoyl phosphate. The reactive and unstable enzyme CC intermediates are sequentially channeled from one active site to the CC next through the interior of the protein over a distance of at least 96 CC A. {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 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|HAMAP-Rule:MF_01210" FT REGION 1..403 FT /note="Carboxyphosphate synthetic domain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT REGION 404..554 FT /note="Oligomerization domain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT REGION 555..942 FT /note="Carbamoyl phosphate synthetic domain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT REGION 943..1080 FT /note="Allosteric domain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 129 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 169 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 175 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 176 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 208 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 210 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 215 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 241 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 242 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 243 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 285 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" 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 285 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 299 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" 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 299 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 299 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" 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 301 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 715 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 754 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 756 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 761 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 787 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 788 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 789 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 790 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 830 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" 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 830 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 847 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" 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 847 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210" FT BINDING 847 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" 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" FT BINDING 849 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" 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 //