ID CARB_XYLFT STANDARD; PRT; 1080 AA. AC Q87EB8; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 13-SEP-2005 (Rel. 48, Last annotation update) DE Carbamoyl-phosphate synthase large chain (EC 6.3.5.5) (Carbamoyl- DE phosphate synthetase ammonia chain). GN Name=carB; OrderedLocusNames=PD0399; OS Xylella fastidiosa (strain Temecula1 / ATCC 700964). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=183190; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22421331; PubMed=12533478; RX DOI=10.1128/JB.185.3.1018-1026.2003; RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., RA Miyaki C.Y., Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., RA Takita M.A., Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., RA Goldman M.H.S., Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., RA Carrer H., Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., RA Coutinho L.L., Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., RA Marino C.L., Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., RA Baia G.S., Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., RA da Cunha A.F., Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., RA Leoni S.G., Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., RA de Souza A.A., Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., RA Civerolo E.L., Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., RA Kitajima J.P.; RT "Comparative analyses of the complete genome sequences of Pierce's RT disease and citrus variegated chlorosis strains of Xylella RT fastidiosa."; RL J. Bacteriol. 185:1018-1026(2003). CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + CO(2) + H(2)O = 2 ADP + CC phosphate + L-glutamate + carbamoyl phosphate. CC -!- COFACTOR: Binds 3 manganese ions per subunit (By similarity). CC -!- PATHWAY: Arginine biosynthesis. CC -!- PATHWAY: Pyrimidine biosynthesis; first step. 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 (By CC similarity). CC -!- SIMILARITY: Belongs to the carB family. CC -!- SIMILARITY: Contains 2 ATP-grasp domains. 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; AE012554; AAO28279.1; -; Genomic_DNA. DR HSSP; P00968; 1M6V. DR HAMAP; MF_01210; -; 1. DR InterPro; IPR006275; CarA_L_glu. DR InterPro; IPR005483; CPase_L. DR InterPro; IPR005480; CPase_L_D3. DR InterPro; IPR005481; CPase_L_N. DR InterPro; IPR005479; Cphp_synth_L_D2. DR InterPro; IPR004362; MG_synth_like. DR Pfam; PF00289; CPSase_L_chain; 2. DR Pfam; PF02786; CPSase_L_D2; 2. DR Pfam; PF02787; CPSase_L_D3; 1. DR Pfam; PF02142; MGS; 1. DR PRINTS; PR00098; CPSASE. DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1. DR PROSITE; PS50975; ATP_GRASP; 2. DR PROSITE; PS00866; CPSASE_1; 1. DR PROSITE; PS00867; CPSASE_2; 2. KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Complete proteome; Ligase; Manganese; Metal-binding; KW Nucleotide-binding; Pyrimidine biosynthesis; Repeat. FT DOMAIN 133 328 ATP-grasp 1. FT DOMAIN 679 876 ATP-grasp 2. FT NP_BIND 153 210 ATP (Potential). FT NP_BIND 303 354 ATP (Potential). FT REGION 1 403 Carboxyphosphate synthetic domain. FT REGION 404 554 Oligomerization domain. FT REGION 555 942 Carbamoyl phosphate synthetic domain. FT REGION 943 1080 Allosteric domain. FT METAL 285 285 Manganese 1 (By similarity). FT METAL 299 299 Manganese 1 and 2 (By similarity). FT METAL 301 301 Manganese 2 (By similarity). FT METAL 830 830 Manganese 3 (By similarity). FT METAL 847 847 Manganese 3 (By similarity). 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 //