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Database: UniProt
Entry: Q87EB8
LinkDB: Q87EB8
Original site: Q87EB8 
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   05-DEC-2018, entry version 112.
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};
GN   OrderedLocusNames=PD_0399;
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].
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.,
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:
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;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01210}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000255|HAMAP-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
CC       the 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}.
DR   EMBL; AE009442; AAO28279.1; -; Genomic_DNA.
DR   RefSeq; WP_004085673.1; NC_004556.1.
DR   ProteinModelPortal; Q87EB8; -.
DR   SMR; Q87EB8; -.
DR   PRIDE; Q87EB8; -.
DR   EnsemblBacteria; AAO28279; AAO28279; PD_0399.
DR   KEGG; xft:PD_0399; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
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; 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.
DR   PROSITE; PS51855; MGS; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Repeat.
FT   CHAIN         1   1080       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000145068.
FT   DOMAIN      133    328       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      679    876       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      943   1080       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     705    762       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
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       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       299    299       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       299    299       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       301    301       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       830    830       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       847    847       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       847    847       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       849    849       Magnesium or manganese 4.
FT                                {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
//
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