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Database: UniProt
Entry: Q9A4D6
LinkDB: Q9A4D6
Original site: Q9A4D6 
ID   CARB_CAUVC              Reviewed;        1099 AA.
AC   Q9A4D6;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   05-DEC-2018, entry version 124.
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=CC_2900;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter
OS   crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J.,
RA   Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J.,
RA   Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L.,
RA   Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK24862.1; -; Genomic_DNA.
DR   PIR; B87608; B87608.
DR   RefSeq; NP_421694.1; NC_002696.2.
DR   RefSeq; WP_010920738.1; NC_002696.2.
DR   ProteinModelPortal; Q9A4D6; -.
DR   SMR; Q9A4D6; -.
DR   STRING; 190650.CC_2900; -.
DR   PRIDE; Q9A4D6; -.
DR   EnsemblBacteria; AAK24862; AAK24862; CC_2900.
DR   GeneID; 943506; -.
DR   KEGG; ccr:CC_2900; -.
DR   PATRIC; fig|190650.5.peg.2904; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   BioCyc; CAULO:CC2900-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001816; 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_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; 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; Reference proteome;
KW   Repeat.
FT   CHAIN         1   1099       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000144999.
FT   DOMAIN      133    328       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      691    887       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      963   1099       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     717    774       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    403       Carboxyphosphate synthetic domain.
FT   REGION      404    562       Oligomerization domain.
FT   REGION      563    962       Carbamoyl phosphate synthetic domain.
FT   REGION      963   1099       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       841    841       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       858    858       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       858    858       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       860    860       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1099 AA;  118310 MW;  9AA47E8DA93E7C4C CRC64;
     MPKRTDISSI LIIGAGPIVI GQACEFDYSG VQACKALRAE GYRIILVNSN PATIMTDPDV
     ADATYIEPIT PEMVAKIIEK ERPDALLPTM GGQTALNTAL ALEADGTLAK FGVEMIGAKA
     EVIDKAEDRQ KFRDAMDKLG LESPRSRACH TLDEAMEGLE FVGLPAIIRP SFTLAGTGGG
     IAYNVEEFKE IVERGLDLSP TTEVLVEESV LGWKEYEMEV VRDKADNCII VCSIENIDPM
     GVHTGDSITV APALTLTDKE YQWMRAASIA VLREIGVETG GSNVQFAVNP ADGRMVVIEM
     NPRVSRSSAL ASKATGFPIA KVAARLAVGY TLDELKNDIT GGATPASFEP SIDYVVTKIP
     RFAFEKYPGS EPLLTTAMKS VGEVMAIGRT FKESVQKALR GLETGLSGFD EVEIAGADDP
     DNGKEAVIRA LGVPTPDRLR VIAQAFRHGL TVDEVNAACS YEPWFLRQIA EIVRQEGWVK
     AGGLPQTAQG FRELKAQGFS DARLAKLTAS TEKAVRAARQ ALNVRPVFKR IDSCAGEFLA
     STPYMYSTYE FGALGQIPQC ESDPSAAKKA VILGGGPNRI GQGIEFDYCC CHAAFALDQI
     GVESIMVNCN PETVSTDYDT SDRLYFEPLT AEDVLELLHV EMSKGTLAGV IVQFGGQTPL
     KLAHALEEAG VPILGTSPDA IDLAEDRERF QQLLNGLNIA QPENAIARSW DEARAEGDKI
     GFPFVMRPSY VLGGRGMEII RDHEAMERYI AGAGEISLEH PILLDHYLSR ATEVDVDALC
     DGKDVFVAGV LEHIEEAGVH SGDSACSMPP FSLKAETVEE LKRQTVQMAL ALNVRGLMNV
     QFAIEEPHSD NPRIYVLEVN PRASRTVPFV AKTIGQPVAA IAAKIMAGES LASFGLKDVP
     YDHIAVKEAV FPFARFAGVD TVLGPEMRST GEVMGLDWKR DGETGMGPAF ARAFAKSQLG
     GGVKLPTKGT AFVSVKESDK PWIVEPVKLL QAAGFKVLST EGTQAYLAAQ GVQVEHVKKV
     LEGRPHIVDV MKNGGVQLVF NTTEGKQALE DSFEIRRTAL MMKVPYYTTS AGALAAAQAI
     AGAPAEALDV RPLQSYAAE
//
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