ID   CARA_BRUSU              Reviewed;         407 AA.
AC   Q8FZJ8;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 48.
DE   RecName: Full=Carbamoyl-phosphate synthase small chain;
DE            EC=6.3.5.5;
DE   AltName: Full=Carbamoyl-phosphate synthetase glutamine chain;
GN   Name=carA; OrderedLocusNames=BR1483;
OS   Brucella suis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=29461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330 / Biovar 1;
RX   MEDLINE=22247741; PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A.,
RA   Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O.,
RA   Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M.,
RA   Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between
RT   animal and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
CC   -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC       ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from HCO(3)(-): step 1/1.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from HCO(3)(-): step 1/6.
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 carA family.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
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DR   EMBL; AE014291; AAN30394.1; -; Genomic_DNA.
DR   RefSeq; NP_698479.1; -.
DR   HSSP; P00907; 1M6V.
DR   GeneID; 1167166; -.
DR   GenomeReviews; AE014291_GR; BR1483.
DR   KEGG; bms:BR1483; -.
DR   NMPDR; fig|204722.1.peg.1436; -.
DR   TIGR; BR1483; -.
DR   HOGENOM; Q8FZJ8; -.
DR   OMA; Q8FZJ8; LFDGSNC.
DR   BioCyc; BSUI204722:BR_1483-MON; -.
DR   BRENDA; 6.3.5.5; 281610.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hyd...; IEA:HAMAP.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01209; -; 1.
DR   InterPro; IPR006220; Anth_synthII.
DR   InterPro; IPR001317; CarbamoylP_synth_GATase.
DR   InterPro; IPR006274; CarbamoylP_synth_ssu.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR011702; GATASE.
DR   InterPro; IPR017926; GATASE_1.
DR   InterPro; IPR000991; GATase_class1_C.
DR   PANTHER; PTHR11405:SF4; CarA_synth_small; 1.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Glutamine amidotransferase; Ligase;
KW   Nucleotide-binding; Pyrimidine biosynthesis.
FT   CHAIN         1    407       Carbamoyl-phosphate synthase small chain.
FT                                /FTId=PRO_0000112260.
FT   DOMAIN      209    397       Glutamine amidotransferase type-1.
FT   REGION        1    205       CPSase.
FT   ACT_SITE    286    286       Nucleophile (By similarity).
FT   ACT_SITE    370    370       By similarity.
FT   ACT_SITE    372    372       By similarity.
SQ   SEQUENCE   407 AA;  43537 MW;  00181332B34E55E0 CRC64;
     MTETTPKTAP WTVQKRTAVL VLADGTVIEG KGLGATGAVE AEVVFNTALT GYEEILTDPS
     YAGQIVTFTF PHIGNVGANA EDIEDLTPAN RHGAVGAIFK ADITAPSNFR AAEDLDSWLK
     HRGIIALAGI DTRALTALIR ERGAQNAVIA HDPNGNFDLD ALKARAANWC GLENLDLAKD
     VTIGQSLVWK ELPWTLQDGY GEQDAPQYHV VALDFGVKRN ILRLLTGLGA KVTVLPATAT
     AEDVLAHNPD GVFLSNGPGD PAATGEYAVP TIGKLVETGI PLFGICLGHQ MLALALGGRT
     EKMHQGHHGA NHPVKDYTTG KVEIVSMNHG FAVDSDSLPE NVEETHVSLF DGTNCGLRVV
     GKPVFSVQHH PEASPGPQDS HYLFRRFINL IRERKGQAPL PEREQAA
//