ID   CARA_CHLTE              Reviewed;         366 AA.
AC   Q8KGA2;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 55.
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=CT0066;
OS   Chlorobium tepidum.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=1097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / TLS;
RX   MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA   Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA   Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA   Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA   Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE006470; AAM71314.1; -; Genomic_DNA.
DR   RefSeq; NP_660972.1; -.
DR   HSSP; P00907; 1A9X.
DR   GeneID; 1006486; -.
DR   GenomeReviews; AE006470_GR; CT0066.
DR   KEGG; cte:CT0066; -.
DR   NMPDR; fig|194439.1.peg.66; -.
DR   TIGR; CT0066; -.
DR   HOGENOM; Q8KGA2; -.
DR   OMA; Q8KGA2; LFDGSNC.
DR   BioCyc; CTEP194439:CT_0066-MON; -.
DR   BRENDA; 6.3.5.5; 189605.
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    366       Carbamoyl-phosphate synthase small chain.
FT                                /FTId=PRO_0000112266.
FT   DOMAIN      178    366       Glutamine amidotransferase type-1.
FT   REGION        1    174       CPSase.
FT   ACT_SITE    256    256       Nucleophile (By similarity).
FT   ACT_SITE    340    340       By similarity.
FT   ACT_SITE    342    342       By similarity.
SQ   SEQUENCE   366 AA;  40111 MW;  64AE575C1B19E3FF CRC64;
     MQEIPAILVL ENGSVYRGTA FGHAGEATGE VVFNTSLTGY QEILTDPSYT GQMVVMTYPL
     IGNYGITPND NESKKIWASA LIVREASNVY SNYESTRSLD ATLKEAGVMG LAGIDTRKLV
     REIRQKGAMR AVISTLCDDV AALKAQAAAI PEMTGLDLVQ RVTTGERYTV DNPDAKYHVV
     AFDYGIKTNI IRQLNAEGCK VTVVNAKTTA DEVLAMNPDG IFLSNGPGDP FAVTYAIDTI
     RELAARNSTL PIFGICLGHQ LLSLAFGAKT YKLKFGHHGA NHPVKNLLSN TIEITSQNHG
     FAVEMESLPG ELELTHKNLY DMTVEGIRHR ELPCFSVQYH PEAAPGPHDS HYLFKEFTEL
     MERLKN
//