ID   CARA_COREF              Reviewed;         400 AA.
AC   Q8FT41;
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=CE1730;
OS   Corynebacterium efficiens.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=152794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   MEDLINE=22723752; PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E.,
RA   Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K.,
RA   Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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; BA000035; BAC18540.1; -; Genomic_DNA.
DR   RefSeq; NP_738340.1; -.
DR   HSSP; P00907; 1CE8.
DR   GeneID; 1034230; -.
DR   GenomeReviews; BA000035_GR; CE1730.
DR   KEGG; cef:CE1730; -.
DR   NMPDR; fig|196164.1.peg.1730; -.
DR   HOGENOM; Q8FT41; -.
DR   OMA; Q8FT41; LFDGSNC.
DR   BioCyc; CEFF196164:CE1730-MON; -.
DR   BRENDA; 6.3.5.5; 277326.
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    400       Carbamoyl-phosphate synthase small chain.
FT                                /FTId=PRO_0000112270.
FT   DOMAIN      200    395       Glutamine amidotransferase type-1.
FT   REGION        1    199       CPSase.
FT   ACT_SITE    278    278       Nucleophile (By similarity).
FT   ACT_SITE    368    368       By similarity.
FT   ACT_SITE    370    370       By similarity.
SQ   SEQUENCE   400 AA;  42885 MW;  CFEE077BA9504756 CRC64;
     MSNETNANST DSRQGVTNIG SVPAYLVLAD GRTFKGFGFG AIGTTLGEAV FTTAMTGYQE
     TMTDPSYHRQ IVVATAPQIG NTGWNEEDNE SHDGSIWVAG LVIRDLAVRV SNWRATTTLQ
     EEMAKQGVVG IGGIDTRALV RHIRNEGAVP AGIFSGADAE RPIEELVEIV KSQPSMVGAN
     LAVEVSVDKP YVIEAEGEAR HTVVAYDLGI KQNTPRRFAA RGVRTVIVPA ETPFEEIKQY
     NPSGVFISNG PGDPAAADIM VNIVREVLAA DIPFFGICFG NQILGRAFGM ETYKLKFGHR
     GINVPVKNHI TGKIDITAQN HGFALKGEAG QEFETDFGTA VVTHTCLNDG VVEGVALKSG
     RAYSVQYHPE AAAGPNDASP LFDQFVALMD EDSENQKEEA
//