ID   CARA_BACHK              Reviewed;         365 AA.
AC   Q6HES7;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 41.
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=BT9727_3629;
OS   Bacillus thuringiensis subsp. konkukian.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=180856;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G.,
RA   Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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; AE017355; AAT61300.1; -; Genomic_DNA.
DR   RefSeq; YP_037949.1; -.
DR   GeneID; 2856642; -.
DR   GenomeReviews; AE017355_GR; BT9727_3629.
DR   KEGG; btk:BT9727_3629; -.
DR   HOGENOM; Q6HES7; -.
DR   OMA; Q6HES7; LFDGSNC.
DR   BioCyc; BTHU281309:BT9727_3629-MON; -.
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    365       Carbamoyl-phosphate synthase small chain.
FT                                /FTId=PRO_0000112253.
FT   DOMAIN      170    357       Glutamine amidotransferase type-1.
FT   REGION        1    166       CPSase.
FT   ACT_SITE    245    245       Nucleophile (By similarity).
FT   ACT_SITE    330    330       By similarity.
FT   ACT_SITE    332    332       By similarity.
SQ   SEQUENCE   365 AA;  40377 MW;  0F340C1663AF29EF CRC64;
     MKRQLILEDG TVLIGTGFGG EIEKSGEVVF TTGMTGYQET LSDPSYCGQI VTFTYPLIGN
     YGINRDDFES IHPSVNGLIV NEICDHPSNF RNEISLNDYL KERNIPGLAG IDTRKLTRKI
     RQYGTLRGRL CNMDADVEYI VSQLKATVFT DHVKRVSTKD PYPSPGRGHR VVLVDFGMKH
     GILRELNKRD CDVIVVPYNT TAEEILRLSP DGIMLSNGPG DPKDVPEAIE MLKDIIGKVP
     LFGICLGHQL FALASGANTS KLKFGHRGLN HPVKNIATGK VAITSQNHGY AVEEESVENT
     ELEITHVALN DGTVEGLRHK KFPAFTVQYH PEASAGPEDA NDLFEDFLTM IENFKKEGEE
     LCQNA
//