ID   CARA_BACCL              Reviewed;         364 AA.
AC   P52557;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Carbamoyl-phosphate synthase pyrimidine-specific small chain;
DE            EC=6.3.5.5;
DE   AltName: Full=Carbamoyl-phosphate synthetase glutamine chain;
GN   Name=pyrAA;
OS   Bacillus caldolyticus.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 405 / IFO 15313 / YP-T;
RX   MEDLINE=94266723; PubMed=8206848;
RA   Ghim S.Y., Neuhard J.;
RT   "The pyrimidine biosynthesis operon of the thermophile Bacillus
RT   caldolyticus includes genes for uracil phosphoribosyltransferase and
RT   uracil permease.";
RL   J. Bacteriol. 176:3698-3707(1994).
CC   -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC       ADP + phosphate + L-glutamate + carbamoyl phosphate.
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.
CC   -!- SIMILARITY: Belongs to the carA family.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
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DR   EMBL; X73308; CAA51738.1; -; Genomic_DNA.
DR   PIR; I40168; I40168.
DR   HSSP; P00907; 1A9X.
DR   BRENDA; 6.3.5.5; 1670.
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   ATP-binding; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW   Pyrimidine biosynthesis.
FT   CHAIN         1    364       Carbamoyl-phosphate synthase pyrimidine-
FT                                specific small chain.
FT                                /FTId=PRO_0000112248.
FT   DOMAIN      171    358       Glutamine amidotransferase type-1.
FT   REGION        1    167       CPSase.
FT   ACT_SITE    246    246       Nucleophile (By similarity).
FT   ACT_SITE    331    331       By similarity.
FT   ACT_SITE    333    333       By similarity.
SQ   SEQUENCE   364 AA;  40289 MW;  383A54A839F6631F CRC64;
     MKRQLILEDG SFFVGERFGS LKETTGEVVF NTGMTGYQEI LSDPSYCGQI VTMTYPLIGN
     YGINRDDFEA IRPHVHGFIV KEACVKPSNW RGELTLDEYL KEKGIPGLSG IDTRKLTRLI
     RQYGTLKGMI CGLDVDPVEA AAKLRAMEWP RDQVRRVSTK SAYPSPGRGE RIVLIDFGMK
     HGILRELNKR NCDVIVLPYN ATAEEVLGWH PDGVMLSNGP GDPKDVPEAI EMIRGILGKV
     PLFGICLGHQ LFALACGANT EKMKFGHRGS NHPVKDLRTG KVAITSQNHG YTVTHESLSG
     TRLEVTHIAL NDGTVEGLRH LDVPAFTVQY HPEASPGPED ANPLFDEFLA LIREFNKKGE
     VIHA
//