ID   CARA_OCEIH              Reviewed;         366 AA.
AC   Q8CXH8;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 49.
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; Synonyms=pyrAA; OrderedLocusNames=OB1490;
OS   Oceanobacillus iheyensis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=182710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / JCM 11309 / KCTC 3954 / HTE831;
RX   MEDLINE=22220767; PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya
RT   Ridge and its unexpected adaptive capabilities to extreme
RT   environments.";
RL   Nucleic Acids Res. 30:3927-3935(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; BA000028; BAC13446.1; -; Genomic_DNA.
DR   RefSeq; NP_692411.1; -.
DR   HSSP; P00907; 1CE8.
DR   GeneID; 1017748; -.
DR   GenomeReviews; BA000028_GR; OB1490.
DR   KEGG; oih:OB1490; -.
DR   NMPDR; fig|221109.1.peg.1492; -.
DR   HOGENOM; Q8CXH8; -.
DR   OMA; Q8CXH8; EADIPFF.
DR   BioCyc; OIHE221109:OB1490-MON; -.
DR   BRENDA; 6.3.5.5; 278212.
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_0000112300.
FT   DOMAIN      172    359       Glutamine amidotransferase type-1.
FT   REGION        1    168       CPSase.
FT   ACT_SITE    247    247       Nucleophile (By similarity).
FT   ACT_SITE    332    332       By similarity.
FT   ACT_SITE    334    334       By similarity.
SQ   SEQUENCE   366 AA;  40740 MW;  10C38A4340928299 CRC64;
     MKKRKLILED GTVFNGTAFG SDAESSGEIV FNTGMTGYQE VITDPSYCGQ FVTLTYPLIG
     NYGINRDDFE TVTPFIHGLV VKEYSEFPSN FRNEETLDEF LQAHNIPGIA NIDTRKLTRI
     IRKHGTMRAV MVDEQKNEQH VIEQLRLAEM PRDQVKRTST IKPYVVPGRG LRVVMVDFGA
     KHGILRELTR RDCHITVVPH NYSAEAILRL KPDGIMLTNG PGDPKDVPEA IEMIKQLLGQ
     IPIFGICLGH QLLALACGAD TEKMKFGHRG ANHPVKDLLA GKTYLTSQNH SYAVNVSSLV
     NTDLELTQIA LNDDTVEGIR HTAFPAFSVQ YHPEASPGPE DTNFLFDEFL NLIKASKVKQ
     GGEVYA
//