ID   CARA_DESVM              Reviewed;         376 AA.
AC   Q8KZA0; B8DIL3;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 43.
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=DvMF_2370;
OS   Desulfovibrio vulgaris (strain Miyazaki F / DSM 19637).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kitamura M., Numata S., Katsura S., Inoue H.;
RT   "The nucleotide sequences of fur, rbr, rlp, and prfC of Desulfovibrio
RT   vulgaris (Miyazaki F).";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Hazen T.C., Richardson P.;
RT   "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; AB090267; BAC10584.1; -; Genomic_DNA.
DR   EMBL; CP001197; ACL09311.1; -; Genomic_DNA.
DR   RefSeq; YP_002436779.1; -.
DR   HSSP; P00907; 1M6V.
DR   GeneID; 7174304; -.
DR   GenomeReviews; CP001197_GR; DvMF_2370.
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    376       Carbamoyl-phosphate synthase small chain.
FT                                /FTId=PRO_0000112273.
FT   DOMAIN      191    376       Glutamine amidotransferase type-1.
FT   REGION        1    187       CPSase.
FT   ACT_SITE    266    266       Nucleophile (By similarity).
FT   ACT_SITE    349    349       By similarity.
FT   ACT_SITE    351    351       By similarity.
SQ   SEQUENCE   376 AA;  41137 MW;  20D227856DAAE83E CRC64;
     MRAFLALEDG FVLEGRSFTG RGESGGEVIF NTGMTGYQEV LTDPSYAGQM VCMTYPLIGN
     YGVTAEDMES GKVHVEAFIV KECCRTPSNW RAIMSLPDYL AQHGVMGIEG IDTRALTRHL
     RINGAMRGII STETDDRDEL VRRARALPTM EGQNLVTRVA PATPYRWDGT RPQPVQLAAD
     GAYAWPGTGP RLVVYDYGIK WNILRLLTDQ GFDLLVVPPS FTAMQVAASG AEAVFLSNGP
     GDPATLTDEV REIRVMTERM PVAGICLGHQ LLGHALGGTT HKLKFGHHGC NHPVKDLVTG
     HIEISSQNHG FCVDIESVPD VEITHVNLND GTLEGFAHKT RPILAVQHHP EASPGPTDSR
     YFFARFRGMV REAVGR
//