ID   CARA_BIFLO              Reviewed;         407 AA.
AC   Q8G816;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 47.
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=BL0067;
OS   Bifidobacterium longum.
OC   Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=216816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   MEDLINE=22294977; PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B.,
RA   Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M.,
RA   Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation
RT   to the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(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; AE014295; AAN23933.1; -; Genomic_DNA.
DR   RefSeq; NP_695297.1; -.
DR   HSSP; P00907; 1A9X.
DR   GeneID; 1022933; -.
DR   GenomeReviews; AE014295_GR; BL0067.
DR   KEGG; blo:BL0067; -.
DR   NMPDR; fig|206672.1.peg.66; -.
DR   HOGENOM; Q8G816; -.
DR   OMA; Q8G816; LFDGSNC.
DR   BioCyc; BLON206672:BL0067-MON; -.
DR   BRENDA; 6.3.5.5; 39917.
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    407       Carbamoyl-phosphate synthase small chain.
FT                                /FTId=PRO_0000112257.
FT   DOMAIN      207    405       Glutamine amidotransferase type-1.
FT   REGION        1    203       CPSase.
FT   ACT_SITE    283    283       Nucleophile (By similarity).
FT   ACT_SITE    378    378       By similarity.
FT   ACT_SITE    380    380       By similarity.
SQ   SEQUENCE   407 AA;  44265 MW;  EC2232518EFFFD48 CRC64;
     MSQNESGTIA IPMYDKDDAV LVLEDGQVYV GKPYGALGET TGEIVFATGM TGYQETLTDP
     SYDRQIVVQT FPHIGDTGVN SEDPESSRIW VAGYIVRDPS PNVSNWRAEG SLDDDLAKNG
     IVGLSHIDTR KLVRHLRSAG VMRAGIFSGD ALTDQATGAL KTIEQLLEDV KNTPQMQGLS
     LYDEVSTKET YTIEPCGEYE GKEPLYTVAA VDLGIKGMTP HRMAERGCRV HVVPSTITFA
     EIENLNPDGV FFSNGPGDPE QAGPEIELLR QVLDAGYPFF GICFGNQLLG RALGFGTYKL
     KFGHRGINQP VKDLTTGKVE VTAHNHGFAV DAPIGKQVDA PFENGKYGKV FVSHIDLNDD
     VVEGLQCVDI PAFSVQYHPE AAAGPHDAAY LFDRFCELMK NNSKEGK
//