ID   CARA_LEPIN              Reviewed;         363 AA.
AC   Q8F6R2;
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; OrderedLocusNames=LA_1239;
OS   Leptospira interrogans.
OC   Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=173;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601 / Serogroup Icterohaemorrhagiae / Serovar lai;
RX   MEDLINE=22598143; PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H.,
RA   Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F.,
RA   Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F.,
RA   Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W.,
RA   Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A.,
RA   Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z.,
RA   Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira
RT   interrogans revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
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; AE010300; AAN48438.1; -; Genomic_DNA.
DR   RefSeq; NP_711420.1; -.
DR   HSSP; P00907; 1M6V.
DR   GeneID; 1150582; -.
DR   GenomeReviews; AE010300_GR; LA_1239.
DR   KEGG; lil:LA1239; -.
DR   NMPDR; fig|189518.1.peg.1239; -.
DR   HOGENOM; Q8F6R2; -.
DR   OMA; Q8F6R2; EADIPFF.
DR   BioCyc; LINT189518:LA1239-MON; -.
DR   BRENDA; 6.3.5.5; 258108.
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    363       Carbamoyl-phosphate synthase small chain.
FT                                /FTId=PRO_0000112289.
FT   DOMAIN      177    363       Glutamine amidotransferase type-1.
FT   REGION        1    173       CPSase.
FT   ACT_SITE    253    253       Nucleophile (By similarity).
FT   ACT_SITE    336    336       By similarity.
FT   ACT_SITE    338    338       By similarity.
SQ   SEQUENCE   363 AA;  40261 MW;  58BD2BB8F43D0BEE CRC64;
     MMKAFLVLDN GTIFEGESFG YETESVGEIV FNTSMAGYQE ILTDPSYCNQ IITLTYPMIG
     NYGIHPDNME SSKIQASGLI VKEYVDLPSN FKSEKTLSQF LKEYKIPAIQ GIDTRKLTRF
     IRTNGSPNGG IFVASEYSPS FLEKVKSFPG IINADLAKVV TTSSKYIFGT HTGKKFKLAV
     YDYGVKTNIL RLLDANGFAV TVYPAKTPSE EIMKEGTDAF FLSNGPGDPA PLDYAIASTQ
     KIMEKRYPLF GICLGHQIIG LSLGKKTEKM KFGHRGGNQP VKNLETGQVE ITSQNHGFAV
     IDDQKQDEPI SFLNLNDHTV EGILKSGYPL LTVQYHPESA PGPNDSRYLF QKFYDLVEKT
     KKG
//