ID B2V5M5_SULSY Unreviewed; 376 AA.
AC B2V5M5;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 29-MAY-2013, entry version 37.
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=SYO3AOP1_1361;
OS Sulfurihydrogenibium sp. (strain YO3AOP1).
OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC Sulfurihydrogenibium.
OX NCBI_TaxID=436114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YO3AOP1;
RX PubMed=19136599; DOI=10.1128/JB.01645-08;
RA Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the
RT Aquificales.";
RL J. Bacteriol. 191:1992-1993(2009).
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 bicarbonate: step 1/1.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
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; CP001080; ACD66969.1; -; Genomic_DNA.
DR RefSeq; YP_001931523.1; NC_010730.1.
DR ProteinModelPortal; B2V5M5; -.
DR STRING; 436114.SYO3AOP1_1361; -.
DR EnsemblBacteria; ACD66969; ACD66969; SYO3AOP1_1361.
DR GeneID; 6331104; -.
DR KEGG; sul:SYO3AOP1_1361; -.
DR PATRIC; 23767593; VBISulSp94719_1421.
DR eggNOG; COG0505; -.
DR HOGENOM; HOG000038087; -.
DR KO; K01956; -.
DR OMA; RDSHYLF; -.
DR ProtClustDB; PRK12564; -.
DR BioCyc; SSP436114:GI6I-1410-MONOMER; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR GO; GO:0070409; P:carbamoyl phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0006543; P:glutamine catabolic process; IEA:InterPro.
DR Gene3D; 3.50.30.20; -; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1; -.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR017926; GATASE.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF52021; CP_synthsmall; 1.
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 DOMAIN 190 376 Glutamine amidotransferase type-1 (By
FT similarity).
FT REGION 1 186 CPSase (By similarity).
FT ACT_SITE 266 266 Nucleophile (By similarity).
FT ACT_SITE 350 350 By similarity.
FT ACT_SITE 352 352 By similarity.
SQ SEQUENCE 376 AA; 42567 MW; 4CF1E689D1000A73 CRC64;
MERAILALED GHFFYGYAFS GFKLKETDGE VIFNTSMTGY QEILTDPSYK GQIVVMTGAE
IGNYGINDED SQSDRVWVNG FVVKDVPAIY SNYRAKKSLK EYLEESNVIG IFGVDTRAVV
RVLRDYGVMK GYIGIGDISP QEAVRKARSI PDISELNLVK EVSTSKVYRW TQKSWKWPEG
YTEQTEFHYK VAVIDYGVKK DILRLLADRN LELICFPHNV SAEEVLSINP DGIFLSNGPG
DPAILTYQIQ QIKKLIASEK PIFGICLGHQ LLSWAFGSRT YKLEFGHHGG NHPVKNLKTG
KVEITAQNHN YATDESKLPQ DVEITHINLN DNTVEGMRHK NYPVFSIQHH PEAAPGPHDS
FYIFDEFYNL IKACKK
//
