CARA_VIBCH
ID CARA_VIBCH Reviewed; 379 AA.
AC Q9KPH8;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Carbamoyl-phosphate synthase small chain {ECO:0000255|HAMAP-Rule:MF_01209};
DE EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01209};
DE AltName: Full=Carbamoyl-phosphate synthetase glutamine chain {ECO:0000255|HAMAP-Rule:MF_01209};
GN Name=carA {ECO:0000255|HAMAP-Rule:MF_01209}; OrderedLocusNames=VC_2390;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01209};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01209}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP-
CC Rule:MF_01209}.
CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC promotes the hydrolysis of glutamine to ammonia, which is used by the
CC large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000255|HAMAP-Rule:MF_01209}.
CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000255|HAMAP-
CC Rule:MF_01209}.
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DR EMBL; AE003852; AAF95533.1; -; Genomic_DNA.
DR PIR; E82083; E82083.
DR RefSeq; NP_232020.1; NC_002505.1.
DR RefSeq; WP_000045131.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KPH8; -.
DR SMR; Q9KPH8; -.
DR STRING; 243277.VC_2390; -.
DR MEROPS; C26.954; -.
DR DNASU; 2613059; -.
DR EnsemblBacteria; AAF95533; AAF95533; VC_2390.
DR GeneID; 57740998; -.
DR KEGG; vch:VC_2390; -.
DR PATRIC; fig|243277.26.peg.2276; -.
DR eggNOG; COG0505; Bacteria.
DR HOGENOM; CLU_035901_2_1_6; -.
DR OMA; CFNTGMT; -.
DR BioCyc; VCHO:VC2390-MON; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.880; -; 1.
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; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
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; SSF52021; 1.
DR SUPFAM; SSF52317; SSF52317; 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 Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..379
FT /note="Carbamoyl-phosphate synthase small chain"
FT /id="PRO_0000112343"
FT DOMAIN 193..379
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT REGION 1..189
FT /note="CPSase"
FT ACT_SITE 269
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT ACT_SITE 353
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT ACT_SITE 355
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
SQ SEQUENCE 379 AA; 40922 MW; B347FC090E9B9318 CRC64;
MSKSALLVLE DGTVFRGVSI GADGISVGEV VFNTSMTGYQ EILTDPSYSQ QIVTLTYPHI
GNTGTNSEDE ESTAIHAQGL VIRDLPLIAS NFRSEQSLSD YLKSQNIVGI ADIDTRKLTR
ILREKGAQNG CIMAGDNLDE ALALAKAKEF PGLKGMDLAK VVSTKEAYAW KQGSWTLEGG
LPEAKADSEL PYHVVAYDFG AKRNILRMLV DRGCRLTVVP AQTSAEDVLA LNPDGVFLSN
GPGDPEPCTY AIEATRVFLE KNIPVFGICL GHQILALASG AKTVKMKFGH HGANHPVKDL
DRGVVMITSQ NHGFAADEAT LPDNLRATHK SLFDGSLQGI HRTDKPAFSF QGHPEASPGP
HDAAPLFDHF IELIKQFRA
