CARA_SALTY
ID CARA_SALTY Reviewed; 382 AA.
AC P14845;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 153.
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=STM0066;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=2843375; DOI=10.1111/j.1432-1033.1988.tb14299.x;
RA Kilstrup M., Lu C.D., Abdelal A., Neuhard J.;
RT "Nucleotide sequence of the carA gene and regulation of the carAB operon in
RT Salmonella typhimurium.";
RL Eur. J. Biochem. 176:421-429(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RA Lu C.D., Walthall D.A., Abdelal A.T.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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;
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (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 the
CC large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000305}.
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DR EMBL; M36540; AAA27032.1; -; Genomic_DNA.
DR EMBL; U81260; AAB39255.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19030.1; -; Genomic_DNA.
DR PIR; S01319; S01319.
DR RefSeq; NP_459071.1; NC_003197.2.
DR RefSeq; WP_000597287.1; NC_003197.2.
DR AlphaFoldDB; P14845; -.
DR SMR; P14845; -.
DR STRING; 99287.STM0066; -.
DR MEROPS; C26.954; -.
DR PaxDb; P14845; -.
DR EnsemblBacteria; AAL19030; AAL19030; STM0066.
DR GeneID; 1251584; -.
DR KEGG; stm:STM0066; -.
DR PATRIC; fig|99287.12.peg.68; -.
DR HOGENOM; CLU_035901_1_1_6; -.
DR OMA; CFNTGMT; -.
DR PhylomeDB; P14845; -.
DR BioCyc; SENT99287:STM0066-MON; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000001014; Chromosome.
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..382
FT /note="Carbamoyl-phosphate synthase small chain"
FT /id="PRO_0000112313"
FT DOMAIN 193..380
FT /note="Glutamine amidotransferase type-1"
FT REGION 1..189
FT /note="CPSase"
FT ACT_SITE 269
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 353
FT /evidence="ECO:0000250"
FT ACT_SITE 355
FT /evidence="ECO:0000250"
FT CONFLICT 14
FT /note="Q -> H (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="L -> V (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 41651 MW; 535C0F1FC33BB5BA CRC64;
MIKSALLVLE DGTQFHGRAI GATGSAVGEV VFNTSMTGYQ EILTDPSYSR QIVTLTYPHI
GNVGTNKADE ESSQVHAQGL VIRDLPLIAS NFRNTEDLSS YLKRHNIVAI ADIDTRKLTR
LLREKGAQNG CIIAGDSPDA KLALEKAKAF PGLNGMDLAK EVTTAETYRW TQGSWTLKDG
LPEAKSEDDL PFHVVAYDFG AKRNILRMLV DRGCRLTVVP AQTSAEEVLK MNPDGIFLSN
GPGDPAPCDY AITAIQKFLE TDIPLFGICL GHQLLALASG AKTVKMKFGH HGGNHPVKDM
DRNVVMITAQ NHGFAVDEDS LPANLRVTHK SLFDGTLQGI HRTDKPAFSF QGHPEASPGP
HDAAPLFDHF IELIEQYRQS AK
