(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 145.
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}.
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   SMR; P14845; -.
DR   MEROPS; C26.954; -.
DR   PaxDb; P14845; -.
DR   PRIDE; P14845; -.
DR   EnsemblBacteria; AAL19030; AAL19030; STM0066.
DR   GeneID; 1251584; -.
DR   KEGG; stm:STM0066; -.
DR   PATRIC; fig|99287.12.peg.68; -.
DR   eggNOG; ENOG4105C1M; Bacteria.
DR   eggNOG; COG0505; LUCA.
DR   HOGENOM; HOG000038087; -.
DR   KO; K01956; -.
DR   OMA; CFNTGMT; -.
DR   PhylomeDB; P14845; -.
DR   BioCyc; SENT99287:STM0066-MONOMER; -.
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;
DR   PRODOM; P14845.
DR   SWISS-2DPAGE; P14845.
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
//

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