CARA_PSEST
ID CARA_PSEST Reviewed; 384 AA.
AC P38099; P20597;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 113.
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;
OS Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=316;
RN [1]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2153657; DOI=10.1128/jb.172.2.630-642.1990;
RA Wong S.C., Abdelal A.T.;
RT "Unorthodox expression of an enzyme: evidence for an untranslated region
RT within carA from Pseudomonas aeruginosa.";
RL J. Bacteriol. 172:630-642(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 10701 / JCM 21571 / JM300;
RX PubMed=8169201; DOI=10.1128/jb.176.9.2532-2542.1994;
RA Kwon D.-H., Lu C.-D., Walthall D.A., Brown T.M., Houghton J.E.,
RA Abdelal A.T.;
RT "Structure and regulation of the carAB operon in Pseudomonas aeruginosa and
RT Pseudomonas stutzeri: no untranslated region exists.";
RL J. Bacteriol. 176:2532-2542(1994).
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 -!- SIMILARITY: Belongs to the CarA family. {ECO:0000305}.
CC -!- CAUTION: PubMed:2153657 sequence was originally thought to originate
CC from Pseudomonas aeruginosa. {ECO:0000305}.
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DR EMBL; M33818; AAA25763.1; -; Genomic_DNA.
DR EMBL; U04993; AAA19049.1; -; Unassigned_DNA.
DR PIR; A35111; A35111.
DR PIR; E55580; E55580.
DR AlphaFoldDB; P38099; -.
DR SMR; P38099; -.
DR STRING; 32042.PstZobell_03590; -.
DR MEROPS; C26.954; -.
DR eggNOG; COG0505; Bacteria.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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.
FT CHAIN 1..384
FT /note="Carbamoyl-phosphate synthase small chain"
FT /id="PRO_0000112307"
FT DOMAIN 197..384
FT /note="Glutamine amidotransferase type-1"
FT REGION 1..193
FT /note="CPSase"
FT ACT_SITE 273
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 357
FT /evidence="ECO:0000250"
FT ACT_SITE 359
FT /evidence="ECO:0000250"
FT CONFLICT 33
FT /note="E -> Q (in Ref. 1; AAA25763)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="D -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="E -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="D -> S (in Ref. 1; AAA25763)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="A -> G (in Ref. 1; AAA25763)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="L -> V (in Ref. 1; AAA25763)"
FT /evidence="ECO:0000305"
FT CONFLICT 324..325
FT /note="SL -> AV (in Ref. 1; AAA25763)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="G -> S (in Ref. 1; AAA25763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 41488 MW; DEE8544C35B3D5C6 CRC64;
MTKPATTPAI LALADGSIFR GESIGADGQT IGEVVFNTAM TGYQEILTDP SYAKQIVTLT
YPHVGNTGTT PQDAESWKVW AAGLVIRDLP LLASNWRNKQ SLPDYLKEND TVAIAGIDTR
RLTRILREKG AQNGCILAGA DATEEKALEL ARSFPGLKGM DLAKEVSVKE RYEWRYSLWN
LETDSHPEIP ASELPYHVVA YDYGVKYNIL RMLVARGCRV TVLPAQTPAS EALALNPDGI
FLANGPGDPE PCDYAIRAIQ EVLETDIPVF GICLGHQLLA LASGAITVKM PSGHHGANHP
VQDLETGVVM ITSQNHGFCA DEASLPANLR ATHKSLFDGT LQGIERTDKV AFGFQGHPEA
SPGPCDVAPL FDRFISAMAP VVDR
