ID   CARA_PSEAE              Reviewed;         378 AA.
AC   P38098;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, 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=PA4758;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(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;
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; U04992; AAA19046.1; -; Unassigned_DNA.
DR   EMBL; U81259; AAB39250.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG08144.1; -; Genomic_DNA.
DR   PIR; B55580; B55580.
DR   RefSeq; NP_253446.1; NC_002516.2.
DR   RefSeq; WP_003095209.1; NZ_QZGE01000018.1.
DR   AlphaFoldDB; P38098; -.
DR   SMR; P38098; -.
DR   STRING; 287.DR97_2102; -.
DR   MEROPS; C26.954; -.
DR   PaxDb; P38098; -.
DR   PRIDE; P38098; -.
DR   EnsemblBacteria; AAG08144; AAG08144; PA4758.
DR   GeneID; 881751; -.
DR   KEGG; pae:PA4758; -.
DR   PATRIC; fig|208964.12.peg.4984; -.
DR   PseudoCAP; PA4758; -.
DR   HOGENOM; CLU_035901_1_1_6; -.
DR   InParanoid; P38098; -.
DR   OMA; CFNTGMT; -.
DR   PhylomeDB; P38098; -.
DR   BioCyc; PAER208964:G1FZ6-4870-MON; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000002438; 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:0071230; P:cellular response to amino acid stimulus; IDA:PseudoCAP.
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..378
FT                   /note="Carbamoyl-phosphate synthase small chain"
FT                   /id="PRO_0000112304"
FT   DOMAIN          193..378
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"
SQ   SEQUENCE   378 AA;  40828 MW;  ACCB99010A2F9E29 CRC64;
     MTKPAILALA DGSIFRGEAI GADGQTVGEV VFNTAMTGYQ EILTDPSYAQ QIVTLTYPHI
     GNTGTTPEDA EANRVWAAGL IIRDLPLIAS NWRSKQSLPD YLKANGTVAI AGIDTRRLTR
     ILREKGSQNG CILAGADATE ERALELARAF PGLKGMDLAK EVTTAERYEW RSSVWNLESD
     SHPEIPAGEL PYHVVAYDYG VKLNILRMLV ARGCRLTVVP AQTPASEVLA LNPDGIFLSN
     GPGDPEPCDY AIQAIREFLD TEIPVFGICL GHQLLALASG AKTLKMGHGH HGANHPVQDL
     DSGVVMITSQ NHGFAVDEST LPDNLRATHK SLFDGTLQGI ERTDKVAFSF QGHPEASPGP
     HDVAPLFDRF ISAMAERR