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Database: UniProt
Entry: Q63V92_BURPS
LinkDB: Q63V92_BURPS
Original site: Q63V92_BURPS 
ID   Q63V92_BURPS            Unreviewed;       381 AA.
AC   Q63V92;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   24-JAN-2024, entry version 131.
DE   RecName: Full=Carbamoyl-phosphate synthase small chain {ECO:0000256|ARBA:ARBA00019036, ECO:0000256|HAMAP-Rule:MF_01209};
DE            EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738, ECO:0000256|HAMAP-Rule:MF_01209};
DE   AltName: Full=Carbamoyl-phosphate synthetase glutamine chain {ECO:0000256|ARBA:ARBA00030197, ECO:0000256|HAMAP-Rule:MF_01209};
GN   Name=carA {ECO:0000256|HAMAP-Rule:MF_01209,
GN   ECO:0000313|EMBL:CAH35347.1};
GN   Synonyms=pyrA {ECO:0000313|EMBL:CAH35347.1};
GN   OrderedLocusNames=BPSL1349 {ECO:0000313|EMBL:CAH35347.1};
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH35347.1, ECO:0000313|Proteomes:UP000000605};
RN   [1] {ECO:0000313|EMBL:CAH35347.1, ECO:0000313|Proteomes:UP000000605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243 {ECO:0000313|EMBL:CAH35347.1,
RC   ECO:0000313|Proteomes:UP000000605};
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA   Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA   Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA   Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA   Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA   Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA   Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA   Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA   Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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         Evidence={ECO:0000256|ARBA:ARBA00001777, ECO:0000256|HAMAP-
CC         Rule:MF_01209};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC       phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077,
CC       ECO:0000256|HAMAP-Rule:MF_01209}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004812, ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01209}.
CC   -!- SIMILARITY: Belongs to the CarA family. {ECO:0000256|ARBA:ARBA00007800,
CC       ECO:0000256|HAMAP-Rule:MF_01209}.
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DR   EMBL; BX571965; CAH35347.1; -; Genomic_DNA.
DR   RefSeq; WP_004198695.1; NZ_CP009538.1.
DR   RefSeq; YP_107974.1; NC_006350.1.
DR   AlphaFoldDB; Q63V92; -.
DR   STRING; 272560.BPSL1349; -.
DR   GeneID; 56595276; -.
DR   KEGG; bps:BPSL1349; -.
DR   PATRIC; fig|272560.51.peg.131; -.
DR   eggNOG; COG0505; Bacteria.
DR   OMA; CFNTGMT; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000000605; Chromosome 1.
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-UniRule.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 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   NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR   PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01209};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01209,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01209};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01209}; Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000605}.
FT   DOMAIN          6..136
FT                   /note="Carbamoyl-phosphate synthase small subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01097"
FT   REGION          1..191
FT                   /note="CPSase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT   ACT_SITE        268
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        352
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        354
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   381 AA;  40653 MW;  FB469FB257A89713 CRC64;
     MLPSFSPALL ALADGTVFRG YSIGAAGHTI GEVVFNTAIT GYQEILTDPS YARQIVTLTY
     PHIGNVGVNA EDVEATKVHA AGLIVRDLPA LASNFRMART LGDYLRDEGV VAIAGIDTRK
     LTRILRDKGA QNGCILTGSD DETKALALAR SFPGLAGMDL AKVVSTAKPF EWKQTEWRLG
     SGYGMQETPR YRVVAFDFGV KYNILRMLAE RGCHVSVLPA QSSAADALAL NPDGIFLSNG
     PGDPQPCDYA IAATREFIER GVPTFGICLG HQIMGLALGA KTLKMKTGHH GANHPVKDLA
     NGRVVITSQN HGFAVDADSL PANARATHVS LFDGTLQGFE LTDKPAFCFQ GHPEASPGPH
     DIGYLFDRFT ALMDAAKARS A
//
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