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Entry: F2K853_PSEBN
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ID   F2K853_PSEBN            Unreviewed;       378 AA.
AC   F2K853;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
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   ORFNames=PSEBR_a767 {ECO:0000313|EMBL:AEA66929.1};
OS   Pseudomonas brassicacearum (strain NFM421).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=994484 {ECO:0000313|EMBL:AEA66929.1, ECO:0000313|Proteomes:UP000006692};
RN   [1] {ECO:0000313|EMBL:AEA66929.1, ECO:0000313|Proteomes:UP000006692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NFM421 {ECO:0000313|EMBL:AEA66929.1,
RC   ECO:0000313|Proteomes:UP000006692};
RX   PubMed=21515771; DOI=10.1128/JB.00411-11;
RA   Ortet P., Barakat M., Lalaouna D., Fochesato S., Barbe V., Vacherie B.,
RA   Santaella C., Heulin T., Achouak W.;
RT   "Complete genome sequence of a beneficial plant root-associated bacterium,
RT   Pseudomonas brassicacearum.";
RL   J. Bacteriol. 193:3146-3146(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NFM421;
RA   Ortet P., Barakat M., Lalaouna D., Fochesato S., Barbe V., Santaella C.,
RA   Heulin T., Achouak W.;
RT   "Complete Genome Sequence of a beneficial plant roots-associated bacterium
RT   Pseudomonas brassicacearum.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002585; AEA66929.1; -; Genomic_DNA.
DR   RefSeq; WP_003197697.1; NC_015379.1.
DR   AlphaFoldDB; F2K853; -.
DR   STRING; 994484.PSEBR_a767; -.
DR   GeneID; 57257458; -.
DR   KEGG; pba:PSEBR_a767; -.
DR   HOGENOM; CLU_035901_1_1_6; -.
DR   OMA; CFNTGMT; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000006692; Chromosome.
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};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW   Rule:MF_01209}.
FT   DOMAIN          3..133
FT                   /note="Carbamoyl-phosphate synthase small subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01097"
FT   REGION          1..192
FT                   /note="CPSase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT   ACT_SITE        269
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        353
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        355
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   378 AA;  40686 MW;  ABA6988D0FB8C919 CRC64;
     MTKPAILALA DGSIFRGEAI GADGQTVGEV VFNTAMTGYQ EILTDPSYAQ QIVTLTYPHI
     GNTGTTPEDA ESDRVWSAGL VIRDLPLVAS NWRNTMSLSD YLKANNVVAI AGIDTRRLTR
     ILREKGAQNG CIMAGDNISE EAAIAAAQGF PGLKGMDLAK VVSTKKQYEW RSTVWDLKTD
     SHATIEASEL PYHVVAYDYG VKLNILRMLV ERGCRVTVVP AQTPAADVLA LKPDGVFLSN
     GPGDPEPCDY AIQAIKDVLE TEIPVFGICL GHQLLALASG AKTLKMGHGH HGANHPVQDL
     DTGVVMITSQ NHGFAVDEAT LPANVRAIHK SLFDGTLQGI ERTDKSAFSF QGHPEASPGP
     NDVAPLFDRF INEMAKRR
//
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