ID A0A1T5MKP9_9BACT Unreviewed; 370 AA.
AC A0A1T5MKP9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Carbamoyl phosphate synthase small chain {ECO:0000256|HAMAP-Rule:MF_01209};
DE EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01209};
DE AltName: Full=Carbamoyl phosphate synthetase glutamine chain {ECO:0000256|HAMAP-Rule:MF_01209};
GN Name=carA {ECO:0000256|HAMAP-Rule:MF_01209};
GN ORFNames=SAMN05660236_5588 {ECO:0000313|EMBL:SKC88439.1};
OS Ohtaekwangia koreensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Ohtaekwangia.
OX NCBI_TaxID=688867 {ECO:0000313|EMBL:SKC88439.1, ECO:0000313|Proteomes:UP000190961};
RN [1] {ECO:0000313|EMBL:SKC88439.1, ECO:0000313|Proteomes:UP000190961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25262 {ECO:0000313|EMBL:SKC88439.1,
RC ECO:0000313|Proteomes:UP000190961};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Small subunit of the glutamine-dependent carbamoyl phosphate
CC synthetase (CPSase). CPSase catalyzes the formation of carbamoyl
CC phosphate from the ammonia moiety of glutamine, carbonate, and
CC phosphate donated by ATP, constituting the first step of 2 biosynthetic
CC pathways, one leading to arginine and/or urea and the other to
CC pyrimidine nucleotides. The small subunit (glutamine amidotransferase)
CC binds and cleaves glutamine to supply the large subunit with the
CC substrate ammonia. {ECO:0000256|HAMAP-Rule:MF_01209}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01209};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; Evidence={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. {ECO:0000256|HAMAP-
CC 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. Tetramer of
CC heterodimers (alpha,beta)4. {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; FUZU01000005; SKC88439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5MKP9; -.
DR STRING; 688867.SAMN05660236_5588; -.
DR OrthoDB; 9804328at2; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000190961; Unassembled WGS sequence.
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; PR00097; ANTSNTHASEII.
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:UP000190961}.
FT DOMAIN 3..133
FT /note="Carbamoyl-phosphate synthase small subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01097"
FT REGION 1..175
FT /note="CPSase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT ACT_SITE 252
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 338
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 340
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 47
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 224
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 226
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 253
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 256
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 294
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 296
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 297
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
SQ SEQUENCE 370 AA; 40627 MW; 5778A1F797E2E1AE CRC64;
MQKKAYLLLE DGLLVEGTAI GKIGTSGGEI CFNTGMTGYQ EIYTDPSYYG QIIVNTTSHI
GNYGALDEEQ ESSQAQIAGL VVNDFAKEFS RKSAKESLQS YLETTGIVGI ADVDTRMLVR
YLRSKGAMNA IISSELSPDQ LMQELKKIPS MDGLELSSRV TTKEAYFVGD KDASIKIAVL
DLGIKKSIVE NLAERGCYCK VFPAKTTFEE MSSWKPDGYF ISNGPGDPSA MDYAIKTVKQ
TLESEKPVFG ICLGHQLLAL ASGVSTYKMH HGHRGLNHPV KNLVTGKGEM TSQNHGFAVS
EKDIDKNPNV EVTHVHLNDS TIMGIRRKDK KAFSVQYHPE ASPGPHDSRY LFDDFVTMIK
SEVKDPSTVS
//
