ID A0A0R1HR74_9LACO Unreviewed; 359 AA.
AC A0A0R1HR74;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=FC96_GL000265 {ECO:0000313|EMBL:KRK49341.1};
OS Secundilactobacillus kimchicus JCM 15530.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1302272 {ECO:0000313|EMBL:KRK49341.1, ECO:0000313|Proteomes:UP000050911};
RN [1] {ECO:0000313|EMBL:KRK49341.1, ECO:0000313|Proteomes:UP000050911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15530 {ECO:0000313|EMBL:KRK49341.1,
RC ECO:0000313|Proteomes:UP000050911};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01209,
CC ECO:0000256|PROSITE-ProRule:PRU00605}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRK49341.1}.
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DR EMBL; AZCX01000001; KRK49341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1HR74; -.
DR STRING; 1302272.FC96_GL000265; -.
DR PATRIC; fig|1302272.5.peg.262; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000050911; 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-KW.
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|ARBA:ARBA00022962,
KW ECO:0000256|HAMAP-Rule:MF_01209};
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:UP000050911}.
FT DOMAIN 4..134
FT /note="Carbamoyl-phosphate synthase small subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01097"
FT REGION 1..171
FT /note="CPSase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT ACT_SITE 335
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 220
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 222
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 249
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 293
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
SQ SEQUENCE 359 AA; 39388 MW; 20D2E98FC5104961 CRC64;
MEMTQRYLIL EDGSVYAGNG FGAGATTTGE IVFNTSMVGY QEVVTNQIYH NQIIVYSQPI
IGATGISHDS YESILPTAKG MVVRDVATIS KNRQRSLSLD QFLKQHNIPG ISDVDTRQLI
RKLQSVGTIK GSIVDVADDH AFDQLHATVL TNQQVAQVAT PKPYPNPNTG YNVVVIDFGL
KHGILRQLSQ RHCNVTVLPW NADAQAIISL DPDGVILSTG PGSPLDVPES VLEMVRTIQE
RIPLFAVGLG HELFALANGA SMTRLGTAHH GPNHPIRKII TNDIIYAEEA QEYVVDSETV
DRNRLITTYL DLIDGSIQGL RHRDYPAFSV QFFPDGAPGP HDSVDLFDEF MEIMGTREG
//
