ID   CARA_LACPL              Reviewed;         364 AA.
AC   P77885; F9URI3;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-MAR-2003, sequence version 2.
DT   02-SEP-2026, entry version 149.
DE   RecName: Full=Carbamoyl phosphate synthase pyrimidine-specific small chain {ECO:0000305};
DE            EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01209};
DE   AltName: Full=Carbamoyl phosphate synthetase glutamine chain 2 {ECO:0000255|HAMAP-Rule:MF_01209};
DE            Short=CPS-P;
GN   Name=pyrAA {ECO:0000255|HAMAP-Rule:MF_01209};
GN   OrderedLocusNames=lp_2701;
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8014 / CCM 1904 / DSM 20205 / NCDO 82 / NCIB 6376;
RX   PubMed=8982065; DOI=10.1016/s0378-1119(96)00461-1;
RA   Elagoez A., Abdi A., Hubert J.-C., Kammerer B.;
RT   "Structure and organisation of the pyrimidine biosynthesis pathway genes in
RT   Lactobacillus plantarum: a PCR strategy for sequencing without cloning.";
RL   Gene 182:37-43(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA   Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA   Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA   Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/jb.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
RN   [4]
RP   FUNCTION.
RC   STRAIN=ATCC 8014 / CCM 1904 / DSM 20205 / NCDO 82 / NCIB 6376;
RX   PubMed=10852872; DOI=10.1128/jb.182.12.3416-3422.2000;
RA   Nicoloff H., Hubert J.-C., Bringel F.;
RT   "In Lactobacillus plantarum, carbamoyl phosphate is synthesized by two
RT   carbamoyl-phosphate synthetases (CPS): carbon dioxide differentiates the
RT   arginine-repressed from the pyrimidine-regulated CPS.";
RL   J. Bacteriol. 182:3416-3422(2000).
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 the
CC       biosynthetic pathway leading to pyrimidine nucleotides. The small
CC       subunit (glutamine amidotransferase) binds and cleaves glutamine to
CC       supply the large subunit with the substrate ammonia.
CC       {ECO:0000269|PubMed:10852872}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl
CC         phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+);
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:0000255|HAMAP-
CC         Rule:MF_01209};
CC   -!- CATALYTIC ACTIVITY: [Carbamoyl phosphate synthase pyrimidine-specific small chain]:
CC       Reaction=L-glutamine + H2O = L-glutamate + NH4(+);
CC         Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01209};
CC   -!- ACTIVITY REGULATION: Inhibited by pyrimidine.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01209}.
CC   -!- SIMILARITY: Belongs to the CarA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01209}.
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DR   EMBL; Z54240; CAA91004.1; -; Genomic_DNA.
DR   EMBL; AL935263; CCC79822.1; -; Genomic_DNA.
DR   RefSeq; WP_011101887.1; NC_004567.2.
DR   AlphaFoldDB; P77885; -.
DR   SMR; P77885; -.
DR   STRING; 220668.lp_2701; -.
DR   MEROPS; C26.963; -.
DR   EnsemblBacteria; CCC79822; CCC79822; lp_2701.
DR   GeneID; 89669937; -.
DR   KEGG; lpl:lp_2701; -.
DR   PATRIC; fig|220668.9.peg.2261; -.
DR   eggNOG; COG0505; Bacteria.
DR   HOGENOM; CLU_035901_2_1_9; -.
DR   OrthoDB; 9804328at2; -.
DR   PhylomeDB; P77885; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000000432; 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:0004359; F:glutaminase activity; IEA:RHEA.
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-UniRule.
DR   GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:L-glutamine metabolic process; IEA:InterPro.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   FunFam; 3.40.50.880:FF:000029; Carbamoyl-phosphate synthase small chain; 1.
DR   FunFam; 3.50.30.20:FF:000001; Carbamoyl-phosphate synthase small chain; 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; IPR050472; Anth_synth/Amidotransfase.
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   NCBIfam; NF009475; PRK12838.1; 1.
DR   PANTHER; PTHR43418:SF7; CARBAMOYL-PHOSPHATE SYNTHASE SMALL CHAIN; 1.
DR   PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 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   ATP-binding; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..364
FT                   /note="Carbamoyl phosphate synthase pyrimidine-specific
FT                   small chain"
FT                   /id="PRO_0000112286"
FT   DOMAIN          169..356
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   REGION          1..169
FT                   /note="CPSase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   ACT_SITE        244
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   ACT_SITE        329
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   ACT_SITE        331
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   BINDING         45
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   BINDING         217
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   BINDING         219
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   BINDING         245
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   BINDING         248
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   BINDING         286
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   BINDING         288
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   BINDING         289
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT   CONFLICT        144
FT                   /note="V -> I (in Ref. 1; CAA91004)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   364 AA;  39983 MW;  5B916580EE4C3267 CRC64;
     MKRYLVLEDG TIYPGTGFGA TTATVGELVF NTGMSGYQES ITDQSYNGEI LMFTYPLIGN
     YGINRDDHES IKPTCKGVVV HEVARRASNW RNAQSLDDYL KQNAIPGIMD IDTRAVTKHI
     RTKGAMKATI VDNVLPDTVD RLKVTELNRA VVAQSSTNNA YPNPATGPNV VVVDFGLKHS
     ILRELAKRQC NLTVLPYNTT ASEIMALNPD GVMLTNGPGD PKDVPGALEM IREVEKHVPL
     FGICLGHQLF ALANGADTFK MKFGHRGFNH PVREIATGRI DFTSQNHGYA VDRDSLAQTD
     LLITHEEIND GTVEGLRHRD YAAFSVQYHP DAAPGPHDAD HIFDEFIDLM AANQATQKGS
     QFNA
//