CARX_LACPL
ID CARX_LACPL Reviewed; 355 AA.
AC O08317; F9UL02;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Carbamoyl-phosphate synthase arginine-specific small chain;
DE EC=6.3.5.5;
DE AltName: Full=Carbamoyl-phosphate synthetase glutamine chain;
DE Short=CPS-A;
GN Name=carA; OrderedLocusNames=lp_0527;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; 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=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).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-217.
RC STRAIN=ATCC 8014 / CCM 1904 / DSM 20205 / NCDO 82 / NCIB 6376;
RX PubMed=9098069; DOI=10.1128/jb.179.8.2697-2706.1997;
RA Bringel F., Frey L., Boivin S., Hubert J.-C.;
RT "Arginine biosynthesis and regulation in Lactobacillus plantarum: the carA
RT gene and the argCJBDF cluster are divergently transcribed.";
RL J. Bacteriol. 179:2697-2706(1997).
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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1.
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 -!- INDUCTION: Repressed by arginine.
CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000305}.
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DR EMBL; X99978; CAA68238.2; -; Genomic_DNA.
DR EMBL; AL935263; CCC78017.1; -; Genomic_DNA.
DR RefSeq; WP_011101043.1; NC_004567.2.
DR RefSeq; YP_004888531.1; NC_004567.2.
DR AlphaFoldDB; O08317; -.
DR SMR; O08317; -.
DR STRING; 220668.lp_0527; -.
DR MEROPS; C26.963; -.
DR EnsemblBacteria; CCC78017; CCC78017; lp_0527.
DR KEGG; lpl:lp_0527; -.
DR PATRIC; fig|220668.9.peg.435; -.
DR eggNOG; COG0505; Bacteria.
DR HOGENOM; CLU_035901_2_1_9; -.
DR OMA; SQNHSYV; -.
DR PhylomeDB; O08317; -.
DR BioCyc; LPLA220668:G1GW0-438-MON; -.
DR UniPathway; UPA00068; UER00171.
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:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; -; 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 Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF52021; SSF52021; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Glutamine amidotransferase; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..355
FT /note="Carbamoyl-phosphate synthase arginine-specific small
FT chain"
FT /id="PRO_0000112287"
FT DOMAIN 166..353
FT /note="Glutamine amidotransferase type-1"
FT REGION 1..162
FT /note="CPSase"
FT ACT_SITE 241
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 326
FT /evidence="ECO:0000250"
FT ACT_SITE 328
FT /evidence="ECO:0000250"
FT CONFLICT 25
FT /note="A -> V (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="A -> T (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 38187 MW; 5DABA5C1657DD89B CRC64;
MNKYLTLADG TQWIGTAIGD CQLEAAGRIV FNTGMTGYQE TLTDPSYLNQ MIAFTYPLIG
NYGIDPTVAQ APTIGAQAII VHELATFNDH YTSRQSLASF LTIHHVAGIE GVDTRDLTIH
IRQTGAQMAI LSNHPITDFE AQLATFAPQV LTATPLPVAT TTIRPRVAIL NFGEKAAITA
ELQARGADVV VLPPTASLKA VAAYHPDGIL LSNGPGDPTD YHTYLATIRQ LAQRYPLAGI
CLGHQLIALA YGAQTYQLSF GHHGLNHPVQ ACADGRIIMT SQNHDYAVDP ASIKGTPLIV
THTELNDGSI EGLRLPHQAV MSVQFHPEAH PGPQEAGQFF DDFLLTIQKE AVVNA
