CARA_LACPL
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 03-AUG-2022, entry version 133.
DE RecName: Full=Carbamoyl-phosphate synthase pyrimidine-specific small chain;
DE EC=6.3.5.5;
DE AltName: Full=Carbamoyl-phosphate synthetase glutamine chain;
DE Short=CPS-P;
GN Name=pyrAA; OrderedLocusNames=lp_2701;
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=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 -!- 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 -!- ACTIVITY REGULATION: Inhibited by pyrimidine.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3.
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 -!- SIMILARITY: Belongs to the CarA family. {ECO:0000305}.
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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 RefSeq; YP_004890336.1; 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; 66450359; -.
DR KEGG; lpl:lp_2701; -.
DR PATRIC; fig|220668.9.peg.2261; -.
DR eggNOG; COG0505; Bacteria.
DR HOGENOM; CLU_035901_2_1_9; -.
DR OMA; CFNTGMT; -.
DR PhylomeDB; P77885; -.
DR BioCyc; LPLA220668:G1GW0-2313-MON; -.
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: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; -; 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 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 REGION 1..165
FT /note="CPSase"
FT ACT_SITE 244
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 329
FT /evidence="ECO:0000250"
FT ACT_SITE 331
FT /evidence="ECO:0000250"
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
