CITG_LACPL
ID CITG_LACPL Reviewed; 280 AA.
AC Q88XT4; F9UMQ8;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Probable 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase {ECO:0000255|HAMAP-Rule:MF_00397};
DE Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase {ECO:0000255|HAMAP-Rule:MF_00397};
DE EC=2.4.2.52 {ECO:0000255|HAMAP-Rule:MF_00397};
GN Name=citG {ECO:0000255|HAMAP-Rule:MF_00397}; OrderedLocusNames=lp_1093;
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 [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 [2]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-dephospho-CoA + ATP = 2'-(5''-triphospho-alpha-D-ribosyl)-
CC 3'-dephospho-CoA + adenine; Xref=Rhea:RHEA:15117, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57328, ChEBI:CHEBI:61378; EC=2.4.2.52;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00397};
CC -!- SIMILARITY: Belongs to the CitG/MdcB family. {ECO:0000255|HAMAP-
CC Rule:MF_00397}.
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DR EMBL; AL935263; CCC78497.1; -; Genomic_DNA.
DR RefSeq; WP_011101256.1; NC_004567.2.
DR RefSeq; YP_004889011.1; NC_004567.2.
DR AlphaFoldDB; Q88XT4; -.
DR STRING; 220668.lp_1093; -.
DR EnsemblBacteria; CCC78497; CCC78497; lp_1093.
DR GeneID; 66448997; -.
DR KEGG; lpl:lp_1093; -.
DR PATRIC; fig|220668.9.peg.926; -.
DR eggNOG; COG1767; Bacteria.
DR HOGENOM; CLU_056179_1_0_9; -.
DR OMA; QSWQRPA; -.
DR PhylomeDB; Q88XT4; -.
DR BioCyc; LPLA220668:G1GW0-940-MON; -.
DR Proteomes; UP000000432; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR HAMAP; MF_00397; CitG; 1.
DR InterPro; IPR002736; CitG.
DR InterPro; IPR017551; TriPribosyl-deP-CoA_syn_CitG.
DR PANTHER; PTHR30201; PTHR30201; 1.
DR Pfam; PF01874; CitG; 1.
DR TIGRFAMs; TIGR03125; citrate_citG; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..280
FT /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT dephosphocoenzyme-A synthase"
FT /id="PRO_0000214675"
SQ SEQUENCE 280 AA; 30279 MW; AAB7B18D994602CC CRC64;
MDTKIIVNHA LRALLYEVTV NPKPGLVDPL SAGPHPDMNA FMFIDSALSL APYFNACAAA
GVAYTAVDLT GLFKQIRGIG VQAEQTMFAA TKGVNTHKGA VFSLGVLVTA AAYQLQHPDV
DLATIVRTML AGLTANDFND LNTKDPTTLT AGERQYLTYG IKGIRGEAEA GYPTVMQVAL
PALRRSRGTI NQRLLDTLMA IVQATVDTNL VKRAHDPHVI DWVHDQAHRY FDLGGSRSEA
GMAFLRELNQ IFVDHNYSLG GSADLLILTI FIGLQTDILA
