(data stored in ACNUC7421 zone)

SWISSPROT: CITG1_SALTY

ID   CITG1_SALTY             Reviewed;         302 AA.
AC   Q8ZRX9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   11-DEC-2019, entry version 78.
DE   RecName: Full=Probable 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase 1 {ECO:0000255|HAMAP-Rule:MF_00397};
DE            Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase 1 {ECO:0000255|HAMAP-Rule:MF_00397};
DE            EC=2.4.2.52 {ECO:0000255|HAMAP-Rule:MF_00397};
GN   Name=citG1 {ECO:0000255|HAMAP-Rule:MF_00397}; OrderedLocusNames=STM0063;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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}.
DR   EMBL; AE006468; AAL19027.1; -; Genomic_DNA.
DR   RefSeq; NP_459068.1; NC_003197.2.
DR   RefSeq; WP_001103238.1; NC_003197.2.
DR   PaxDb; Q8ZRX9; -.
DR   EnsemblBacteria; AAL19027; AAL19027; STM0063.
DR   GeneID; 1251581; -.
DR   KEGG; stm:STM0063; -.
DR   PATRIC; fig|99287.12.peg.65; -.
DR   eggNOG; ENOG4108K6F; Bacteria.
DR   eggNOG; COG1767; LUCA.
DR   HOGENOM; HOG000258582; -.
DR   KO; K05966; -.
DR   OMA; MLTPKPG; -.
DR   PhylomeDB; Q8ZRX9; -.
DR   BioCyc; SENT99287:STM0063-MONOMER; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   GO; GO:0051191; P:prosthetic group biosynthetic process; IBA:GO_Central.
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;
DR   PRODOM; Q8ZRX9.
DR   SWISS-2DPAGE; Q8ZRX9.
KW   ATP-binding; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..302
FT                   /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT                   dephosphocoenzyme-A synthase 1"
FT                   /id="PRO_0000255413"
SQ   SEQUENCE   302 AA;  32851 MW;  ADA93ECBD4D47F57 CRC64;
     MNVSVVTERR TPAYSSLAAG ELNGLVARAL LTEARLTPKP GLVDIRNSGA HRDMDLAAFE
     RSTTAIAPWM EKFFIMGNNT AALAAENVLV MLRPLGMACE NDMLQATNGV NTHRGAIFAF
     GLLSAAIGRL LARGEPLEQN RICDQVARLS RNIVAHELSA KKAGKLTKSE THFQCYGLSG
     ARGEAESGFR TVRTQALPVF NRVVQEHDDT HLALLQTLLH LMAWNDDTNL VSRGGLEGLY
     YVQQQAQKLL WQGGVLVEGG IEAMQSLDDE LILRNLSPGG SADLLAVTWF LSHFPAGSLY
     PE
//

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