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CITG2_SALCH
ID   CITG2_SALCH             Reviewed;         298 AA.
AC   Q57RV7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Probable 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase 2 {ECO:0000255|HAMAP-Rule:MF_00397};
DE            Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase 2 {ECO:0000255|HAMAP-Rule:MF_00397};
DE            EC=2.4.2.52 {ECO:0000255|HAMAP-Rule:MF_00397};
GN   Name=citG2 {ECO:0000255|HAMAP-Rule:MF_00397}; OrderedLocusNames=SCH_0648;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX64554.1; -; Genomic_DNA.
DR   RefSeq; WP_000982660.1; NC_006905.1.
DR   AlphaFoldDB; Q57RV7; -.
DR   EnsemblBacteria; AAX64554; AAX64554; SCH_0648.
DR   KEGG; sec:SCH_0648; -.
DR   HOGENOM; CLU_056179_1_0_6; -.
DR   OMA; QSWQRPA; -.
DR   Proteomes; UP000000538; 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; Transferase.
FT   CHAIN           1..298
FT                   /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT                   dephosphocoenzyme-A synthase 2"
FT                   /id="PRO_0000255408"
SQ   SEQUENCE   298 AA;  32626 MW;  33FA5F1BD22E5054 CRC64;
     MMPIPANPTN ASIQPQSLYD AWADLAWRAM LTEVNLSPKP GLVDRLNCGA HKDMALADFH
     RSAEAIRHWL PRFMEYGASC TRLPPESVLA GLRPLGMACE AAMFRATAGV NTHKGSIFSL
     GLLCAAIGRL YQLRQPITAE TLCATAADFC RGLTTRELRQ NNLQLTAGQR LYQQLGLTGA
     RGEAEAGYPL VIRHALPHYR ALLAQGRDPE LALLDTLLLL MSLNGDTNVA SRGGADGLRW
     LQQQAAVLLH QGGIRTPDDL VYLHRFDQQC IERNLSPGGS ADLLIVTWFL AQISQVNH
 
 
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