(data stored in ACNUC7421 zone)

SWISSPROT: CITG_SHISS

ID   CITG_SHISS              Reviewed;         292 AA.
AC   Q3Z4I0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 71.
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};
GN   OrderedLocusNames=SSON_0565;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-dephospho-CoA + ATP = 2'-(5''-triphospho-alpha-D-
CC         ribosyl)-3'-dephospho-CoA + adenine; Xref=Rhea:RHEA:15117,
CC         ChEBI:CHEBI:16708, ChEBI:CHEBI:30616, ChEBI:CHEBI:57328,
CC         ChEBI:CHEBI:61378; EC=2.4.2.52; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00397};
CC   -!- SIMILARITY: Belongs to the CitG/MdcB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00397}.
DR   EMBL; CP000038; AAZ87332.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ87332; AAZ87332; SSON_0565.
DR   KEGG; ssn:SSON_0565; -.
DR   HOGENOM; HOG000258582; -.
DR   KO; K05966; -.
DR   OMA; QSWQRPA; -.
DR   BioCyc; SSON300269:G1GL2-664-MONOMER; -.
DR   Proteomes; UP000002529; 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;
DR   PRODOM; Q3Z4I0.
DR   SWISS-2DPAGE; Q3Z4I0.
KW   ATP-binding; Complete proteome; Nucleotide-binding; Transferase.
FT   CHAIN         1    292       Probable 2-(5''-triphosphoribosyl)-3'-
FT                                dephosphocoenzyme-A synthase.
FT                                /FTId=PRO_0000255416.
SQ   SEQUENCE   292 AA;  31626 MW;  8563812509D7CD86 CRC64;
     MSMPATSTKT TKLATSLIDE YALLGWRAML TEVNLSPKPG LVDRINCGAH KDMALEDFHR
     SALAIQGWLP RFIEFGACSA EIAPEAVLHG LRPIGMACEG DMFRATAGVN THKGSIFSLG
     LLCAAIGRLL QLNQPVTPTT VCSTAASFCR GLTDRELRTN NSQLTAGQRL YQQLGLTGAR
     GEAEAGYPLV INHALPHYLT LLDQGLDPEL ALLDTLLLLM AINGDTNVAS RGGEGGLRWL
     QREAQTLLQK GGIRTPADLD YLRQFDRECI ERNLSPGGSA DLLILTWFLA QI
//

If you have problems or comments...

PBIL Back to PBIL home page