(data stored in SCRATCH zone)

SWISSPROT: C5B709_EDWI9

ID   C5B709_EDWI9            Unreviewed;       303 AA.
AC   C5B709;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 56.
DE   RecName: Full=Probable 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase {ECO:0000256|HAMAP-Rule:MF_00397};
DE            Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase {ECO:0000256|HAMAP-Rule:MF_00397};
DE            EC=2.4.2.52 {ECO:0000256|HAMAP-Rule:MF_00397};
GN   Name=citG {ECO:0000256|HAMAP-Rule:MF_00397};
GN   OrderedLocusNames=NT01EI_0228 {ECO:0000313|EMBL:ACR67471.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67471.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + 3'-dephospho-CoA = 2'-(5-triphospho-
CC       alpha-D-ribosyl)-3'-dephospho-CoA + adenine. {ECO:0000256|HAMAP-
CC       Rule:MF_00397, ECO:0000256|SAAS:SAAS00390774}.
CC   -!- SIMILARITY: Belongs to the CitG/MdcB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00397}.
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DR   EMBL; CP001600; ACR67471.1; -; Genomic_DNA.
DR   RefSeq; WP_015869680.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0228; -.
DR   EnsemblBacteria; ACR67471; ACR67471; NT01EI_0228.
DR   GeneID; 7960009; -.
DR   KEGG; eic:NT01EI_0228; -.
DR   PATRIC; fig|634503.3.peg.204; -.
DR   eggNOG; ENOG4108K6F; Bacteria.
DR   eggNOG; COG1767; LUCA.
DR   HOGENOM; HOG000258582; -.
DR   KO; K05966; -.
DR   OMA; TCVLSRA; -.
DR   OrthoDB; POG091H0I1L; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IEA:UniProtKB-HAMAP.
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   Pfam; PF01874; CitG; 1.
DR   TIGRFAMs; TIGR03125; citrate_citG; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B709.
DR   SWISS-2DPAGE; C5B709.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00397,
KW   ECO:0000256|SAAS:SAAS00100819};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Glycosyltransferase {ECO:0000313|EMBL:ACR67471.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00397,
KW   ECO:0000256|SAAS:SAAS00100822};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00397,
KW   ECO:0000256|SAAS:SAAS00100823, ECO:0000313|EMBL:ACR67471.1}.
SQ   SEQUENCE   303 AA;  32292 MW;  271EDC752F213907 CRC64;
     MPNPITRNPY PGTLEQVCGH YAILGWRAML AEVNLTPKPG LVDRHNSGAH RDMAHSDFVR
     SADAIAPWLA RFVEYGADSA ALDGSSVLPG LRALGIACEA DMFRATAGVN THKGSIFSLG
     LLCAAAGRSH QRGQPVTPAR LCGYAAQFCR GLVARELAPL RPAQASTAGQ RLFMTLGITG
     ARGEAEAGYP LVLNLALPHY QQALAAGRDP ELALLDTLVQ LMAHNQDTNV AARGGESGLR
     WMQLSAAALL ATGGIRTPAD LQALRRFDAE CINRHLSPGG SADLLILTWF LAHLCYPILH
     AEH
//

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