(data stored in ACNUC7421 zone)

SWISSPROT: C5BH38_EDWI9

ID   C5BH38_EDWI9            Unreviewed;       154 AA.
AC   C5BH38;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 53.
DE   RecName: Full=Anaerobic ribonucleoside-triphosphate reductase-activating protein {ECO:0000256|PIRNR:PIRNR000368};
DE            EC=1.97.1.- {ECO:0000256|PIRNR:PIRNR000368};
GN   OrderedLocusNames=NT01EI_0486 {ECO:0000313|EMBL:ACR67721.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67721.1, 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.
RN   [2] {ECO:0000313|EMBL:ACR67721.1, ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|EMBL:ACR67721.1,
RC   ECO:0000313|Proteomes:UP000001485};
RX   PubMed=22247535; DOI=10.1128/JB.06522-11;
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., Banes M.M.,
RA   Lawrence M.L.;
RT   "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated
RT   with a Natural Channel Catfish Outbreak of Enteric Septicemia of
RT   Catfish.";
RL   J. Bacteriol. 194:740-741(2012).
CC   -!- FUNCTION: Activation of anaerobic ribonucleoside-triphosphate
CC       reductase under anaerobic conditions by generation of an organic
CC       free radical, using S-adenosylmethionine and reduced flavodoxin as
CC       cosubstrates to produce 5'-deoxy-adenosine.
CC       {ECO:0000256|PIRNR:PIRNR000368}.
CC   -!- SIMILARITY: Belongs to the organic radical-activating enzymes
CC       family. {ECO:0000256|PIRNR:PIRNR000368}.
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DR   EMBL; CP001600; ACR67721.1; -; Genomic_DNA.
DR   RefSeq; WP_015869922.1; NC_012779.2.
DR   EnsemblBacteria; ACR67721; ACR67721; NT01EI_0486.
DR   GeneID; 7961513; -.
DR   KEGG; eic:NT01EI_0486; -.
DR   PATRIC; fig|634503.3.peg.440; -.
DR   eggNOG; ENOG4108RDD; Bacteria.
DR   eggNOG; COG0602; LUCA.
DR   HOGENOM; HOG000222587; -.
DR   KO; K04068; -.
DR   OMA; NQVIHYL; -.
DR   OrthoDB; 1141206at2; -.
DR   BioCyc; EICT634503:G1GVC-454-MONOMER; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012837; NrdG.
DR   InterPro; IPR034457; Organic_radical-activating.
DR   InterPro; IPR001989; Radical_activat_CS.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR30352; PTHR30352; 1.
DR   PANTHER; PTHR30352:SF2; PTHR30352:SF2; 1.
DR   PIRSF; PIRSF000368; NrdG; 1.
DR   SFLD; SFLDF00299; anaerobic_ribonucleoside-triph; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   TIGRFAMs; TIGR02491; NrdG; 1.
DR   PROSITE; PS01087; RADICAL_ACTIVATING; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BH38.
DR   SWISS-2DPAGE; C5BH38.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000368,
KW   ECO:0000313|EMBL:ACR67721.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
SQ   SEQUENCE   154 AA;  17354 MW;  EE200773B5E354D4 CRC64;
     MNYHQYYPVD VVNGPGTRCT LFVAGCVHQC PGCYNKATWR LDSGVPFTAA LEDRIIADLN
     DTRINHQGLS LSGGDPLHPH NVATILRLVQ RVRAECRGKD IWLWTGYRLE ELTAEQQAVV
     NLINVLVDGK FVQDLKDPML IWRGSSNQVV HCLR
//

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