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Database: UniProt
Entry: P0AC63
LinkDB: P0AC63
Original site: P0AC63 
ID   GLRX3_ECOL6             Reviewed;          83 AA.
AC   P0AC63; P37687;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   14-MAY-2014, entry version 54.
DE   RecName: Full=Glutaredoxin-3;
DE            Short=Grx3;
GN   Name=grxC; OrderedLocusNames=c4433;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: The disulfide bond functions as an electron carrier in
CC       the glutathione-dependent synthesis of deoxyribonucleotides by the
CC       enzyme ribonucleotide reductase. In addition, it is also involved
CC       in reducing some disulfides in a coupled system with glutathione
CC       reductase (By similarity).
CC   -!- SUBUNIT: Monomer (Probable).
CC   -!- SIMILARITY: Belongs to the glutaredoxin family.
CC   -!- SIMILARITY: Contains 1 glutaredoxin domain.
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DR   EMBL; AE014075; AAN82869.1; -; Genomic_DNA.
DR   RefSeq; NP_756295.1; NC_004431.1.
DR   ProteinModelPortal; P0AC63; -.
DR   SMR; P0AC63; 2-83.
DR   STRING; 199310.c4433; -.
DR   EnsemblBacteria; AAN82869; AAN82869; c4433.
DR   GeneID; 1038120; -.
DR   KEGG; ecc:c4433; -.
DR   PATRIC; 18286573; VBIEscCol75197_4161.
DR   HOGENOM; HOG000095203; -.
DR   KO; K03676; -.
DR   OMA; RCIACAR; -.
DR   OrthoDB; EOG6Z3KS6; -.
DR   BioCyc; ECOL199310:C4433-MONOMER; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.30.10; -; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR011900; GRX_bact.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR02181; GRX_bact; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Deoxyribonucleotide synthesis; Disulfide bond;
KW   Electron transport; Redox-active center; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2     83       Glutaredoxin-3.
FT                                /FTId=PRO_0000141590.
FT   DOMAIN        2     83       Glutaredoxin.
FT   DISULFID     12     15       Redox-active (By similarity).
SQ   SEQUENCE   83 AA;  9137 MW;  5B19A85BB0C9FBEF CRC64;
     MANVEIYTKE TCPYCHRAKA LLSSKGVSFQ ELPIDGNAAK REEMIKRSGR TTVPQIFIDA
     QHIGGCDDLY ALDARGGLDP LLK
//
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