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 01-MAY-2013, entry version 50.
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; IYTRQFC; -.
DR ProtClustDB; PRK10638; -.
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 GO; GO:0022900; P:electron transport chain; 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; Thiordxn-like_fd; 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
//
