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   03-AUG-2022, entry version 84.
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; Enterobacterales;
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., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   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 the
CC       glutathione-dependent synthesis of deoxyribonucleotides by the enzyme
CC       ribonucleotide reductase. In addition, it is also involved in reducing
CC       some disulfides in a coupled system with glutathione reductase (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN82869.1; -; Genomic_DNA.
DR   RefSeq; WP_000024392.1; NC_004431.1.
DR   AlphaFoldDB; P0AC63; -.
DR   BMRB; P0AC63; -.
DR   SMR; P0AC63; -.
DR   STRING; 199310.c4433; -.
DR   EnsemblBacteria; AAN82869; AAN82869; c4433.
DR   GeneID; 67417613; -.
DR   KEGG; ecc:c4433; -.
DR   eggNOG; COG0695; Bacteria.
DR   HOGENOM; CLU_026126_7_3_6; -.
DR   OMA; GRTTFPQ; -.
DR   BioCyc; ECOL199310:C4433-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) 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   CDD; cd03418; GRX_GRXb_1_3_like; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR011900; GRX_bact.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
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   Deoxyribonucleotide synthesis; Disulfide bond; Electron transport;
KW   Redox-active center; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..83
FT                   /note="Glutaredoxin 3"
FT                   /id="PRO_0000141590"
FT   DOMAIN          2..83
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   DISULFID        12..15
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   83 AA;  9137 MW;  5B19A85BB0C9FBEF CRC64;
     MANVEIYTKE TCPYCHRAKA LLSSKGVSFQ ELPIDGNAAK REEMIKRSGR TTVPQIFIDA
     QHIGGCDDLY ALDARGGLDP LLK