ID   GLRX2_ECO57             Reviewed;         215 AA.
AC   P0AC61; P39811; P75928; P77043;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Glutaredoxin 2;
DE            Short=Grx2;
GN   Name=grxB; OrderedLocusNames=Z1701, ECs1442;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Involved in reducing some disulfides in a coupled system with
CC       glutathione reductase. Does not act as hydrogen donor for
CC       ribonucleotide reductase (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG55810.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34865.1; -; Genomic_DNA.
DR   PIR; B99809; B99809.
DR   PIR; F85668; F85668.
DR   RefSeq; NP_309469.1; NC_002695.1.
DR   RefSeq; WP_000780912.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AC61; -.
DR   BMRB; P0AC61; -.
DR   SMR; P0AC61; -.
DR   STRING; 155864.EDL933_1640; -.
DR   EnsemblBacteria; AAG55810; AAG55810; Z1701.
DR   EnsemblBacteria; BAB34865; BAB34865; ECs_1442.
DR   GeneID; 58461742; -.
DR   GeneID; 912384; -.
DR   KEGG; ece:Z1701; -.
DR   KEGG; ecs:ECs_1442; -.
DR   PATRIC; fig|386585.9.peg.1543; -.
DR   eggNOG; COG2999; Bacteria.
DR   HOGENOM; CLU_072939_0_1_6; -.
DR   OMA; GKKMAPI; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
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:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   CDD; cd03199; GST_C_GRX2; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR007494; Glutaredoxin2_C.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR011901; Grx2.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF04399; Glutaredoxin2_C; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDG01204; Grx2-like.1; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR02182; GRXB; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Electron transport; Redox-active center;
KW   Reference proteome; Transport.
FT   CHAIN           1..215
FT                   /note="Glutaredoxin 2"
FT                   /id="PRO_0000141586"
FT   DOMAIN          1..77
FT                   /note="GST N-terminal"
FT   DISULFID        9..12
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   215 AA;  24350 MW;  A8AAAB2548D824FE CRC64;
     MKLYIYDHCP YCLKARMIFG LKNIPVELHV LLNDDAETPT RMVGQKQVPI LQKDDSRYMP
     ESMDIVHYVD KLDGKPLLTG KRSPAIEEWL RKVNGYANKL LLPRFAKSAF DEFSTPAARK
     YFVDKKEASA GNFADLLAHS DGLIKNISDD LRALDKLIVK PNAVNGELSE DDIQLFPLLR
     NLTLVAGINW PSRVADYRDN MAKQTQINLL SSMAI