ID   GLRX1_SHIFL             Reviewed;          85 AA.
AC   P68689; P00277;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   04-NOV-2026, entry version 122.
DE   RecName: Full=Glutaredoxin 1;
DE            Short=Grx1;
GN   Name=grxA; Synonyms=grx; OrderedLocusNames=SF0802, S0845;
OS   Shigella flexneri.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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:0000250}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR   EMBL; AE005674; AAN42435.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16308.1; -; Genomic_DNA.
DR   RefSeq; NP_706728.2; NC_004337.2.
DR   RefSeq; WP_001195240.1; NZ_AP040250.1.
DR   AlphaFoldDB; P68689; -.
DR   BMRB; P68689; -.
DR   SMR; P68689; -.
DR   STRING; 198214.SF0802; -.
DR   PaxDb; 198214-SF0802; -.
DR   GeneID; 1023787; -.
DR   GeneID; 93776573; -.
DR   KEGG; sfl:SF0802; -.
DR   KEGG; sfx:S0845; -.
DR   PATRIC; fig|198214.7.peg.930; -.
DR   HOGENOM; CLU_026126_7_3_6; -.
DR   OMA; ADFEFKF; -.
DR   Proteomes; UP000001006; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IEA:TreeGrafter.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:TreeGrafter.
DR   CDD; cd02066; GRX_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR011902; GRXA.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR02183; GRXA; 1.
DR   NCBIfam; NF008401; PRK11200.1; 1.
DR   PANTHER; PTHR45694:SF28; GLUTAREDOXIN 1; 1.
DR   PANTHER; PTHR45694; GLUTAREDOXIN 2; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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; Reference proteome; Transport.
FT   CHAIN           1..85
FT                   /note="Glutaredoxin 1"
FT                   /id="PRO_0000141584"
FT   DOMAIN          1..85
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   DISULFID        11..14
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   85 AA;  9685 MW;  33C185A47021EF42 CRC64;
     MQTVIFGRSG CPYCVRAKDL AEKLSNERDD FQYQYVDIRA EGITKEDLQQ KAGKPVETVP
     QIFVDQQHIG GYTDFAAWVK ENLDA
//