GLRX3_ECO57
ID GLRX3_ECO57 Reviewed; 83 AA.
AC P0AC64; P37687;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Glutaredoxin 3;
DE Short=Grx3;
GN Name=grxC; OrderedLocusNames=Z5037, ECs4488;
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: 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; AE005174; AAG58757.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37911.1; -; Genomic_DNA.
DR PIR; A86037; A86037.
DR PIR; H91189; H91189.
DR RefSeq; NP_312515.1; NC_002695.1.
DR RefSeq; WP_000024392.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AC64; -.
DR BMRB; P0AC64; -.
DR SMR; P0AC64; -.
DR STRING; 155864.EDL933_4874; -.
DR EnsemblBacteria; AAG58757; AAG58757; Z5037.
DR EnsemblBacteria; BAB37911; BAB37911; ECs_4488.
DR GeneID; 67417613; -.
DR GeneID; 915569; -.
DR KEGG; ece:Z5037; -.
DR KEGG; ecs:ECs_4488; -.
DR PATRIC; fig|386585.9.peg.4703; -.
DR eggNOG; COG0695; Bacteria.
DR HOGENOM; CLU_026126_7_3_6; -.
DR OMA; GRTTFPQ; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..83
FT /note="Glutaredoxin 3"
FT /id="PRO_0000141589"
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
