GLRX2_ECOLI
ID GLRX2_ECOLI Reviewed; 215 AA.
AC P0AC59; 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 122.
DE RecName: Full=Glutaredoxin 2;
DE Short=Grx2;
GN Name=grxB; OrderedLocusNames=b1064, JW1051;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=K12;
RX PubMed=9111025; DOI=10.1074/jbc.272.17.11236;
RA Vlamis-Gardikas A., Aaslund F., Spyrou G., Bergman T., Holmgren A.;
RT "Cloning, overexpression, and characterization of glutaredoxin 2, an
RT atypical glutaredoxin from Escherichia coli.";
RL J. Biol. Chem. 272:11236-11243(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-18, AND CHARACTERIZATION.
RX PubMed=7937896; DOI=10.1073/pnas.91.21.9813;
RA Aaslund F., Ehn B., Miranda-Vizuete A., Pueyo C., Holmgren A.;
RT "Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is
RT a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin
RT 1 double mutant.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9813-9817(1994).
CC -!- FUNCTION: Involved in reducing some disulfide bonds in a coupled system
CC with glutathione reductase. Does not act as hydrogen donor for
CC ribonucleotide reductase.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR EMBL; X92076; CAA63058.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74148.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35872.1; -; Genomic_DNA.
DR PIR; E64849; E64849.
DR RefSeq; NP_415582.1; NC_000913.3.
DR RefSeq; WP_000780912.1; NZ_STEB01000016.1.
DR PDB; 1G7O; NMR; -; A=1-215.
DR PDB; 4KSM; X-ray; 2.40 A; A=1-215.
DR PDB; 4KX4; X-ray; 1.60 A; A=1-215.
DR PDBsum; 1G7O; -.
DR PDBsum; 4KSM; -.
DR PDBsum; 4KX4; -.
DR AlphaFoldDB; P0AC59; -.
DR BMRB; P0AC59; -.
DR SMR; P0AC59; -.
DR BioGRID; 4260069; 19.
DR DIP; DIP-48247N; -.
DR IntAct; P0AC59; 1.
DR STRING; 511145.b1064; -.
DR jPOST; P0AC59; -.
DR PaxDb; P0AC59; -.
DR PRIDE; P0AC59; -.
DR EnsemblBacteria; AAC74148; AAC74148; b1064.
DR EnsemblBacteria; BAA35872; BAA35872; BAA35872.
DR GeneID; 58461742; -.
DR GeneID; 946926; -.
DR KEGG; ecj:JW1051; -.
DR KEGG; eco:b1064; -.
DR PATRIC; fig|1411691.4.peg.1204; -.
DR EchoBASE; EB2551; -.
DR eggNOG; COG2999; Bacteria.
DR HOGENOM; CLU_072939_0_1_6; -.
DR InParanoid; P0AC59; -.
DR OMA; GKKMAPI; -.
DR PhylomeDB; P0AC59; -.
DR BioCyc; EcoCyc:GRXB-MON; -.
DR BioCyc; MetaCyc:GRXB-MON; -.
DR SABIO-RK; P0AC59; -.
DR EvolutionaryTrace; P0AC59; -.
DR PRO; PR:P0AC59; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Electron transport; Redox-active center; Reference proteome; Transport.
FT CHAIN 1..215
FT /note="Glutaredoxin 2"
FT /id="PRO_0000141585"
FT DOMAIN 1..77
FT /note="GST N-terminal"
FT DISULFID 9..12
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CONFLICT 13
FT /note="L -> I (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:4KX4"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:4KX4"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:4KX4"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:4KX4"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:4KX4"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:4KX4"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1G7O"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:4KX4"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:4KX4"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:4KX4"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:4KX4"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:4KX4"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:4KX4"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:4KX4"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:4KX4"
FT HELIX 140..155
FT /evidence="ECO:0007829|PDB:4KX4"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1G7O"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:4KX4"
FT HELIX 192..205
FT /evidence="ECO:0007829|PDB:4KX4"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:4KX4"
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
