GLRX3_ECOLI
ID GLRX3_ECOLI Reviewed; 83 AA.
AC P0AC62; P37687; Q2M7S4;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Glutaredoxin 3;
DE Short=Grx3;
GN Name=grxC; Synonyms=yibM; OrderedLocusNames=b3610, JW3585;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-83.
RX PubMed=8636094; DOI=10.1074/jbc.271.12.6736;
RA Aaslund F., Nordstrand K., Berndt K.D., Nikkola M., Bergman T.,
RA Ponsting H., Joernvall H., Otting G., Holmgren A.;
RT "Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR
RT assignments, and structural analysis.";
RL J. Biol. Chem. 271:6736-6745(1996).
RN [5]
RP PROTEIN SEQUENCE OF 2-21, 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).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=9973569; DOI=10.1006/jmbi.1998.2444;
RA Nordstrand K., Aaslund F., Holmgren A., Otting G., Berndt K.D.;
RT "NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed
RT disulfide complex: implications for the enzymatic mechanism.";
RL J. Mol. Biol. 286:541-552(1999).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=11031118; DOI=10.1006/jmbi.2000.4145;
RA Nordstrand K., Sandstroem A., Aaslund F., Holmgren A., Otting G.,
RA Berndt K.D.;
RT "NMR structure of oxidized glutaredoxin 3 from Escherichia coli.";
RL J. Mol. Biol. 303:423-432(2000).
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 disulfide bonds in a coupled system with glutathione reductase.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR EMBL; U00039; AAB18587.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76634.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77682.1; -; Genomic_DNA.
DR PIR; S47831; S47831.
DR RefSeq; NP_418067.1; NC_000913.3.
DR RefSeq; WP_000024392.1; NZ_STEB01000024.1.
DR PDB; 1FOV; NMR; -; A=2-83.
DR PDB; 3GRX; NMR; -; A=2-83.
DR PDBsum; 1FOV; -.
DR PDBsum; 3GRX; -.
DR AlphaFoldDB; P0AC62; -.
DR BMRB; P0AC62; -.
DR SMR; P0AC62; -.
DR BioGRID; 4263295; 22.
DR BioGRID; 852439; 1.
DR IntAct; P0AC62; 2.
DR STRING; 511145.b3610; -.
DR jPOST; P0AC62; -.
DR PaxDb; P0AC62; -.
DR PRIDE; P0AC62; -.
DR EnsemblBacteria; AAC76634; AAC76634; b3610.
DR EnsemblBacteria; BAE77682; BAE77682; BAE77682.
DR GeneID; 67417613; -.
DR GeneID; 948132; -.
DR KEGG; ecj:JW3585; -.
DR KEGG; eco:b3610; -.
DR PATRIC; fig|1411691.4.peg.3096; -.
DR EchoBASE; EB2202; -.
DR eggNOG; COG0695; Bacteria.
DR HOGENOM; CLU_026126_7_3_6; -.
DR InParanoid; P0AC62; -.
DR OMA; GRTTFPQ; -.
DR PhylomeDB; P0AC62; -.
DR BioCyc; EcoCyc:GRXC-MON; -.
DR BioCyc; MetaCyc:GRXC-MON; -.
DR SABIO-RK; P0AC62; -.
DR EvolutionaryTrace; P0AC62; -.
DR PRO; PR:P0AC62; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0043295; F:glutathione binding; IDA:EcoCyc.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IBA:GO_Central.
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:0015035; F:protein-disulfide reductase activity; IDA:EcoCyc.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Deoxyribonucleotide synthesis; Direct protein sequencing;
KW Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7937896,
FT ECO:0000269|PubMed:8636094"
FT CHAIN 2..83
FT /note="Glutaredoxin 3"
FT /id="PRO_0000141588"
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"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1FOV"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:1FOV"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1FOV"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:1FOV"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1FOV"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1FOV"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:1FOV"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:1FOV"
SQ SEQUENCE 83 AA; 9137 MW; 5B19A85BB0C9FBEF CRC64;
MANVEIYTKE TCPYCHRAKA LLSSKGVSFQ ELPIDGNAAK REEMIKRSGR TTVPQIFIDA
QHIGGCDDLY ALDARGGLDP LLK
