NRDH_ECOLI
ID NRDH_ECOLI Reviewed; 81 AA.
AC P0AC65; Q2MAC4; Q47414;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Glutaredoxin-like protein NrdH;
GN Name=nrdH; Synonyms=ygaN; OrderedLocusNames=b2673, JW2648;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8820648; DOI=10.1046/j.1365-2958.1996.424950.x;
RA Jordan A., Aragall E., Gibert I., Barbe J.;
RT "Promoter identification and expression analysis of Salmonella typhimurium
RT and Escherichia coli nrdEF operons encoding one of two class I
RT ribonucleotide reductases present in both bacteria.";
RL Mol. Microbiol. 19:777-790(1996).
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 INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=11441020; DOI=10.1074/jbc.m105094200;
RA Stehr M., Schneider G., Aslund F., Holmgren A., Lindqvist Y.;
RT "Structural basis for the thioredoxin-like activity profile of the
RT glutaredoxin-like NrdH-redoxin from Escherichia coli.";
RL J. Biol. Chem. 276:35836-35841(2001).
CC -!- FUNCTION: Electron transport system for the ribonucleotide reductase
CC system NrdEF.
CC -!- INDUCTION: Induced 2-fold by hydroxyurea.
CC {ECO:0000269|PubMed:20005847}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR EMBL; X79787; CAA56184.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75720.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76782.1; -; Genomic_DNA.
DR PIR; S70891; S70891.
DR RefSeq; NP_417159.1; NC_000913.3.
DR RefSeq; WP_001223227.1; NZ_STEB01000042.1.
DR PDB; 1H75; X-ray; 1.70 A; A=1-81.
DR PDBsum; 1H75; -.
DR AlphaFoldDB; P0AC65; -.
DR SMR; P0AC65; -.
DR BioGRID; 4260693; 13.
DR BioGRID; 851493; 2.
DR DIP; DIP-48164N; -.
DR IntAct; P0AC65; 7.
DR STRING; 511145.b2673; -.
DR PaxDb; P0AC65; -.
DR PRIDE; P0AC65; -.
DR EnsemblBacteria; AAC75720; AAC75720; b2673.
DR EnsemblBacteria; BAE76782; BAE76782; BAE76782.
DR GeneID; 67414033; -.
DR GeneID; 947161; -.
DR KEGG; ecj:JW2648; -.
DR KEGG; eco:b2673; -.
DR PATRIC; fig|1411691.4.peg.4068; -.
DR EchoBASE; EB3071; -.
DR eggNOG; COG0695; Bacteria.
DR HOGENOM; CLU_026126_9_0_6; -.
DR InParanoid; P0AC65; -.
DR OMA; PACVQCD; -.
DR PhylomeDB; P0AC65; -.
DR BioCyc; EcoCyc:G7401-MON; -.
DR EvolutionaryTrace; P0AC65; -.
DR PRO; PR:P0AC65; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:EcoCyc.
DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; IMP:EcoCyc.
DR InterPro; IPR011909; GlrX_NrdH.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00462; Glutaredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02194; GlrX_NrdH; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Transport.
FT CHAIN 1..81
FT /note="Glutaredoxin-like protein NrdH"
FT /id="PRO_0000141638"
FT DOMAIN 1..81
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT DISULFID 11..14
FT /note="Redox-active"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1H75"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:1H75"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1H75"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:1H75"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:1H75"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1H75"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1H75"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:1H75"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1H75"
SQ SEQUENCE 81 AA; 9139 MW; 6D0878E9CD133137 CRC64;
MRITIYTRND CVQCHATKRA MENRGFDFEM INVDRVPEAA EALRAQGFRQ LPVVIAGDLS
WSGFRPDMIN RLHPAPHAAS A
