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Glutaredoxin 4 (Grx4) (Monothiol glutaredoxin)

 GLRX4_ECOLI             Reviewed;         115 AA.
P0AC69; P37010; P77424;
08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
08-NOV-2005, sequence version 1.
25-OCT-2017, entry version 95.
RecName: Full=Glutaredoxin 4;
Short=Grx4;
AltName: Full=Monothiol glutaredoxin;
Name=grxD; Synonyms=ydhD; OrderedLocusNames=b1654, JW1646;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097039; DOI=10.1093/dnares/3.6.363;
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-115.
STRAIN=K12;
PubMed=7559321; DOI=10.1128/jb.177.19.5393-5400.1995;
Reuven N.B., Koonin E.V., Rudd K.E., Deutscher M.P.;
"The gene for the longest known Escherichia coli protein is a member
of helicase superfamily II.";
J. Bacteriol. 177:5393-5400(1995).
[5]
CHARACTERIZATION, AND SUBCELLULAR LOCATION.
PubMed=15833738; DOI=10.1074/jbc.M500678200;
Fernandes A.P., Fladvad M., Berndt C., Andresen C., Lillig C.H.,
Neubauer P., Sunnerhagen M., Holmgren A., Vlamis-Gardikas A.;
"A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve
as a substrate for thioredoxin reductase.";
J. Biol. Chem. 280:24544-24552(2005).
[6]
STRUCTURE BY NMR.
PubMed=15840565; DOI=10.1074/jbc.M500679200;
Fladvad M., Bellanda M., Fernandes A.P., Mammi S., Vlamis-Gardikas A.,
Holmgren A., Sunnerhagen M.;
"Molecular mapping of functionalities in the solution structure of
reduced Grx4, a monothiol glutaredoxin from Escherichia coli.";
J. Biol. Chem. 280:24553-24561(2005).
[7]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
CLUSTER AND GLUTATHIONE, AND SUBUNIT.
PubMed=19505088; DOI=10.1021/bi900440m;
Iwema T., Picciocchi A., Traore D.A., Ferrer J.L., Chauvat F.,
Jacquamet L.;
"Structural basis for delivery of the intact [Fe2S2] cluster by
monothiol glutaredoxin.";
Biochemistry 48:6041-6043(2009).
-!- FUNCTION: Monothiol glutaredoxin involved in the biogenesis of
iron-sulfur clusters. {ECO:0000305}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19505088}.
-!- INTERACTION:
P0ABE2:bolA; NbExp=4; IntAct=EBI-545828, EBI-545774;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15833738}.
-!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol
subfamily. {ECO:0000305}.
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EMBL; U00096; AAC74726.1; -; Genomic_DNA.
EMBL; AP009048; BAA15420.1; -; Genomic_DNA.
EMBL; L01622; AAC37010.1; -; Genomic_DNA.
PIR; H64922; H64922.
RefSeq; NP_416171.1; NC_000913.3.
RefSeq; WP_000108172.1; NZ_LN832404.1.
PDB; 1YKA; NMR; -; A=1-115.
PDB; 2WCI; X-ray; 1.90 A; A/B=1-115.
PDBsum; 1YKA; -.
PDBsum; 2WCI; -.
ProteinModelPortal; P0AC69; -.
SMR; P0AC69; -.
BioGrid; 4260269; 433.
DIP; DIP-11729N; -.
IntAct; P0AC69; 18.
MINT; MINT-1258030; -.
STRING; 316385.ECDH10B_1788; -.
SWISS-2DPAGE; P0AC69; -.
PaxDb; P0AC69; -.
PRIDE; P0AC69; -.
EnsemblBacteria; AAC74726; AAC74726; b1654.
EnsemblBacteria; BAA15420; BAA15420; BAA15420.
GeneID; 946169; -.
KEGG; ecj:JW1646; -.
KEGG; eco:b1654; -.
PATRIC; fig|1411691.4.peg.605; -.
EchoBASE; EB2098; -.
EcoGene; EG12181; grxD.
eggNOG; ENOG4105M2J; Bacteria.
eggNOG; COG0278; LUCA.
HOGENOM; HOG000095211; -.
InParanoid; P0AC69; -.
KO; K07390; -.
PhylomeDB; P0AC69; -.
BioCyc; EcoCyc:EG12181-MONOMER; -.
EvolutionaryTrace; P0AC69; -.
PRO; PR:P0AC69; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:EcoCyc.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
CDD; cd03028; GRX_PICOT_like; 1.
InterPro; IPR002109; Glutaredoxin.
InterPro; IPR033658; GRX_PICOT-like.
InterPro; IPR014434; Monothiol_GRX.
InterPro; IPR004480; Monothiol_GRX-rel.
InterPro; IPR036249; Thioredoxin-like_sf.
PANTHER; PTHR10293; PTHR10293; 1.
Pfam; PF00462; Glutaredoxin; 1.
PIRSF; PIRSF005894; Monothiol_GRX; 1.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR00365; TIGR00365; 1.
PROSITE; PS51354; GLUTAREDOXIN_2; 1.
1: Evidence at protein level;
2Fe-2S; 3D-structure; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
Metal-binding; Redox-active center; Reference proteome.
CHAIN 1 115 Glutaredoxin 4.
/FTId=PRO_0000102257.
DOMAIN 5 107 Glutaredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
REGION 84 85 Glutathione binding.
METAL 30 30 Iron-sulfur (2Fe-2S); shared with dimeric
partner.
BINDING 22 22 Glutathione.
{ECO:0000269|PubMed:19505088}.
BINDING 59 59 Glutathione.
{ECO:0000269|PubMed:19505088}.
BINDING 71 71 Glutathione; via amide nitrogen and
carbonyl oxygen.
{ECO:0000269|PubMed:19505088}.
HELIX 3 14 {ECO:0000244|PDB:2WCI}.
STRAND 16 23 {ECO:0000244|PDB:2WCI}.
STRAND 25 30 {ECO:0000244|PDB:2WCI}.
HELIX 31 41 {ECO:0000244|PDB:2WCI}.
STRAND 48 51 {ECO:0000244|PDB:2WCI}.
HELIX 52 54 {ECO:0000244|PDB:2WCI}.
HELIX 56 66 {ECO:0000244|PDB:2WCI}.
STRAND 67 70 {ECO:0000244|PDB:1YKA}.
STRAND 73 76 {ECO:0000244|PDB:2WCI}.
STRAND 79 83 {ECO:0000244|PDB:2WCI}.
HELIX 84 92 {ECO:0000244|PDB:2WCI}.
HELIX 95 107 {ECO:0000244|PDB:2WCI}.
STRAND 108 110 {ECO:0000244|PDB:1YKA}.
SEQUENCE 115 AA; 12879 MW; 254B540430632645 CRC64;
MSTTIEKIQR QIAENPILLY MKGSPKLPSC GFSAQAVQAL AACGERFAYV DILQNPDIRA
ELPKYANWPT FPQLWVDGEL VGGCDIVIEM YQRGELQQLI KETAAKYKSE EPDAE


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