GLRX4_ECOLI
ID GLRX4_ECOLI Reviewed; 115 AA.
AC P0AC69; P37010; P77424;
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 4;
DE Short=Grx4;
DE AltName: Full=Monothiol glutaredoxin;
GN Name=grxD; Synonyms=ydhD; OrderedLocusNames=b1654, JW1646;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-115.
RC STRAIN=K12;
RX PubMed=7559321; DOI=10.1128/jb.177.19.5393-5400.1995;
RA Reuven N.B., Koonin E.V., Rudd K.E., Deutscher M.P.;
RT "The gene for the longest known Escherichia coli protein is a member of
RT helicase superfamily II.";
RL J. Bacteriol. 177:5393-5400(1995).
RN [5]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=15833738; DOI=10.1074/jbc.m500678200;
RA Fernandes A.P., Fladvad M., Berndt C., Andresen C., Lillig C.H.,
RA Neubauer P., Sunnerhagen M., Holmgren A., Vlamis-Gardikas A.;
RT "A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a
RT substrate for thioredoxin reductase.";
RL J. Biol. Chem. 280:24544-24552(2005).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=15840565; DOI=10.1074/jbc.m500679200;
RA Fladvad M., Bellanda M., Fernandes A.P., Mammi S., Vlamis-Gardikas A.,
RA Holmgren A., Sunnerhagen M.;
RT "Molecular mapping of functionalities in the solution structure of reduced
RT Grx4, a monothiol glutaredoxin from Escherichia coli.";
RL J. Biol. Chem. 280:24553-24561(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER
RP AND GLUTATHIONE, AND SUBUNIT.
RX PubMed=19505088; DOI=10.1021/bi900440m;
RA Iwema T., Picciocchi A., Traore D.A., Ferrer J.L., Chauvat F.,
RA Jacquamet L.;
RT "Structural basis for delivery of the intact [Fe2S2] cluster by monothiol
RT glutaredoxin.";
RL Biochemistry 48:6041-6043(2009).
CC -!- FUNCTION: Monothiol glutaredoxin involved in the biogenesis of iron-
CC sulfur clusters. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19505088}.
CC -!- INTERACTION:
CC P0AC69; P0ABE2: bolA; NbExp=5; IntAct=EBI-545828, EBI-545774;
CC P0AC69; P0A9W6: ibaG; NbExp=4; IntAct=EBI-545828, EBI-1131877;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15833738}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00096; AAC74726.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15420.1; -; Genomic_DNA.
DR EMBL; L01622; AAC37010.1; -; Genomic_DNA.
DR PIR; H64922; H64922.
DR RefSeq; NP_416171.1; NC_000913.3.
DR RefSeq; WP_000108172.1; NZ_STEB01000003.1.
DR PDB; 1YKA; NMR; -; A=1-115.
DR PDB; 2WCI; X-ray; 1.90 A; A/B=1-115.
DR PDBsum; 1YKA; -.
DR PDBsum; 2WCI; -.
DR AlphaFoldDB; P0AC69; -.
DR SMR; P0AC69; -.
DR BioGRID; 4260269; 437.
DR ComplexPortal; CPX-2206; GRXD iron-sulfur cluster assembly homodimer complex.
DR ComplexPortal; CPX-5898; bolA-grxD iron-sulfur cluster assembly complex.
DR ComplexPortal; CPX-5899; ibaG-grxD iron-sulfur cluster assembly complex.
DR DIP; DIP-11729N; -.
DR IntAct; P0AC69; 19.
DR STRING; 511145.b1654; -.
DR SWISS-2DPAGE; P0AC69; -.
DR jPOST; P0AC69; -.
DR PaxDb; P0AC69; -.
DR PRIDE; P0AC69; -.
DR EnsemblBacteria; AAC74726; AAC74726; b1654.
DR EnsemblBacteria; BAA15420; BAA15420; BAA15420.
DR GeneID; 67415642; -.
DR GeneID; 946169; -.
DR KEGG; ecj:JW1646; -.
DR KEGG; eco:b1654; -.
DR PATRIC; fig|1411691.4.peg.605; -.
DR EchoBASE; EB2098; -.
DR eggNOG; COG0278; Bacteria.
DR HOGENOM; CLU_026126_2_1_6; -.
DR InParanoid; P0AC69; -.
DR OMA; KGTKLMP; -.
DR PhylomeDB; P0AC69; -.
DR BioCyc; EcoCyc:EG12181-MON; -.
DR EvolutionaryTrace; P0AC69; -.
DR PRO; PR:P0AC69; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IPI:ComplexPortal.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045454; P:cell redox homeostasis; IC:ComplexPortal.
DR GO; GO:0055072; P:iron ion homeostasis; IC:ComplexPortal.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IC:ComplexPortal.
DR CDD; cd03028; GRX_PICOT_like; 1.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR033658; GRX_PICOT-like.
DR InterPro; IPR014434; Monothiol_GRX.
DR InterPro; IPR004480; Monothiol_GRX-rel.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR10293; PTHR10293; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PIRSF; PIRSF005894; Monothiol_GRX; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR00365; TIGR00365; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Redox-active center; Reference proteome.
FT CHAIN 1..115
FT /note="Glutaredoxin 4"
FT /id="PRO_0000102257"
FT DOMAIN 5..107
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 22
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:19505088"
FT BINDING 30
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 59
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:19505088"
FT BINDING 71
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:19505088"
FT BINDING 84..85
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:2WCI"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:2WCI"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:2WCI"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:2WCI"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:2WCI"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:2WCI"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:2WCI"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1YKA"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2WCI"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:2WCI"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:2WCI"
FT HELIX 95..107
FT /evidence="ECO:0007829|PDB:2WCI"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1YKA"
SQ SEQUENCE 115 AA; 12879 MW; 254B540430632645 CRC64;
MSTTIEKIQR QIAENPILLY MKGSPKLPSC GFSAQAVQAL AACGERFAYV DILQNPDIRA
ELPKYANWPT FPQLWVDGEL VGGCDIVIEM YQRGELQQLI KETAAKYKSE EPDAE
