GLRX4_HAEDU
ID GLRX4_HAEDU Reviewed; 107 AA.
AC O30824; Q7BY79;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Glutaredoxin 4;
DE Short=Grx4;
DE AltName: Full=Monothiol glutaredoxin;
GN Name=grxD; OrderedLocusNames=HD_0324; ORFNames=hypo107;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RX PubMed=9511768; DOI=10.1016/s0378-1119(97)00642-2;
RA San Mateo L.R., Toffer K.L., Kawula T.H.;
RT "The sodA gene of Haemophilus ducreyi encodes a hydrogen peroxide-
RT inhibitable superoxide dismutase.";
RL Gene 207:251-257(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Monothiol glutaredoxin involved in the biogenesis of iron-
CC sulfur clusters. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC {ECO:0000305}.
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DR EMBL; AF017750; AAC46217.1; -; Genomic_DNA.
DR EMBL; AE017143; AAP95301.1; -; Genomic_DNA.
DR RefSeq; WP_010944354.1; NC_002940.2.
DR AlphaFoldDB; O30824; -.
DR SMR; O30824; -.
DR STRING; 233412.HD_0324; -.
DR EnsemblBacteria; AAP95301; AAP95301; HD_0324.
DR KEGG; hdu:HD_0324; -.
DR eggNOG; COG0278; Bacteria.
DR HOGENOM; CLU_026126_2_1_6; -.
DR OMA; KGTKLMP; -.
DR Proteomes; UP000001022; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW 2Fe-2S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Redox-active center;
KW Reference proteome.
FT CHAIN 1..107
FT /note="Glutaredoxin 4"
FT /id="PRO_0000293132"
FT DOMAIN 4..106
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 21
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 83..84
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
SQ SEQUENCE 107 AA; 12079 MW; 7221B6F3A80B988F CRC64;
METIDKIKQQ INENPILLYM KGSPKFPSCG FSARAVEAII QCQVPFGYVD ILTNPDIRSE
LPKFANWPTF PQLWVEGELI GGCDIILEMF QKGELHTLLK ETATKHG
