ID   GLRX4_HAEIN             Reviewed;         107 AA.
AC   P45085;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Glutaredoxin 4;
DE            Short=Grx4;
DE   AltName: Full=Monothiol glutaredoxin;
GN   Name=grxD; OrderedLocusNames=HI_1165;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC22820.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L42023; AAC22820.1; ALT_INIT; Genomic_DNA.
DR   PIR; F64168; F64168.
DR   RefSeq; NP_439323.2; NC_000907.1.
DR   RefSeq; WP_010869143.1; NC_000907.1.
DR   AlphaFoldDB; P45085; -.
DR   SMR; P45085; -.
DR   STRING; 71421.HI_1165; -.
DR   EnsemblBacteria; AAC22820; AAC22820; HI_1165.
DR   KEGG; hin:HI_1165; -.
DR   PATRIC; fig|71421.8.peg.1217; -.
DR   eggNOG; COG0278; Bacteria.
DR   HOGENOM; CLU_026126_2_1_6; -.
DR   PhylomeDB; P45085; -.
DR   BioCyc; HINF71421:G1GJ1-1199-MON; -.
DR   Proteomes; UP000000579; 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_0000102261"
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;  11941 MW;  E20EF7B8C16DF9FC CRC64;
     METLDKIKKQ ISENPILIYM KGSPKLPSCG FPARASEALM HCKVPFGYVD ILQHPDIRAE
     LPTYANWPTF PQLWVEGELI GGCDIILEMY QAGELQTLLA EVAAKHA