GLRX_VERFO
ID GLRX_VERFO Reviewed; 104 AA.
AC O81187;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Glutaredoxin;
OS Vernicia fordii (Tung) (Aleurites fordii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Aleuritideae;
OC Vernicia.
OX NCBI_TaxID=73154;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. L-2; TISSUE=Seed;
RA Tang F., Dyer J.M., Lax A.R., Shih D.S., Chapital D.C., Pepperman A.B.;
RT "Nucleotide sequence of a cDNA clone for glutaredoxin from Aleurites fordii
RT seeds.";
RL (er) Plant Gene Register PGR98-090(1998).
CC -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC presence of NADPH and glutathione reductase. Reduces low molecular
CC weight disulfides and proteins (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. CPYC subfamily.
CC {ECO:0000305}.
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DR EMBL; AF047694; AAC39481.1; -; mRNA.
DR AlphaFoldDB; O81187; -.
DR SMR; O81187; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02180; GRX_euk; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Disulfide bond; Electron transport; Redox-active center;
KW Transport.
FT CHAIN 1..104
FT /note="Glutaredoxin"
FT /id="PRO_0000141609"
FT DOMAIN 3..103
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT DISULFID 23..26
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 104 AA; 11128 MW; 9F5FC7E99D4362BD CRC64;
MAMIKAQELV SSNSVVVFSK TFCPYCTSVK QLLNQLGAQF KVIELDSESD GSDLQNALAE
WTGQRTVPNV FIGGKHIGGC DKTTGMHQEG KLIPLLTEAG AVKA