ID   GLRX_SOLLC              Reviewed;         108 AA.
AC   Q9ZR41;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Glutaredoxin;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. West Virginia 106; TISSUE=Fruit;
RA   Chevalier C., Joubes J., Petit J., Raymond P.;
RT   "Isolation and characterization of a cDNA clone for glutaredoxin from
RT   tomato (Lycopersicon esculentum Mill.) developing fruits.";
RL   (er) Plant Gene Register PGR99-001(1999).
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}.
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; Y18346; CAA77130.1; -; mRNA.
DR   AlphaFoldDB; Q9ZR41; -.
DR   SMR; Q9ZR41; -.
DR   STRING; 4081.Solyc06g005260.2.1; -.
DR   PaxDb; Q9ZR41; -.
DR   PRIDE; Q9ZR41; -.
DR   ProMEX; Q9ZR41; -.
DR   eggNOG; KOG1752; Eukaryota.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q9ZR41; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
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   Reference proteome; Transport.
FT   CHAIN           1..108
FT                   /note="Glutaredoxin"
FT                   /id="PRO_0000141606"
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   108 AA;  11377 MW;  C2CF7A476EE4283B CRC64;
     MSLAKAKEIV SGNPVAVFSK TYCPFCVSVK DLLSKLGATF KAVELDSEKD GSEIQAALAE
     WTGQRTVPNV FIGRKHIGGC DATTALHREG KLLPLLTEAG AIAKTSTA