ID   GLRX1_RHIID             Reviewed;         101 AA.
AC   B7ZFT1; U9T9D2;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 3.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Glutaredoxin-1 {ECO:0000312|EMBL:CAP69667.1};
DE   AltName: Full=Glutathione-dependent oxidoreductase 1 {ECO:0000250|UniProtKB:P25373};
GN   Name=GRX1 {ECO:0000303|PubMed:18955149}; ORFNames=GLOINDRAFT_350295;
OS   Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS   (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=747089;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAP69667.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP   AND INDUCTION.
RC   STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194;
RX   PubMed=18955149; DOI=10.1016/j.fgb.2008.09.013;
RA   Benabdellah K., Merlos M.A., Azcon-Aguilar C., Ferrol N.;
RT   "GintGRX1, the first characterized glomeromycotan glutaredoxin, is a
RT   multifunctional enzyme that responds to oxidative stress.";
RL   Fungal Genet. Biol. 46:94-103(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194;
RX   PubMed=24277808; DOI=10.1073/pnas.1313452110;
RA   Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA   Charron P., Duensing N., Frei dit Frey N., Gianinazzi-Pearson V.,
RA   Gilbert L.B., Handa Y., Herr J.R., Hijri M., Koul R., Kawaguchi M.,
RA   Krajinski F., Lammers P.J., Masclaux F.G., Murat C., Morin E.,
RA   Ndikumana S., Pagni M., Petitpierre D., Requena N., Rosikiewicz P.,
RA   Riley R., Saito K., San Clemente H., Shapiro H., van Tuinen D., Becard G.,
RA   Bonfante P., Paszkowski U., Shachar-Hill Y.Y., Tuskan G.A., Young J.P.W.,
RA   Sanders I.R., Henrissat B., Rensing S.A., Grigoriev I.V., Corradi N.,
RA   Roux C., Martin F.;
RT   "Genome of an arbuscular mycorrhizal fungus provides insight into the
RT   oldest plant symbiosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:20117-20122(2013).
CC   -!- FUNCTION: Multifunctional enzyme with glutathione-dependent
CC       oxidoreductase, glutathione peroxidase and glutathione S-transferase
CC       (GST) activity. The disulfide bond functions as an electron carrier in
CC       the glutathione-dependent synthesis of deoxyribonucleotides by the
CC       enzyme ribonucleotide reductase. In addition, it is also involved in
CC       reducing cytosolic protein- and non-protein-disulfides in a coupled
CC       system with glutathione reductase. May play a role in protection
CC       against oxidative stress caused by superoxide in vivo by regulating the
CC       redox state of the protein sulfhydryl groups.
CC       {ECO:0000250|UniProtKB:P68688, ECO:0000269|PubMed:18955149,
CC       ECO:0000303|PubMed:18955149}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18955149}.
CC   -!- INDUCTION: Up-regulation of expression first detected at 24 hours after
CC       exposure to copper and reaches to a maximum after 7 days. Up-regulation
CC       of expression reaches to a maximum at 12 hours after exposure to
CC       paraquat and returns to basal levels within 24 hours.
CC       {ECO:0000269|PubMed:18955149}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAP69667.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AM932873; CAP69667.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; KI294008; ESA04784.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7ZFT1; -.
DR   SMR; B7ZFT1; -.
DR   STRING; 588596.B7ZFT1; -.
DR   PRIDE; B7ZFT1; -.
DR   VEuPathDB; FungiDB:GLOIN_2v1633026; -.
DR   eggNOG; KOG1752; Eukaryota.
DR   HOGENOM; CLU_026126_7_2_1; -.
DR   GO; GO:0005829; C:cytosol; 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   2: Evidence at transcript level;
KW   Cytoplasm; Disulfide bond; Electron transport; Redox-active center;
KW   Transport.
FT   CHAIN           1..101
FT                   /note="Glutaredoxin-1"
FT                   /id="PRO_0000410489"
FT   DOMAIN          5..101
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   DISULFID        25..28
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P68688"
FT   CONFLICT        94
FT                   /note="L -> P (in Ref. 1; CAP69667)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   101 AA;  11180 MW;  5D9B5A10662A5430 CRC64;
     MSQIKDRVEK LIQTNPVMMF SKSFCPYCKK AKATLKELNV EPGICELDED SEGRAIQDYL
     KEKTSQNTVP NIFIKGQHVG GCDDLLAAKD NGSLSKMIAA L