ID   GLRX1_SCHPO             Reviewed;         101 AA.
AC   O36032; Q9US58;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Glutaredoxin-1;
GN   Name=grx1; ORFNames=SPAC4F10.20;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kawamukai M.;
RT   "S.pombe glutaredoxin.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kim H.-G., Cho Y.-W., Park E.-H., Lim C.-J.;
RT   "Characterization of cDNA encoding thioltransferase (glutaredoxin) from
RT   Schizosaccharomyces pombe.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Cho Y.-W., Kim H.-G., Lim C.-J.;
RT   "Isolation and expression of the genomic DNA encoding thioltransferase
RT   (Glutaredoxin) from Schizosaccharomyces pombe.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: The disulfide bond functions as an electron carrier in the
CC       glutathione-dependent synthesis of deoxyribonucleotides by the enzyme
CC       ribonucleotide reductase. In addition, it is also involved in reducing
CC       some disulfides in a coupled system with glutathione reductase.
CC       Thioltransferase catalyzes cellular thiol-disulfide transhydrogenation
CC       reactions. It transfers reducing equivalents to cytosolic protein and
CC       nonprotein disulfides (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR   EMBL; AB015167; BAA28750.1; -; mRNA.
DR   EMBL; AF121275; AAD25391.1; -; mRNA.
DR   EMBL; AF192764; AAF19628.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB11722.1; -; Genomic_DNA.
DR   PIR; T38824; T38824.
DR   RefSeq; NP_594763.1; NM_001020190.2.
DR   AlphaFoldDB; O36032; -.
DR   SMR; O36032; -.
DR   BioGRID; 279973; 3.
DR   STRING; 4896.SPAC4F10.20.1; -.
DR   iPTMnet; O36032; -.
DR   MaxQB; O36032; -.
DR   PaxDb; O36032; -.
DR   PRIDE; O36032; -.
DR   EnsemblFungi; SPAC4F10.20.1; SPAC4F10.20.1:pep; SPAC4F10.20.
DR   GeneID; 2543556; -.
DR   KEGG; spo:SPAC4F10.20; -.
DR   PomBase; SPAC4F10.20; grx1.
DR   VEuPathDB; FungiDB:SPAC4F10.20; -.
DR   eggNOG; KOG1752; Eukaryota.
DR   HOGENOM; CLU_026126_7_2_1; -.
DR   InParanoid; O36032; -.
DR   OMA; LLWWKGV; -.
DR   PhylomeDB; O36032; -.
DR   PRO; PR:O36032; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IDA:PomBase.
DR   GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0004602; F:glutathione peroxidase activity; ISO:PomBase.
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   GO; GO:0019430; P:removal of superoxide radicals; IC:PomBase.
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   Disulfide bond; Electron transport; Redox-active center;
KW   Reference proteome; Transport.
FT   CHAIN           1..101
FT                   /note="Glutaredoxin-1"
FT                   /id="PRO_0000141610"
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"
FT   CONFLICT        52
FT                   /note="N -> D (in Ref. 3; AAF19628)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   101 AA;  11261 MW;  30557E19BF33E9BB CRC64;
     MSSVESFVDS AVADNDVVVF AKSYCPYCHA TEKVIADKKI KAQVYQIDLM NNGDEIQSYL
     LKKTGQRTVP NIFIHQKHVG GNSDFQALFK KGELDSLFNT A