ID   GTO2_SCHPO              Reviewed;         313 AA.
AC   O94524;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 136.
DE   RecName: Full=Glutathione S-transferase omega-like 2;
DE            EC=2.5.1.18;
DE   AltName: Full=Glutathione-dependent dehydroascorbate reductase;
DE            EC=1.8.5.1;
GN   Name=gto2; ORFNames=SPCC1281.07c;
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 [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).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Active as '1-Cys' thiol transferase against beta-hydroxyethyl
CC       disulfide (HED), as dehydroascorbate reductase and as dimethylarsinic
CC       acid reductase, while not active against the standard GST substrate 1-
CC       chloro-2,4-dinitrobenzene (CDNB). May be involved in cell wall
CC       organization and biogenesis (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + L-dehydroascorbate = glutathione disulfide +
CC         L-ascorbate; Xref=Rhea:RHEA:24424, ChEBI:CHEBI:38290,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58539; EC=1.8.5.1;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}. Golgi apparatus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC       {ECO:0000305}.
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DR   EMBL; CU329672; CAA22828.1; -; Genomic_DNA.
DR   PIR; T40926; T40926.
DR   RefSeq; NP_588171.1; NM_001023160.2.
DR   AlphaFoldDB; O94524; -.
DR   SMR; O94524; -.
DR   BioGRID; 275601; 11.
DR   STRING; 4896.SPCC1281.07c.1; -.
DR   MaxQB; O94524; -.
DR   PaxDb; O94524; -.
DR   GeneID; 2539028; -.
DR   KEGG; spo:SPCC1281.07c; -.
DR   PomBase; SPCC1281.07c; -.
DR   eggNOG; KOG2903; Eukaryota.
DR   HOGENOM; CLU_037263_0_1_1; -.
DR   InParanoid; O94524; -.
DR   PhylomeDB; O94524; -.
DR   PRO; PR:O94524; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004364; F:glutathione transferase activity; ISM:PomBase.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0098869; P:cellular oxidant detoxification; IC:PomBase.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR016639; GST_Omega/GSH.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR32419; PTHR32419; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   PIRSF; PIRSF015753; GST; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01206; Xi.1; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Cytoplasm; Golgi apparatus; Nucleus;
KW   Oxidoreductase; Reference proteome; Transferase.
FT   CHAIN           1..313
FT                   /note="Glutathione S-transferase omega-like 2"
FT                   /id="PRO_0000343153"
FT   DOMAIN          161..289
FT                   /note="GST C-terminal"
FT   ACT_SITE        49
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   313 AA;  37056 MW;  BF05B5D02FE8E196 CRC64;
     MSNTHITDWS SKDGEFRRQV SSFRERISPE HKYFQPEKDR YHLYVSYACP WAHRTLIVRK
     LKGLENVIPV HVVGWLMGPN GWNFDKENDS TGDPLYNSPY LRNLYFRADP NYNMRFTVPV
     LWDSKYNTIV NNESAEIIRM FNDAFNEVIE DEEKRVVDLY PSSLRTKIDE LNDYFYDTVN
     NGVYKTGFAT TAEAYEKNVR VVFQGLDRLE QVLKESKGPF LLGDHLTETD VRLYTTIVRF
     DPVYVQHFKC NIGTIRHNYP HINQWLKRLY WKHPAFHETT DFKHIKCHYT QSHTQINPLG
     ITPLGPIPNV EYF