ID M3CBW2_SPHMS Unreviewed; 242 AA.
AC M3CBW2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 03-MAY-2023, entry version 34.
DE RecName: Full=Glutathione S-transferase kappa {ECO:0000256|PIRNR:PIRNR006386};
DE EC=2.5.1.18 {ECO:0000256|PIRNR:PIRNR006386};
GN ORFNames=SEPMUDRAFT_70826 {ECO:0000313|EMBL:EMF09902.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF09902.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF09902.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF09902.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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 Evidence={ECO:0000256|PIRNR:PIRNR006386};
CC -!- SIMILARITY: Belongs to the GST superfamily. Kappa family.
CC {ECO:0000256|PIRNR:PIRNR006386}.
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DR EMBL; KB456268; EMF09902.1; -; Genomic_DNA.
DR RefSeq; XP_016758023.1; XM_016909915.1.
DR AlphaFoldDB; M3CBW2; -.
DR STRING; 692275.M3CBW2; -.
DR GeneID; 27907052; -.
DR eggNOG; ENOG502S5GX; Eukaryota.
DR HOGENOM; CLU_069253_1_4_1; -.
DR OMA; ECTNSKG; -.
DR OrthoDB; 4159077at2759; -.
DR Proteomes; UP000016931; Unassembled WGS sequence.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR InterPro; IPR014440; HCCAis_GSTk.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR42943; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR PANTHER; PTHR42943:SF2; GLUTATHIONE S-TRANSFERASE KAPPA 1; 1.
DR Pfam; PF01323; DSBA; 1.
DR PIRSF; PIRSF006386; HCCAis_GSTk; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW Transferase {ECO:0000256|PIRNR:PIRNR006386}.
FT DOMAIN 9..223
FT /note="DSBA-like thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF01323"
FT ACT_SITE 17
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006386-1"
SQ SEQUENCE 242 AA; 27462 MW; 378EE4BE747C80A4 CRC64;
MADSKGKKLT LYVDVISPFG YMAYWLTRHS PAFTSIPTTY IPILLGGLMS QTKNSPPLTI
TNKREWIETE RLRTSKSLQI PMMQTFPEKF PVPTTNVQRL LCYLYLKQQE QEQSNGKEKQ
KKKENFIKSL DAFFQACWVQ GKTSEINTEV VIEEILHSIF ENDGAKVREI LQGMNSEAAK
TKLRENTNEA FRSGAFGLPW FVAENATTGE REGFWGVDSV GKVLECLGVE VQGEGGRYKT
ML
//