ID K1XII2_MARBU Unreviewed; 224 AA.
AC K1XII2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Glutathione S-transferase kappa {ECO:0000256|PIRNR:PIRNR006386};
DE EC=2.5.1.18 {ECO:0000256|PIRNR:PIRNR006386};
GN ORFNames=MBM_09585 {ECO:0000313|EMBL:EKD12264.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD12264.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD12264.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD12264.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(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; JH921460; EKD12264.1; -; Genomic_DNA.
DR RefSeq; XP_007297474.1; XM_007297412.1.
DR AlphaFoldDB; K1XII2; -.
DR GeneID; 18765520; -.
DR KEGG; mbe:MBM_09585; -.
DR eggNOG; ENOG502S5GX; Eukaryota.
DR HOGENOM; CLU_069253_1_4_1; -.
DR InParanoid; K1XII2; -.
DR OMA; ECTNSKG; -.
DR OrthoDB; 4159077at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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 Isomerase {ECO:0000313|EMBL:EKD12264.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Transferase {ECO:0000256|PIRNR:PIRNR006386}.
FT DOMAIN 7..209
FT /note="DSBA-like thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF01323"
FT ACT_SITE 15
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006386-1"
SQ SEQUENCE 224 AA; 24919 MW; 28E61B6A680C6D51 CRC64;
MAPRPKLTLY IDTVSPFAYI AYHVLRNDPV FKECEITYIP VFLGGIMKAC NNVPPISIKN
KDAWINVERK RWARLFNVPM ADEAPEGFPH LTLTIMRALC ALIILHPGDE GQDVLAKALE
ALCRAYWVDK RKTFERDVLV EVLAETFGGE EAEKVMATAG QEGKALLAKN SEQAVTEGAF
GLPYFVATNS QGETDRFWGV DHMGLLTMHL GLKKPATGGW RALL
//
