ID E4V5F3_ARTGP Unreviewed; 220 AA.
AC E4V5F3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Glutathione S-transferase kappa {ECO:0000256|PIRNR:PIRNR006386};
DE EC=2.5.1.18 {ECO:0000256|PIRNR:PIRNR006386};
GN ORFNames=MGYG_08339 {ECO:0000313|EMBL:EFR05328.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(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; DS989830; EFR05328.1; -; Genomic_DNA.
DR RefSeq; XP_003169435.1; XM_003169387.1.
DR AlphaFoldDB; E4V5F3; -.
DR STRING; 535722.E4V5F3; -.
DR GeneID; 10024665; -.
DR VEuPathDB; FungiDB:MGYG_08339; -.
DR eggNOG; ENOG502R0HS; Eukaryota.
DR HOGENOM; CLU_069253_1_4_1; -.
DR InParanoid; E4V5F3; -.
DR OMA; ECTNSKG; -.
DR OrthoDB; 4159077at2759; -.
DR Proteomes; UP000002669; 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:EFR05328.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002669};
KW Transferase {ECO:0000256|PIRNR:PIRNR006386}.
FT DOMAIN 6..202
FT /note="DSBA-like thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF01323"
FT ACT_SITE 14
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006386-1"
SQ SEQUENCE 220 AA; 23856 MW; 9C148CAE66A6776E CRC64;
MAAPKITLYV DIVSPFAYIA YHVLRNSPVF AKCTTTYVPV LLGGIIQATG NVPPIRIKNK
DKWINMERLR WSKLLGVPIT EAMPDGFPVF TLAVQRALCA VAADHPEKLT GCIDALYNAL
WVNRDSTIIK PEGYVPVLEA VIGKEAAIKV AEKATAADMK QTLVSNTERS VESGAFGLPW
MECTNSKGET ESFFGVDHLG QVTAFLGLDG TLGKGFKALL
//
