ID A0A2I1FSS6_9GLOM Unreviewed; 239 AA.
AC A0A2I1FSS6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN ORFNames=RhiirA4_390386 {ECO:0000313|EMBL:PKY37406.1};
OS Rhizophagus irregularis.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY37406.1, ECO:0000313|Proteomes:UP000234323};
RN [1] {ECO:0000313|EMBL:PKY37406.1, ECO:0000313|Proteomes:UP000234323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4 {ECO:0000313|EMBL:PKY37406.1,
RC ECO:0000313|Proteomes:UP000234323};
RA Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA Kruger M., Pelin A., Brachmann A., Corradi N.;
RT "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT ancient asexual fungus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000710};
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|ARBA:ARBA00007409, ECO:0000256|RuleBase:RU003494}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKY37406.1}.
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DR EMBL; LLXI01000002; PKY37406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1FSS6; -.
DR VEuPathDB; FungiDB:FUN_012823; -.
DR VEuPathDB; FungiDB:GLOIN_2v1508456; -.
DR VEuPathDB; FungiDB:RhiirA1_412327; -.
DR OrthoDB; 2226298at2759; -.
DR Proteomes; UP000234323; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd03048; GST_N_Ure2p_like; 1.
DR Gene3D; 1.20.1050.130; -; 1.
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; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR44051:SF8; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG01150; Main.1:_Beta-like; 1.
DR SFLD; SFLDG01151; Main.2:_Nu-like; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000234323};
KW Transferase {ECO:0000313|EMBL:PKY37406.1}.
FT DOMAIN 3..87
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 94..215
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 239 AA; 27412 MW; 9E5BAA518DEA450A CRC64;
MTTPDITLYT YGTQNGVKIS IILEELGIPY KAKQIELVKN EQYEPWFLKI NPNSKIPAIV
DHNKDDFPVF ESTAIAIYLC ENYDPEEKLL PKNDLKLRSQ VIQWVMFEAS GIAPAQGQSN
IYCRYLPEKI PFVINNCAKE IRRLYGVLNK SLEGKEYLVG NKFTLADAMS YPVIRGHAFS
GVESIDEFPN LKAWIERIDT RPATQKGLNV PVPDIMKNPE KLEEYGNLIQ SYFKDRLNM
//
