ID A5E437_LODEL Unreviewed; 222 AA.
AC A5E437;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 89.
DE RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN ORFNames=LELG_04376 {ECO:0000313|EMBL:EDK46195.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK46195.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK46195.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2] {ECO:0007829|PDB:4IVF}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RG Enzyme Function Initiative (EFI);
RA Vetting M.W., Toro R., Bhosle R., Al Obaidi N.F., Morisco L.L.,
RA Wasserman S.R., Sojitra S., Washington E., Scott Glenn A., Chowdhury S.,
RA Evans B., Hammonds J., Hillerich B., Love J., Seidel R.D., Imker H.J.,
RA Armstrong R.N., Gerlt J.A., Almo S.C.;
RT "Crystal structure of glutathione transferase homolog from Lodderomyces
RT elongisporus, target EFI-501753, with two GSH per subunit.";
RL Submitted (JAN-2013) to the PDB data bank.
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}.
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DR EMBL; CH981529; EDK46195.1; -; Genomic_DNA.
DR RefSeq; XP_001524404.1; XM_001524354.1.
DR PDB; 4IVF; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-222.
DR PDBsum; 4IVF; -.
DR AlphaFoldDB; A5E437; -.
DR SMR; A5E437; -.
DR STRING; 379508.A5E437; -.
DR GeneID; 5231402; -.
DR KEGG; lel:LELG_04376; -.
DR VEuPathDB; FungiDB:LELG_04376; -.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_14_0_1; -.
DR InParanoid; A5E437; -.
DR OMA; SAGDQFK; -.
DR OrthoDB; 1404190at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
DR CDD; cd03048; GST_N_Ure2p_like; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
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; SFLDG01151; Main.2:_Nu-like; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4IVF};
KW Reference proteome {ECO:0000313|Proteomes:UP000001996}.
FT DOMAIN 3..91
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 98..222
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT BINDING 13
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4IVF"
FT BINDING 15
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4IVF"
FT BINDING 15
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4IVF"
FT BINDING 55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4IVF"
FT BINDING 55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4IVF"
FT BINDING 56
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4IVF"
FT BINDING 75
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4IVF"
FT BINDING 76
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4IVF"
FT BINDING 115
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="3"
FT /evidence="ECO:0007829|PDB:4IVF"
FT BINDING 115
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4IVF"
FT BINDING 115
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4IVF"
FT BINDING 117
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4IVF"
FT BINDING 118
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4IVF"
FT BINDING 140
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4IVF"
FT BINDING 140
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="4"
FT /evidence="ECO:0007829|PDB:4IVF"
FT BINDING 140
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4IVF"
SQ SEQUENCE 222 AA; 25363 MW; CD739EBD9A298767 CRC64;
MALKPIKLYT APTPNGYKIS IFLEVLGLDY EVQKFDLSKN ETKEDWFVKL NPNGRIPTIN
DPNFKGVDGG LVLSQTGAIL QYLADTYDKE HKFSYPAGTA EYYKTLEYLI FQVAENGPIQ
GQANHFVFAA KEKVPYGINR YITDTKRIYG VFEDILSRNK ANDSKYLVGD RYTVADFALL
GWAYRLSRLE IDINQWPLLG KWYDSLLKLP AVQKGFEVPP KN
//