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Database: UniProt
Entry: A5E0V2_LODEL
LinkDB: A5E0V2_LODEL
Original site: A5E0V2_LODEL 
ID   A5E0V2_LODEL            Unreviewed;       214 AA.
AC   A5E0V2;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE            EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN   ORFNames=LELG_03239 {ECO:0000313|EMBL:EDK45060.1};
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:EDK45060.1, ECO:0000313|Proteomes:UP000001996};
RN   [1] {ECO:0000313|EMBL:EDK45060.1, 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:4EXJ}
RP   X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS).
RA   Patskovsky Y., Toro R., Bhosle R., Zencheck W.D., Hillerich B.,
RA   Seidel R.D., Washington E., Scott Glenn A., Chowdhury S., Evans B.,
RA   Hammonds J., Imker H.J., Armstrong R.N., Gerlt J.A., Almo S.C.;
RT   "Crystal structure of glutathione s-transferase like protein lelg_03239
RT   (target efi-501752) from lodderomyces elongisporus.";
RL   Submitted (APR-2012) 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}.
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DR   EMBL; CH981527; EDK45060.1; -; Genomic_DNA.
DR   RefSeq; XP_001525311.1; XM_001525261.1.
DR   PDB; 4EXJ; X-ray; 1.64 A; A/B=1-214.
DR   PDBsum; 4EXJ; -.
DR   AlphaFoldDB; A5E0V2; -.
DR   SMR; A5E0V2; -.
DR   STRING; 379508.A5E0V2; -.
DR   GeneID; 5232782; -.
DR   KEGG; lel:LELG_03239; -.
DR   VEuPathDB; FungiDB:LELG_03239; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_6_0_1; -.
DR   InParanoid; A5E0V2; -.
DR   OMA; DWYLKLN; -.
DR   OrthoDB; 1404190at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
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; 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; PF13409; GST_N_2; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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:4EXJ};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001996}.
FT   DOMAIN          1..81
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          90..214
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   214 AA;  25054 MW;  B2821666AA76B071 CRC64;
     MAILYTGPTG NGRKPLVLGK LLNAPIKVHM FHWPTKDIQE DWYLKLNPAG IVPTLVDDKG
     TPITESNNIL LYIADTYDKE HKFFYSLKQD PKLYWEQNEL LFYQATQFQS QTLTIANANY
     QNGHIDENIA QYVLSSFEKV FAFMETKLSG RDWFVGDKFT IVDIAFLVGE HRRRERLHNS
     PIWIDLKENF PNVEKWFQRA IAFENVEEIL KEHA
//
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