ID A0A100IJ92_ASPNG Unreviewed; 411 AA.
AC A0A100IJ92;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN ORFNames=ABL_04917 {ECO:0000313|EMBL:GAQ42256.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ42256.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ42256.1}.
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DR EMBL; BCMY01000007; GAQ42256.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A100IJ92; -.
DR VEuPathDB; FungiDB:An07g00520; -.
DR VEuPathDB; FungiDB:An16g02290; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1163716; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1183857; -.
DR VEuPathDB; FungiDB:ATCC64974_31700; -.
DR VEuPathDB; FungiDB:ATCC64974_43430; -.
DR VEuPathDB; FungiDB:M747DRAFT_283490; -.
DR VEuPathDB; FungiDB:M747DRAFT_335399; -.
DR Proteomes; UP000068243; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd06558; crotonase-like; 1.
DR CDD; cd03053; GST_N_Phi; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.90.226.20; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43900; GLUTATHIONE S-TRANSFERASE RHO; 1.
DR PANTHER; PTHR43900:SF3; GLUTATHIONE S-TRANSFERASE RHO; 1.
DR Pfam; PF00378; ECH_1; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:GAQ42256.1}.
FT DOMAIN 69..151
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
SQ SEQUENCE 411 AA; 45728 MW; A473F5054ABF78B6 CRC64;
MALDMAEKMV CIAAGMPSTS GMPVIVEPSR AGSRRQIYMS FSTIDYGNFN RPGHFLSNET
LAFPCKMPLT PKVYGSVSST CTQRVLIVLE ELEIDYELIP INMRAGEHKG PSYLSEHNPF
GYIPAYQDKD VKIFESRAIC HYLAAKSGGH LVPPSNPLKV AEFQQAASVE YSYFDPPMKQ
LAYESLFKSM MGHGEPDTSL VSLYKDQIRK CLDYYEGILE KQDYLGGTLP KLVNNNINVA
RAFYSHSKIL VTALNGPVIG LSATLISHSD FIYTVSNTWL MTPFTSLGLM AEGGSSVTFI
QQMDQRKANE ALLLGRKIPV SKLAQIGFVN KVFENKDNFR KQVMGYLQQT FGEHLVPSSL
LGTKALIRRR LIQEQDKQAP LEMFGGLDRF CQGIPQAKMG EALSKSKASR L
//