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Database: UniProt
Entry: A0A319AB00_ASPLB
LinkDB: A0A319AB00_ASPLB
Original site: A0A319AB00_ASPLB 
ID   A0A319AB00_ASPLB        Unreviewed;       228 AA.
AC   A0A319AB00;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   08-NOV-2023, entry version 16.
DE   SubName: Full=Maleylacetoacetate isomerase {ECO:0000313|EMBL:PYH56661.1};
GN   ORFNames=BO96DRAFT_412213 {ECO:0000313|EMBL:PYH56661.1};
OS   Aspergillus lacticoffeatus (strain CBS 101883).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH56661.1, ECO:0000313|Proteomes:UP000247441};
RN   [1] {ECO:0000313|EMBL:PYH56661.1, ECO:0000313|Proteomes:UP000247441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH56661.1,
RC   ECO:0000313|Proteomes:UP000247441};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Zeta family.
CC       {ECO:0000256|ARBA:ARBA00010007}.
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DR   EMBL; KZ821349; PYH56661.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319AB00; -.
DR   SMR; A0A319AB00; -.
DR   OrthoDB; 986565at2759; -.
DR   Proteomes; UP000247441; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009072; P:aromatic amino acid metabolic process; IEA:InterPro.
DR   CDD; cd03191; GST_C_Zeta; 1.
DR   CDD; cd03042; GST_N_Zeta; 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; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR005955; GST_Zeta.
DR   InterPro; IPR034330; GST_Zeta_C.
DR   InterPro; IPR034333; GST_Zeta_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR01262; maiA; 1.
DR   PANTHER; PTHR42673; MALEYLACETOACETATE ISOMERASE; 1.
DR   PANTHER; PTHR42673:SF4; MALEYLACETOACETATE ISOMERASE; 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   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:PYH56661.1}.
FT   DOMAIN          4..90
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          98..220
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   228 AA;  25287 MW;  8620DBF806F596EF CRC64;
     MSEQTITLHT YFRSSCSARL RIALNLKSLP YTSIPINLLK NEHHQSQNTS LNPSASVPTL
     IIENPDGKSI IIPQSLAALE YLEETHPQAH PLLPPLSDPT ARATVRTLSS IIACDVQPVT
     NMRILKRVAP LGVDRETWSK DLVEDGFRAY EAIAEKTAGK YSVGDEITLA DVCLLPAVWG
     AERVGVDLGN FPVIKGVRER LEEVEAVKRA HWRCQGDTPE EFRVGDRQ
//
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