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Database: UniProt
Entry: A0A117DYT2_ASPNG
LinkDB: A0A117DYT2_ASPNG
Original site: A0A117DYT2_ASPNG 
ID   A0A117DYT2_ASPNG        Unreviewed;       351 AA.
AC   A0A117DYT2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:GAQ39953.1};
GN   ORFNames=ABL_03410 {ECO:0000313|EMBL:GAQ39953.1};
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:GAQ39953.1, 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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the threonine aldolase family.
CC       {ECO:0000256|ARBA:ARBA00006966}.
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:GAQ39953.1}.
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DR   EMBL; BCMY01000004; GAQ39953.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117DYT2; -.
DR   PaxDb; 5061-CADANGAP00005238; -.
DR   VEuPathDB; FungiDB:An07g00680; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1120378; -.
DR   VEuPathDB; FungiDB:ATCC64974_43540; -.
DR   VEuPathDB; FungiDB:M747DRAFT_318902; -.
DR   OMA; DFDYRCK; -.
DR   Proteomes; UP000068243; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   PANTHER; PTHR48097:SF5; LOW SPECIFICITY L-THREONINE ALDOLASE; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
FT   DOMAIN          54..300
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   351 AA;  39513 MW;  23E0CB5A2FC148AC CRC64;
     MIVKLTQPYS FLDDYSEGAH PRLLQSLLLT NATQQTGYGT DEYTHEARQL IYSQIQATDD
     EVAIHFVPSG TAANLISIAS CLRPYEAVLA VETGHILDKE AGAIEATGHK VIPVPGVRGK
     MTPENLERVL DRNTFFPHMA KPRLVYISNA TEVGTIYTRS ELRRLSETCR RRDLLLHVDG
     ARLGVALSAE INDLTLRDMV DYTDIFWIGG TKMGALLGEA VVVRRSLAEG FEFNIKQRGA
     LLGKSRVMGV QFAELFRDGL YFELARHANA MARRISAQFE RMGWELAADT ETNQVFVVVP
     DAMLHRLAER IRFYEWDKRE TGTVIRIVTA WATDEMAVDK LCQWLQAIHQ A
//
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