ID   A0A0L6WQ98_9AGAR        Unreviewed;       437 AA.
AC   A0A0L6WQ98;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial {ECO:0000313|EMBL:KNZ77518.1};
GN   ORFNames=J132_05266 {ECO:0000313|EMBL:KNZ77518.1};
OS   Termitomyces sp. J132.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC   Termitomyces.
OX   NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ77518.1, ECO:0000313|Proteomes:UP000053712};
RN   [1] {ECO:0000313|Proteomes:UP000053712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA   Hu H., Poulsen M.;
RT   "The genome of Termitomyces.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; KQ412512; KNZ77518.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6WQ98; -.
DR   STRING; 1306850.A0A0L6WQ98; -.
DR   OrthoDB; 5486605at2759; -.
DR   Proteomes; UP000053712; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR42790; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42790:SF3; KYNURENINE_ALPHA-AMINOADIPATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KNZ77518.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053712};
KW   Transferase {ECO:0000313|EMBL:KNZ77518.1}.
FT   DOMAIN          169..428
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   437 AA;  48938 MW;  45B69FB45351F6AC CRC64;
     MNVDPTFQAP AKALPVDYYT PFLSDLAKRR KPSAIRSLFP LEHTPGLISL LAGKPNPTTF
     PFTSFSFTAE SPTKGEADVE VKIGSTELAH GLQYGATAGY EKLWEWFVGL QEFVHCRKKT
     EDWSISIGSG SQDLIYKILI SPKGCRCTRK SRRSCPCRVS SLCVEVETDA HGIKSSSLRS
     ILEEWPVGKP KPRVLYTVPY GCNPTGMTAT LERRKEVLAL SREHDFIILE DDPYYYLYYG
     TAPRYPSYFN LEMEEPQTGR VLRFDSLSKI LSAGIRIGFA SGPKPLLDAI NKHTATSNLQ
     TASLTQVIVY KLLETWGYDT FIQHTKKVSN FYREKRDVFE AAMKKHLTGL AEWVAPEAGM
     FFWFKLLLTD DPSVEGDSQA LIAEKAVKSG VLALPGTAFL PNDRKTAHVR AAFSLLSEED
     VNEALRRLSK VIKDART
//