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Database: UniProt
Entry: A0A0F4YJK5_TALEM
LinkDB: A0A0F4YJK5_TALEM
Original site: A0A0F4YJK5_TALEM 
ID   A0A0F4YJK5_TALEM        Unreviewed;       488 AA.
AC   A0A0F4YJK5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Kynurenine--oxoglutarate transaminase {ECO:0000313|EMBL:KKA18066.1};
DE            EC=2.6.1.7 {ECO:0000313|EMBL:KKA18066.1};
GN   ORFNames=T310_7982 {ECO:0000313|EMBL:KKA18066.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA18066.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA18066.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA18066.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA   Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KKA18066.1}.
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DR   EMBL; LASV01000503; KKA18066.1; -; Genomic_DNA.
DR   RefSeq; XP_013324678.1; XM_013469224.1.
DR   AlphaFoldDB; A0A0F4YJK5; -.
DR   STRING; 1408163.A0A0F4YJK5; -.
DR   GeneID; 25320247; -.
DR   OrthoDB; 176869at2759; -.
DR   Proteomes; UP000053958; Unassembled WGS sequence.
DR   GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
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   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43807; FI04487P; 1.
DR   PANTHER; PTHR43807:SF20; FI04487P; 1.
DR   Pfam; PF00155; Aminotran_1_2; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:KKA18066.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKA18066.1}.
FT   DOMAIN          87..161
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   DOMAIN          182..467
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   488 AA;  54120 MW;  B5ED563B0F493231 CRC64;
     MFACSKQRFS SAFVALKKAP CLGSPATLSV SSPAFPSVVF AQCPPPLPVQ TLFGLRRGSQ
     ANDKMSVPLR LRSIVNEAAA ASPVQPIVNM GQGFFGYNPP QFAIDAAKEA LDKVECNQYS
     PTKGRPRLKK AIADAYSASF GRKLDPDTEV TITTGANEGW LEIAVPNKLD ARADQRTGML
     CAFMAFVEPG DEVIVFEPFF DQYISNIEMP GGTIRYVPLH PPKDGATRTS SAAEWTIDFD
     QLEKTINPKT RMIVLNSPRS HNPVGKVFSR EELERIGALA VKHNLIILSD EVYDRLYYVP
     FTRIATLSPE LYERTLTVGS AGKAFYATGW RVGYLIGPPH LIKYVAAAHT RICYSSVSPL
     QEASAVAFEK ADAVGFWDQS RTEMRQKVER FCKVFDELEI PYSDPEGGYF VLANMSSVKL
     PENYPFPPHV ASRPRDFKLS WFLIKEVGVA AIPPTEFYTD ENAHIAEDYL RFAVYECIPP
     VSPVDETK
//
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