ID   A0A2K6ADB8_MANLE        Unreviewed;       372 AA.
AC   A0A2K6ADB8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Kynurenine aminotransferase 1 {ECO:0000313|Ensembl:ENSMLEP00000038030.1};
GN   Name=KYAT1 {ECO:0000313|Ensembl:ENSMLEP00000038030.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000038030.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000038030.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-
CC         glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959,
CC         ChEBI:CHEBI:58454; EC=2.6.1.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00023912};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65561;
CC         Evidence={ECO:0000256|ARBA:ARBA00023912};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an S-substituted L-cysteine + H2O = a thiol + NH4(+) +
CC         pyruvate; Xref=Rhea:RHEA:18121, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29256, ChEBI:CHEBI:58717; EC=4.4.1.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00023937};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18122;
CC         Evidence={ECO:0000256|ARBA:ARBA00023937};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; kynurenate
CC       from L-kynurenine: step 1/2. {ECO:0000256|ARBA:ARBA00024016}.
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DR   AlphaFoldDB; A0A2K6ADB8; -.
DR   Ensembl; ENSMLET00000061639.1; ENSMLEP00000038030.1; ENSMLEG00000043087.1.
DR   GeneTree; ENSGT00940000158797; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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); 1.
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:SF14; KYNURENINE--OXOGLUTARATE TRANSAMINASE 1; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT   DOMAIN          63..359
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   372 AA;  42256 MW;  F357949BCB9EB644 CRC64;
     MAKQLQARRL DGIDHNPWVE FVKLASEHDV VNLGQGFPDF PPPDFAVEAF QHAVSGDFML
     NQYTKAFVII IEPFFDCYEP MTVMAGGRPV FVPLKPGPIQ NGELGSSSNW QLDSMELASK
     FTPRTKALVL NTPNNPLGKV FSREELELVA SLCQQHDVVC ITDEVYQWMV YDGHPHISIA
     SLPGMWERTL TIGSAGKTFS ATGWKVGWVL GPDHIMKHLR TVHQNSIFHC PTQSQAAVAE
     SFEREQLLFG QPSSYFVQFP QAMQRCRDHM VRSLQSVGLK PVVPQGSYFL ITDISDFKRK
     MPDLPGAVDE PYDRRFVKWM IKNKGLVAIP VSIFCSVPHQ KHFDHYIRFC FVKDEATLQA
     MDEKLRKWKA EL
//