ID A0A093FP52_TYTAL Unreviewed; 406 AA.
AC A0A093FP52;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Kynurenine--oxoglutarate transaminase 1 {ECO:0000313|EMBL:KFV58430.1};
DE Flags: Fragment;
GN ORFNames=N341_02869 {ECO:0000313|EMBL:KFV58430.1};
OS Tyto alba (Barn owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV58430.1, ECO:0000313|Proteomes:UP000054190};
RN [1] {ECO:0000313|EMBL:KFV58430.1, ECO:0000313|Proteomes:UP000054190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV58430.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KK398123; KFV58430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093FP52; -.
DR Proteomes; UP000054190; Unassembled WGS sequence.
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; 1.
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:UP000054190}.
FT DOMAIN 34..405
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV58430.1"
FT NON_TER 406
FT /evidence="ECO:0000313|EMBL:KFV58430.1"
SQ SEQUENCE 406 AA; 45731 MW; 64ED50A6E9407BF8 CRC64;
QAKMSRPVQA QRLEGIDKNI WVEFVKLAAT YSTVNLGQGF PDFPPPDFLK EAFMRALSGE
NHMLHQYTRA FGHLPLVKIL AQFFGKLLGR DLDPMTNVMV TVGAYQALFC CFQAFVDEGD
EVIIIEPFFD CYEPMVKMAG GMPVFVPLRP KAPKDGKLMS SADWQLDPAE LASKFSERTK
AIVLNSPNNP LGKVFSRGEL ELIADLCVKH DVLCISDEVY EWLVYDGKEH IRIASLQGMW
DRTVIIGSAG KTFSATGWKV GWTVGPNRLL QHLRTVHQNS VYHCATVAQE AVAEGFQREL
ELYGKPESYF VQLPKALQQK RDWLVQSLDA VGMKPIIPEG TYFLVADISE FKSDVPDVPD
SDEPYDSRFA KWMVKNKGLA AIPLSAFYCG AHKNNYNHFI RFCFAK
//
