KAT3_DANRE
ID KAT3_DANRE Reviewed; 450 AA.
AC Q7T3E5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Kynurenine--oxoglutarate transaminase 3 {ECO:0000250|UniProtKB:Q71RI9};
DE EC=2.6.1.7 {ECO:0000250|UniProtKB:Q71RI9};
DE AltName: Full=Cysteine-S-conjugate beta-lyase 2 {ECO:0000250|UniProtKB:Q71RI9};
DE EC=4.4.1.13 {ECO:0000250|UniProtKB:Q71RI9};
DE AltName: Full=Kynurenine aminotransferase 3 {ECO:0000250|UniProtKB:Q6YP21};
DE AltName: Full=Kynurenine aminotransferase III;
DE Short=KATIII;
DE AltName: Full=Kynurenine--glyoxylate transaminase {ECO:0000250|UniProtKB:Q71RI9};
DE EC=2.6.1.63 {ECO:0000250|UniProtKB:Q71RI9};
DE AltName: Full=Kynurenine--oxoglutarate transaminase III;
GN Name=kyat3 {ECO:0000250|UniProtKB:Q6YP21}; Synonyms=ccbl2, kat3;
GN ORFNames=zgc:63929;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan
CC metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in
CC the tryptophan catabolic pathway which is also a broad spectrum
CC antagonist of the three ionotropic excitatory amino acid receptors
CC among others. May catalyze the beta-elimination of S-conjugates and Se-
CC conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S
CC or C-Se bond. {ECO:0000250|UniProtKB:Q71RI9}.
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:0000250|UniProtKB:Q71RI9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65561;
CC Evidence={ECO:0000250|UniProtKB:Q71RI9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-kynurenine = glycine + H2O + kynurenate;
CC Xref=Rhea:RHEA:65896, ChEBI:CHEBI:15377, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.63;
CC Evidence={ECO:0000250|UniProtKB:Q71RI9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65897;
CC Evidence={ECO:0000250|UniProtKB:Q71RI9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-L-kynurenine + glyoxylate = glycine + H2O +
CC xanthurenate; Xref=Rhea:RHEA:65900, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:58125,
CC ChEBI:CHEBI:71201; EC=2.6.1.63;
CC Evidence={ECO:0000250|UniProtKB:Q71RI9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65901;
CC Evidence={ECO:0000250|UniProtKB:Q71RI9};
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:0000250|UniProtKB:Q71RI9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18122;
CC Evidence={ECO:0000250|UniProtKB:Q71RI9};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q71RI9};
CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; kynurenate
CC from L-kynurenine: step 1/2. {ECO:0000250|UniProtKB:Q71RI9}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q71RI9}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH53152.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC053152; AAH53152.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q7T3E5; -.
DR SMR; Q7T3E5; -.
DR STRING; 7955.ENSDARP00000063535; -.
DR PaxDb; Q7T3E5; -.
DR ZFIN; ZDB-GENE-040426-1299; kyat3.2.
DR eggNOG; KOG0257; Eukaryota.
DR InParanoid; Q7T3E5; -.
DR PhylomeDB; Q7T3E5; -.
DR UniPathway; UPA00334; UER00726.
DR PRO; PR:Q7T3E5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0047315; F:kynurenine-glyoxylate transaminase activity; ISS:UniProtKB.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; ISS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; ISS:UniProtKB.
DR GO; GO:0070189; P:kynurenine metabolic process; ISS:UniProtKB.
DR GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR034612; KAT_III.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43807:SF6; PTHR43807:SF6; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 2: Evidence at transcript level;
KW Aminotransferase; Lyase; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..450
FT /note="Kynurenine--oxoglutarate transaminase 3"
FT /id="PRO_0000287707"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT MOD_RES 278
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
SQ SEQUENCE 450 AA; 50345 MW; 473A55EBF1401312 CRC64;
MHPIHLLRIV SSVRRLLQTN RCRSFSSCQH NMASIKHKNA RRIEGLDKNV WVAFTSVAAD
PSIVNLGQGY PDIPPPSYVK EGLAQAAMVD RLNQYTRGFG HPTLVKALSK VYGKVYDRQL
DPFKEILVTV GGYGSLFSTM QALVEEGDEV IIIEPFFDCY VPMVKMAGAK PVLIPLRLKS
TATTGISSAD WVLDQEELAS KFNSKTKAII VNTPNNPIGK IFSRSELQAI ADLCIKHDTL
CFSDEVYEWL IYKGHEHVKI ATLPGMWDRT ITVGSAGKTF SVTGWKLGWS IGPEHLIRHL
QTVMQNSLYT CPTPLQEAVG RGLLRDFELM GQPDCYFSAL ALELEGKRDR MAAMLAQTGM
TPVVPEGGYF MIVDVTALNQ DLTHMGDDEP YDYKFVKWMI KEKKLAAIPV TAFVGEDSVK
QFEKYIRLCF IKQESTLDAA EAILKNWNKG
