KAT3_RAT
ID KAT3_RAT Reviewed; 454 AA.
AC Q58FK9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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:0000312|RGD:1359262};
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:0000312|RGD:1359262}; Synonyms=Ccbl2, Kat3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16376499; DOI=10.1016/j.gene.2005.09.034;
RA Yu P., Li Z., Zhang L., Tagle D.A., Cai T.;
RT "Characterization of kynurenine aminotransferase III, a novel member of a
RT phylogenetically conserved KAT family.";
RL Gene 365:111-118(2006).
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. Has transaminase activity towards L-kynurenine,
CC tryptophan, phenylalanine, serine, cysteine, methionine, histidine,
CC glutamine and asparagine with glyoxylate as an amino group acceptor (in
CC vitro). Has lower activity with 2-oxoglutarate as amino group acceptor
CC (in vitro). {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}.
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DR EMBL; AY955395; AAX55607.1; -; mRNA.
DR RefSeq; NP_001015037.1; NM_001015037.1.
DR AlphaFoldDB; Q58FK9; -.
DR SMR; Q58FK9; -.
DR iPTMnet; Q58FK9; -.
DR PhosphoSitePlus; Q58FK9; -.
DR PRIDE; Q58FK9; -.
DR GeneID; 541589; -.
DR KEGG; rno:541589; -.
DR CTD; 56267; -.
DR RGD; 1359262; Kyat3.
DR InParanoid; Q58FK9; -.
DR OrthoDB; 683031at2759; -.
DR PhylomeDB; Q58FK9; -.
DR BRENDA; 2.6.1.7; 5301.
DR UniPathway; UPA00334; UER00726.
DR PRO; PR:Q58FK9; -.
DR Proteomes; UP000002494; 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:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISO:RGD.
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 Acetylation; Aminotransferase; Lyase; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..454
FT /note="Kynurenine--oxoglutarate transaminase 3"
FT /id="PRO_0000287706"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT MOD_RES 116
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6YP21"
FT MOD_RES 116
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q71RI9"
FT MOD_RES 280
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
SQ SEQUENCE 454 AA; 51044 MW; 77F70B4DEC32D9AC CRC64;
MLLAQRRLFS LGCRAKPIKT IYSSKVLGLS TSAKMALRFK NAKRIEGLDQ NVWVEFTKLA
ADPSVVNLGQ GFPDITLPSY VQEELSKAAF IDNLNQYTRG FGHPSLVKAL SCLYGKIYQK
QIDPNEEILV TVGGYGSLFN AIQGLVDPGD EVIIMVPFYD CYEPMVKMAG AVPVFIPLRS
KRTDGMKWTS SDWTFNPQEL ESKFSSKTKA IILNTPHNPI GKVYTREELQ VIADLCIKHD
TLCISDEVYE WLVYTGHKHI KVASLPGMWD RTLTIGSAGK TFSVTGWKLG WSIGPGHLIK
HLRTVQQTSV YTCATPLQAA LAEAFWIDIK RMDDPECYFN SLPKELEVKR DRMACLLNSV
GLKPIIPDGG YFIIADVSSL GVDLSDVKSD EPYDYKFVKW MTKNKKLSAI PVSAFCDSES
KPHFEKLVRF CFIKKDSTLD AAEEIFRTWN SRKS
