KAT3_BOVIN
ID KAT3_BOVIN Reviewed; 455 AA.
AC Q0P5G4;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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. 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; BC120067; AAI20068.1; -; mRNA.
DR RefSeq; NP_001068838.1; NM_001075370.1.
DR AlphaFoldDB; Q0P5G4; -.
DR SMR; Q0P5G4; -.
DR STRING; 9913.ENSBTAP00000000643; -.
DR PaxDb; Q0P5G4; -.
DR PRIDE; Q0P5G4; -.
DR Ensembl; ENSBTAT00000000643; ENSBTAP00000000643; ENSBTAG00000000505.
DR GeneID; 508712; -.
DR KEGG; bta:508712; -.
DR CTD; 56267; -.
DR VEuPathDB; HostDB:ENSBTAG00000000505; -.
DR VGNC; VGNC:30758; KYAT3.
DR eggNOG; KOG0257; Eukaryota.
DR GeneTree; ENSGT00940000155827; -.
DR HOGENOM; CLU_017584_4_0_1; -.
DR InParanoid; Q0P5G4; -.
DR OMA; SVAMTGW; -.
DR OrthoDB; 683031at2759; -.
DR TreeFam; TF352342; -.
DR UniPathway; UPA00334; UER00726.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000000505; Expressed in granulosa cell and 104 other tissues.
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; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:Ensembl.
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..455
FT /note="Kynurenine--oxoglutarate transaminase 3"
FT /id="PRO_0000287703"
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 430
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 455 AA; 51472 MW; E353F80DCD854BD6 CRC64;
MFLAWERLCT LSCRPKFLKT VWASKILGLS TSAKMSLRFK NAKRIEGLDS NIWIEFTKLA
ADPSVVNLGQ GLPDISPPVY VKEELSKIAA IDNLNQYTRG FGHPSLVKAL SCLYEKFYHN
KINPNEEILV TVGAYGSLFN AIQGLIDEGD EVIVIVPFFD CYESMVRMAG ATPVFVPLRC
KPVDGKKCSS SDWTLDPQEL ASKFNSKTKA IILNTPHNPL GKVYTKEELQ VIADLCIKYD
TLCISDEVYE WLVYTGNKHF KIATFPGMWE RTITIGSAGK TFSVTGWKLG WSIGPKHLIK
HLQTVQQNTV YTCATPLQEA LAQAFWIDIK RMDDPECYFN SLPKELEVKR DRMVHLLESV
GLKSIVPDGG YFIIADVSLL DVDLLDMKDS NEPYDYKFVK WMIKNKKLSA IPVSAFCNAE
TKSQFEKFVR FCFIKKDSTL DAAEEIIKAW SRQNS
