ID A0A3Q4HRG6_NEOBR Unreviewed; 303 AA.
AC A0A3Q4HRG6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Kynurenine--oxoglutarate transaminase 3 {ECO:0000256|ARBA:ARBA00019100};
DE EC=2.6.1.63 {ECO:0000256|ARBA:ARBA00013010};
DE EC=2.6.1.7 {ECO:0000256|ARBA:ARBA00012751};
DE AltName: Full=Cysteine-S-conjugate beta-lyase 2 {ECO:0000256|ARBA:ARBA00031600};
DE AltName: Full=Kynurenine aminotransferase 3 {ECO:0000256|ARBA:ARBA00029778};
DE AltName: Full=Kynurenine aminotransferase III {ECO:0000256|ARBA:ARBA00030993};
DE AltName: Full=Kynurenine--glyoxylate transaminase {ECO:0000256|ARBA:ARBA00031198};
DE AltName: Full=Kynurenine--oxoglutarate transaminase III {ECO:0000256|ARBA:ARBA00031371};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000019987.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000019987.1}
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=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:0000256|ARBA:ARBA00023992};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65901;
CC Evidence={ECO:0000256|ARBA:ARBA00023992};
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 -!- 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:0000256|ARBA:ARBA00023943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65897;
CC Evidence={ECO:0000256|ARBA:ARBA00023943};
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}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR AlphaFoldDB; A0A3Q4HRG6; -.
DR Ensembl; ENSNBRT00000020518.1; ENSNBRP00000019987.1; ENSNBRG00000015169.1.
DR GeneTree; ENSGT00940000155827; -.
DR UniPathway; UPA00334; UER00726.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000015169; Expressed in skeletal muscle tissue and 6 other cell types or tissues.
DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0047315; F:kynurenine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00609; AAT_like; 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 PANTHER; PTHR43807; FI04487P; 1.
DR PANTHER; PTHR43807:SF6; KYNURENINE--OXOGLUTARATE TRANSAMINASE 3; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 30..279
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 303 AA; 33568 MW; 26B4C90BF8F6535C CRC64;
MMSRHTHAKR IEGLDKNVWV AFTALAADPS VVNLGQGFPD IPPPSYVKEA LAKAASVDMM
NQYTRGFGHP SLVKALSQVY GKAYGRQIDP LKEILVTVGG YGSLFSAIQA LVEEGDEVII
IEPFFDCYVP MVRMAGGKPV LIPLRLSGKK TITSADWFLD PDELAGKFNS KTKAIIINTP
NNPIGKVFTK DELQMIADLC IKHDTLCFSD EVYEWLVYRG HQHVKIATLP GMWDRTVTIG
SAGKTFSVTG WKLGWSIGPE HLMKHLQTVM QNSLYTCQTG TVVGEYYNML CVYLIICSQL
SEI
//
