ID M3ZUD8_XIPMA Unreviewed; 444 AA.
AC M3ZUD8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Kynurenine aminotransferase 1 {ECO:0000313|Ensembl:ENSXMAP00000005831.2};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000005831.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000005831.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000005831.2};
RG Ensembl;
RL Submitted (NOV-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=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 RefSeq; XP_005798734.1; XM_005798677.2.
DR AlphaFoldDB; M3ZUD8; -.
DR STRING; 8083.ENSXMAP00000005831; -.
DR Ensembl; ENSXMAT00000005837.2; ENSXMAP00000005831.2; ENSXMAG00000005791.2.
DR GeneID; 102237088; -.
DR KEGG; xma:102237088; -.
DR CTD; 883; -.
DR eggNOG; KOG0257; Eukaryota.
DR GeneTree; ENSGT00940000158797; -.
DR HOGENOM; CLU_017584_4_0_1; -.
DR InParanoid; M3ZUD8; -.
DR OMA; SQGANQY; -.
DR OrthoDB; 176869at2759; -.
DR Proteomes; UP000002852; 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:UP000002852}.
FT DOMAIN 55..435
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 444 AA; 49878 MW; 18CE487FF405FCDC CRC64;
MGIIRILAPY LTLIRPNLGQ NHKLIMARRL YASRTIGVDK NVWVEFTQLA ADYKAVNLGQ
GFPDFSPPQF VQDAFCKAVS GGPQMHQYTR AFGHPRLVKS LAKFFSRIVG QEIDPFEDVL
VTVGAYQALF CAFQALIDDG DEVIIVEPFF DCYQPMVLMA GGTAVYVPLR PKGGSTVLSS
GDWVLSAEEL ASKITPRTKA IVINTPNNPL GKVYKVEELQ MIADLCIKHD LLCFSDEVYE
WLTYDGAKHI KIASLPGMWE RTITVGSAGK TFSATGWKVG WAISSGKLIK HMKIIHQNSV
YHCATAAQEA VSHGFDREYE LFGTPESYFQ QLPAMLHQKR QKVASCLRSV GLQPVMPEGG
YFMITDISSV HVDLNDESTK NESYDFRFVK WLIKEKGLAT IPVSAFFSPE HSKEFDKYIR
FCFVKEDSTL EAAEEILRKW SQKE
//
