KAT_AEDAE
ID KAT_AEDAE Reviewed; 477 AA.
AC Q17CS8; Q95VY4;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Kynurenine aminotransferase {ECO:0000303|PubMed:12110301};
DE EC=2.6.1.- {ECO:0000269|PubMed:12110301, ECO:0000269|PubMed:15556614};
DE EC=2.6.1.63 {ECO:0000269|PubMed:15556614};
DE EC=2.6.1.7 {ECO:0000269|PubMed:12110301, ECO:0000269|PubMed:15556614};
DE AltName: Full=AeKAT {ECO:0000303|PubMed:12110301};
DE Flags: Precursor;
GN Name=KAT {ECO:0000303|PubMed:12110301};
GN ORFNames=AAEL004435 {ECO:0000312|EMBL:EAT44194.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000312|Proteomes:UP000008820};
RN [1] {ECO:0000312|EMBL:AAK97625.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12110301; DOI=10.1016/s0965-1748(02)00032-2;
RA Fang J., Han Q., Li J.;
RT "Isolation, characterization, and functional expression of kynurenine
RT aminotransferase cDNA from the yellow fever mosquito, Aedes aegypti(1).";
RL Insect Biochem. Mol. Biol. 32:943-950(2002).
RN [2] {ECO:0000312|Proteomes:UP000008820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000312|Proteomes:UP000008820};
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RX PubMed=15556614; DOI=10.1016/j.febslet.2004.09.088;
RA Han Q., Li J.;
RT "Cysteine and keto acids modulate mosquito kynurenine aminotransferase
RT catalyzed kynurenic acid production.";
RL FEBS Lett. 577:381-385(2004).
RN [4] {ECO:0007744|PDB:1YIY, ECO:0007744|PDB:1YIZ}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 49-477 WITH PYRIDOXAL PHOSPHATE,
RP COFACTOR, AND SUBUNIT.
RX PubMed=15853804; DOI=10.1111/j.1742-4658.2005.04643.x;
RA Han Q., Gao Y.G., Robinson H., Ding H., Wilson S., Li J.;
RT "Crystal structures of Aedes aegypti kynurenine aminotransferase.";
RL FEBS J. 272:2198-2206(2005).
RN [5] {ECO:0007744|PDB:2R5C, ECO:0007744|PDB:2R5E}
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 49-477 WITH PYRIDOXAL PHOSPHATE;
RP CYSTEINE AND GLUTAMINE, COFACTOR, AND SUBUNIT.
RX PubMed=18186649; DOI=10.1021/bi701800j;
RA Han Q., Gao Y.G., Robinson H., Li J.;
RT "Structural insight into the mechanism of substrate specificity of aedes
RT kynurenine aminotransferase.";
RL Biochemistry 47:1622-1630(2008).
RN [6] {ECO:0007744|PDB:5VEH}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 49-475, AND X-RAY STRUCTURE
RP REFINEMENT OF 1YIZ.
RX PubMed=29113027; DOI=10.1111/febs.14320;
RA Wlodawer A., Dauter Z., Porebski P.J., Minor W., Stanfield R.,
RA Jaskolski M., Pozharski E., Weichenberger C.X., Rupp B.;
RT "Detect, correct, retract: How to manage incorrect structural models.";
RL FEBS J. 285:444-466(2018).
CC -!- FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan
CC metabolite L-kynurenine to form kynurenic acid (KA) (PubMed:12110301,
CC PubMed:15556614). Also catalyzes the irreversible transamination of
CC several amino acids including cysteine, tyrosine, glutamine,
CC methionine, histidine and phenylalanine (PubMed:15556614). Can use
CC various keto-acids as the amino group acceptor (PubMed:15556614,
CC PubMed:12110301). {ECO:0000269|PubMed:12110301,
CC ECO:0000269|PubMed:15556614}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-kynurenine + pyruvate = H2O + kynurenate + L-alanine;
CC Xref=Rhea:RHEA:65916, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57959, ChEBI:CHEBI:57972, ChEBI:CHEBI:58454;
CC Evidence={ECO:0000269|PubMed:12110301, ECO:0000269|PubMed:15556614};
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; Evidence={ECO:0000269|PubMed:12110301,
CC ECO:0000269|PubMed:15556614};
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:0000269|PubMed:15556614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxobutanoate + L-kynurenine = (2S)-2-aminobutanoate + H2O +
CC kynurenate; Xref=Rhea:RHEA:66044, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16763, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454,
CC ChEBI:CHEBI:74359; Evidence={ECO:0000269|PubMed:15556614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxobutanoate + L-cysteine = (2S)-2-aminobutanoate + 2-oxo-3-
CC sulfanylpropanoate; Xref=Rhea:RHEA:66108, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:57678, ChEBI:CHEBI:74359;
CC Evidence={ECO:0000269|PubMed:15556614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxobutanoate + L-tyrosine = (2S)-2-aminobutanoate + 3-(4-
CC hydroxyphenyl)pyruvate; Xref=Rhea:RHEA:66112, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:36242, ChEBI:CHEBI:58315, ChEBI:CHEBI:74359;
CC Evidence={ECO:0000269|PubMed:15556614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxobutanoate + L-glutamine = (2S)-2-aminobutanoate + 2-
CC oxoglutaramate; Xref=Rhea:RHEA:66116, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:16769, ChEBI:CHEBI:58359, ChEBI:CHEBI:74359;
CC Evidence={ECO:0000269|PubMed:15556614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxobutanoate + L-methionine = (2S)-2-aminobutanoate + 4-
CC methylsulfanyl-2-oxobutanoate; Xref=Rhea:RHEA:66120,
CC ChEBI:CHEBI:16723, ChEBI:CHEBI:16763, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:74359; Evidence={ECO:0000269|PubMed:15556614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxobutanoate + L-histidine = (2S)-2-aminobutanoate + 3-
CC (imidazol-5-yl)pyruvate; Xref=Rhea:RHEA:66124, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:57595, ChEBI:CHEBI:58133, ChEBI:CHEBI:74359;
CC Evidence={ECO:0000269|PubMed:15556614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxobutanoate + L-phenylalanine = (2S)-2-aminobutanoate + 3-
CC phenylpyruvate; Xref=Rhea:RHEA:66128, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:18005, ChEBI:CHEBI:58095, ChEBI:CHEBI:74359;
CC Evidence={ECO:0000269|PubMed:15556614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=indole-3-pyruvate + L-kynurenine = H2O + kynurenate + L-
CC tryptophan; Xref=Rhea:RHEA:66052, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17640, ChEBI:CHEBI:57912, ChEBI:CHEBI:57959,
CC ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:15556614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxohexanoate + L-kynurenine = H2O + kynurenate + L-2-
CC aminohexanoate; Xref=Rhea:RHEA:66060, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:35177, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454,
CC ChEBI:CHEBI:58455; Evidence={ECO:0000269|PubMed:15556614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methyl-2-oxopentanoate + L-kynurenine = H2O + kynurenate +
CC L-leucine; Xref=Rhea:RHEA:66068, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:57427, ChEBI:CHEBI:57959,
CC ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:15556614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxopentanoate + L-kynurenine = H2O + kynurenate + L-2-
CC aminopentanoate; Xref=Rhea:RHEA:66076, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28644, ChEBI:CHEBI:57959, ChEBI:CHEBI:58441,
CC ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:15556614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-kynurenine + oxaloacetate = H2O + kynurenate + L-aspartate;
CC Xref=Rhea:RHEA:66084, ChEBI:CHEBI:15377, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454;
CC Evidence={ECO:0000269|PubMed:15556614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenylpyruvate + L-kynurenine = H2O + kynurenate + L-
CC phenylalanine; Xref=Rhea:RHEA:66092, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18005, ChEBI:CHEBI:57959, ChEBI:CHEBI:58095,
CC ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:15556614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(4-hydroxyphenyl)pyruvate + L-kynurenine = H2O + kynurenate
CC + L-tyrosine; Xref=Rhea:RHEA:66100, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:36242, ChEBI:CHEBI:57959, ChEBI:CHEBI:58315,
CC ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:15556614};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:15853804, ECO:0000269|PubMed:18186649};
CC -!- ACTIVITY REGULATION: Competitive inhibition of L-kynurenine
CC transamination by glutamine, methionine and histidine but not by
CC tyrosine and phenylalanine (PubMed:15556614). Cysteine concentration
CC between 0.31-2.5 mM increases L-kynurenine transamination while
CC concentration above 2.5 mM inhibits L-kynurenine transamination
CC (PubMed:15556614). Keto-acids as amino acceptors modulate the
CC transamination activity toward L-kynurenine (PubMed:15556614).
CC {ECO:0000269|PubMed:15556614}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 mM for cysteine (at 45 degrees Celsius, at pH 8.5 and with
CC ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614};
CC KM=0.9 mM for tyrosine (at 45 degrees Celsius, at pH 8.5 and with
CC ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614};
CC KM=3.8 mM for glutamine (at 45 degrees Celsius, at pH 8.5 and with
CC ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614};
CC KM=1.4 mM for methionine (at 45 degrees Celsius, at pH 8.5 and with
CC ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614};
CC KM=1.5 mM for histidine (at 45 degrees Celsius, at pH 8.5 and with
CC ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614};
CC KM=3.5 mM for phenylalanine (at 45 degrees Celsius, at pH 8.5 and
CC with ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614};
CC KM=4.3 mM for kynurenine (at 45 degrees Celsius, at pH 8.5 and with
CC ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614};
CC KM=6.1 mM for asparagine (at 45 degrees Celsius, at pH 8.5 and with
CC ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614};
CC KM=12.9 mM for tryptophan (at 45 degrees Celsius, at pH 8.5 and with
CC ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614};
CC KM=34.5 mM for leucine (at 45 degrees Celsius, at pH 8.5 and with
CC ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614};
CC KM=32.7 mM for serine (at 45 degrees Celsius, at pH 8.5 and with
CC ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614};
CC KM=246 mM for alanine (at 45 degrees Celsius, at pH 8.5 and with
CC ketobutyrate as cosubstrate) {ECO:0000269|PubMed:15556614};
CC KM=92.7 mM for amino-butyrate (at 45 degrees Celsius, at pH 8.5 and
CC with pyruvate as cosubstrate) {ECO:0000269|PubMed:15556614};
CC Note=kcat is 206 min(-1) for cysteine (at 45 degrees Celsius, at pH
CC 8.5 and with ketobutyrate as cosubstrate) (PubMed:15556614). kcat is
CC 139 min(-1) for tyrosine (at 45 degrees Celsius, at pH 8.5 and with
CC ketobutyrate as cosubstrate) (PubMed:15556614). kcat is 561 min(-1)
CC for glutamine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate
CC as cosubstrate) (PubMed:15556614). kcat is 163 min(-1) for methionine
CC (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as
CC cosubstrate) (PubMed:15556614). kcat is 168 min(-1) for histidine (at
CC 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)
CC (PubMed:15556614). kcat is 283 min(-1) for cysteine (at 45 degrees
CC Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)
CC (PubMed:15556614). kcat is 172 min(-1) for kynurenine (at 45 degrees
CC Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)
CC (PubMed:15556614). kcat is 230 min(-1) for asparagine (at 45 degrees
CC Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)
CC (PubMed:15556614). kcat is 283 min(-1) for tryptophan (at 45 degrees
CC Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)
CC (PubMed:15556614). kcat is 758 min(-1) for leucine (at 45 degrees
CC Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)
CC (PubMed:15556614). kcat is 345 min(-1) for serine (at 45 degrees
CC Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)
CC (PubMed:15556614). kcat is 1540 min(-1) for alanine (at 45 degrees
CC Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)
CC (PubMed:15556614). kcat is 317 min(-1) for amino-butyrate (at 45
CC degrees Celsius, at pH 8.5 and with pyruvate as cosubstrate)
CC (PubMed:15556614). {ECO:0000269|PubMed:15556614};
CC pH dependence:
CC Optimum pH is 8.5 and 10 (with pyruvate as cosubstrate).
CC {ECO:0000269|PubMed:12110301};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius (at pH 8.5 and with
CC pyruvate as cosubstrate). {ECO:0000269|PubMed:12110301};
CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; kynurenate
CC from L-kynurenine: step 1/2. {ECO:0000269|PubMed:12110301,
CC ECO:0000269|PubMed:15556614}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:12110301,
CC ECO:0000305|PubMed:15853804, ECO:0000305|PubMed:18186649}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in developing ovaries (PubMed:12110301).
CC Expressed at high levels in the head (PubMed:12110301).
CC {ECO:0000269|PubMed:12110301}.
CC -!- DEVELOPMENTAL STAGE: Expressed in larvae, pupae and adults
CC (PubMed:12110301). Expressed at low levels in larvae, then expression
CC increases at the beginning of pupal development to reach high
CC expression levels in adults (PubMed:12110301).
CC {ECO:0000269|PubMed:12110301}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- CAUTION: X-ray structure in 1YIZ has been refined and redeposited in
CC 5VEH. {ECO:0000269|PubMed:29113027}.
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DR EMBL; AF395204; AAK97625.1; -; mRNA.
DR EMBL; CH477304; EAT44194.1; -; Genomic_DNA.
DR RefSeq; XP_001649143.1; XM_001649093.1.
DR PDB; 1YIY; X-ray; 1.90 A; A/B=49-477.
DR PDB; 1YIZ; X-ray; 1.55 A; A/B=49-477.
DR PDB; 2R5C; X-ray; 1.96 A; A/B=49-477.
DR PDB; 2R5E; X-ray; 1.84 A; A/B=49-477.
DR PDB; 5VEH; X-ray; 1.55 A; A/B=49-475.
DR PDBsum; 1YIY; -.
DR PDBsum; 1YIZ; -.
DR PDBsum; 2R5C; -.
DR PDBsum; 2R5E; -.
DR PDBsum; 5VEH; -.
DR AlphaFoldDB; Q17CS8; -.
DR SMR; Q17CS8; -.
DR STRING; 7159.AAEL004435-PA; -.
DR GeneID; 5564787; -.
DR KEGG; aag:5564787; -.
DR VEuPathDB; VectorBase:AAEL004435; -.
DR eggNOG; KOG0257; Eukaryota.
DR HOGENOM; CLU_017584_4_0_1; -.
DR InParanoid; Q17CS8; -.
DR OMA; SVAMTGW; -.
DR OrthoDB; 683031at2759; -.
DR PhylomeDB; Q17CS8; -.
DR BRENDA; 2.6.1.7; 149.
DR UniPathway; UPA00334; UER00726.
DR Proteomes; UP000008820; Chromosome 3.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0047315; F:kynurenine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Glycoprotein; Mitochondrion;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..49
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 50..477
FT /note="Kynurenine aminotransferase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000452236"
FT BINDING 44..45
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18186649,
FT ECO:0000312|PDB:2R5C, ECO:0000312|PDB:2R5E"
FT BINDING 121
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:15853804,
FT ECO:0000269|PubMed:18186649, ECO:0000312|PDB:1YIY,
FT ECO:0000312|PDB:2R5C, ECO:0000312|PDB:2R5E"
FT BINDING 158..159
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:15853804,
FT ECO:0000269|PubMed:18186649, ECO:0000312|PDB:1YIY,
FT ECO:0000312|PDB:2R5C, ECO:0000312|PDB:2R5E"
FT BINDING 241
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:15853804,
FT ECO:0000269|PubMed:18186649, ECO:0000312|PDB:1YIY,
FT ECO:0000312|PDB:2R5C, ECO:0000312|PDB:2R5E"
FT BINDING 272
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:15853804,
FT ECO:0000269|PubMed:18186649, ECO:0000312|PDB:1YIY,
FT ECO:0000312|PDB:2R5C, ECO:0000312|PDB:2R5E"
FT BINDING 300
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:15853804,
FT ECO:0000269|PubMed:18186649, ECO:0000312|PDB:1YIY,
FT ECO:0000312|PDB:2R5C, ECO:0000312|PDB:2R5E"
FT BINDING 311
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:15853804,
FT ECO:0000269|PubMed:18186649, ECO:0000312|PDB:1YIY,
FT ECO:0000312|PDB:2R5C, ECO:0000312|PDB:2R5E"
FT BINDING 453
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18186649,
FT ECO:0000312|PDB:2R5C, ECO:0000312|PDB:2R5E"
FT MOD_RES 303
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:15853804,
FT ECO:0000312|PDB:1YIY"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 105
FT /note="D -> N (in Ref. 1; AAK97625)"
FT /evidence="ECO:0000305"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 74..85
FT /evidence="ECO:0007829|PDB:1YIZ"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 128..142
FT /evidence="ECO:0007829|PDB:1YIZ"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:1YIZ"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 157..169
FT /evidence="ECO:0007829|PDB:1YIZ"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:1YIZ"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:1YIZ"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:2R5E"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:1YIZ"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:1YIZ"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 249..262
FT /evidence="ECO:0007829|PDB:1YIZ"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:1YIZ"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:1YIZ"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:1YIZ"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:2R5E"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:1YIZ"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 319..330
FT /evidence="ECO:0007829|PDB:1YIZ"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 338..352
FT /evidence="ECO:0007829|PDB:1YIZ"
FT TURN 353..356
FT /evidence="ECO:0007829|PDB:1YIZ"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:2R5C"
FT HELIX 361..383
FT /evidence="ECO:0007829|PDB:1YIZ"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:1YIZ"
FT STRAND 391..399
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:2R5E"
FT TURN 405..408
FT /evidence="ECO:0007829|PDB:1YIZ"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 417..428
FT /evidence="ECO:0007829|PDB:1YIZ"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 436..439
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 442..447
FT /evidence="ECO:0007829|PDB:1YIZ"
FT TURN 448..450
FT /evidence="ECO:0007829|PDB:1YIZ"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:1YIZ"
FT HELIX 460..473
FT /evidence="ECO:0007829|PDB:1YIZ"
SQ SEQUENCE 477 AA; 53506 MW; 85B9FA606569B1CA CRC64;
MMFLRNHNSV GGAIRTAVVL QDLQFIVSNK SSALTGAVSS VHRQQIRTMS STSNETMHNK
FDLPKRYQGS TKSVWVEYIQ LAAQYKPLNL GQGFPDYHAP KYALDALAAA ANSPDPLANQ
YTRGFGHPRL VQALSKLYSQ LVDRTINPMT EVLVTVGAYE ALYATIQGHV DEGDEVIIIE
PFFDCYEPMV KAAGGIPRFI PLKPNKTGGT ISSADWVLDN NELEALFNEK TKMIIINTPH
NPLGKVMDRA ELEVVANLCK KWNVLCVSDE VYEHMVFEPF EHIRICTLPG MWERTITIGS
AGKTFSLTGW KIGWAYGPEA LLKNLQMVHQ NCVYTCATPI QEAIAVGFET ELKRLKSPEC
YFNSISGELM AKRDYMASFL AEVGMNPTVP QGGYFMVADW SSLDSKVDLT QETDARKDYR
FTKWMTKSVG LQGIPPSAFY SEPNKHLGED FVRYCFFKKD ENLQKAAEIL RKWKGSS
