KAT1_RAT
ID KAT1_RAT Reviewed; 423 AA.
AC Q08415; Q9R096;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Kynurenine--oxoglutarate transaminase 1 {ECO:0000305|PubMed:7796908};
DE Short=Kynurenine--oxoglutarate transaminase I;
DE EC=2.6.1.7 {ECO:0000269|PubMed:2072101, ECO:0000269|PubMed:6783036, ECO:0000269|PubMed:7796908};
DE AltName: Full=Cysteine-S-conjugate beta-lyase {ECO:0000305|PubMed:8502223};
DE EC=4.4.1.13 {ECO:0000269|PubMed:8502223};
DE AltName: Full=Glutamine transaminase K;
DE Short=GTK;
DE AltName: Full=Glutamine--phenylpyruvate transaminase {ECO:0000305|PubMed:8502223};
DE EC=2.6.1.64 {ECO:0000269|PubMed:7796908, ECO:0000269|PubMed:8502223};
DE AltName: Full=Kynurenine aminotransferase 1 {ECO:0000312|RGD:1306912};
DE AltName: Full=Kynurenine aminotransferase I;
DE Short=KATI;
GN Name=Kyat1 {ECO:0000312|RGD:1306912}; Synonyms=Ccbl1, Kat;
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] (ISOFORM 2), PROTEIN SEQUENCE OF 39-62; 228-259
RP AND 388-401, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=8502223;
RA Perry S.J., Schofield M.A., MacFarlane M., Lock E.A., King L.J.,
RA Gibson G.G., Goldfarb P.S.;
RT "Isolation and expression of a cDNA coding for rat kidney cytosolic
RT cysteine conjugate beta-lyase.";
RL Mol. Pharmacol. 43:660-665(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=7926014; DOI=10.1016/0014-5793(94)01003-x;
RA Mosca M., Cozzi L., Breton J., Speciale C., Okuno E., Schwarcz R.,
RA Benatti L.;
RT "Molecular cloning of rat kynurenine aminotransferase: identity with
RT glutamine transaminase K.";
RL FEBS Lett. 353:21-24(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), AND BIOPHYSICOCHEMICAL
RP PROPERTIES (ISOFORM 1).
RC TISSUE=Cerebellum;
RX PubMed=7796908; DOI=10.1016/0014-5793(95)00546-l;
RA Malherbe P., Alberati-Giani D., Koehler C., Cesura A.M.;
RT "Identification of a mitochondrial form of kynurenine
RT aminotransferase/glutamine transaminase K from rat brain.";
RL FEBS Lett. 367:141-144(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=12850267; DOI=10.1016/s0167-4781(03)00071-x;
RA Mosca M., Croci C., Mostardini M., Breton J., Malyszko J., Avanzi N.,
RA Toma S., Benatti L., Gatti S.;
RT "Tissue expression and translational control of rat kynurenine
RT aminotransferase/glutamine transaminase K mRNAs.";
RL Biochim. Biophys. Acta 1628:1-10(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=6783036; DOI=10.1042/bj1890581;
RA Okuno E., Minatogawa Y., Nakamura M., Kamoda N., Nakanishi J., Makino M.,
RA Kido R.;
RT "Crystallization and characterization of human liver kynurenine-glyoxylate
RT aminotransferase. Identity with alanine-glyoxylate aminotransferase and
RT serine-pyruvate aminotransferase.";
RL Biochem. J. 189:581-590(1980).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=2072101; DOI=10.1111/j.1471-4159.1991.tb03783.x;
RA Okuno E., Schmidt W., Parks D.A., Nakamura M., Schwarcz R.;
RT "Measurement of rat brain kynurenine aminotransferase at physiological
RT kynurenine concentrations.";
RL J. Neurochem. 57:533-540(1991).
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 (PubMed:7796908, PubMed:6783036, PubMed:2072101).
CC Metabolizes the cysteine conjugates of certain halogenated alkenes and
CC alkanes to form reactive metabolites. Catalyzes the beta-elimination of
CC S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the
CC cleavage of the C-S or C-Se bond (PubMed:8502223).
CC {ECO:0000269|PubMed:2072101, ECO:0000269|PubMed:6783036,
CC ECO:0000269|PubMed:7796908, ECO:0000269|PubMed:8502223}.
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:2072101,
CC ECO:0000269|PubMed:6783036, ECO:0000269|PubMed:7796908};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65561;
CC Evidence={ECO:0000305|PubMed:7796908};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenylpyruvate + L-glutamine = 2-oxoglutaramate + L-
CC phenylalanine; Xref=Rhea:RHEA:17593, ChEBI:CHEBI:16769,
CC ChEBI:CHEBI:18005, ChEBI:CHEBI:58095, ChEBI:CHEBI:58359; EC=2.6.1.64;
CC Evidence={ECO:0000269|PubMed:7796908, ECO:0000269|PubMed:8502223};
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:0000269|PubMed:8502223};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18122;
CC Evidence={ECO:0000305|PubMed:8502223};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- ACTIVITY REGULATION: Inhibited by aminooxyacetate (in vitro).
CC {ECO:0000269|PubMed:2072101}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for L-kynurenine (with 2-oxoglutarate as cosubstrate)
CC {ECO:0000269|PubMed:2072101};
CC KM=910 uM for L-kynurenine (with pyruvate as cosubstrate)
CC {ECO:0000269|PubMed:2072101};
CC KM=150 uM for 2-oxoglutarate {ECO:0000269|PubMed:2072101};
CC KM=160 uM for pyruvate {ECO:0000269|PubMed:2072101};
CC pH dependence:
CC Optimum pH is 9-9.5. {ECO:0000269|PubMed:6783036};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 1]:
CC Kinetic parameters:
CC KM=1630 uM for L-kynurenine (with 2-oxoglutarate as cosubstrate)
CC {ECO:0000269|PubMed:7796908};
CC KM=96.2 uM for L-kynurenine (with L-pyruvate as cosubstrate)
CC {ECO:0000269|PubMed:7796908};
CC Vmax=10.8 nmol/min/mg enzyme with L-kynurenine as substrate (with 2-
CC oxoglutarate as cosubstrate) {ECO:0000269|PubMed:7796908};
CC Vmax=0.39 nmol/min/mg enzyme with L-kynurenine as substrate (with L-
CC pyruvate as cosubstrate) {ECO:0000269|PubMed:7796908};
CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; kynurenate
CC from L-kynurenine: step 1/2. {ECO:0000305|PubMed:7796908}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:6783036}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:7796908, ECO:0000269|PubMed:8502223}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion matrix
CC {ECO:0000269|PubMed:7796908}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=S-KAT/GTK {ECO:0000303|PubMed:7796908};
CC IsoId=Q08415-2; Sequence=Displayed;
CC Name=1; Synonyms=M-KAT/GTK {ECO:0000303|PubMed:7796908};
CC IsoId=Q08415-1; Sequence=VSP_060909;
CC -!- TISSUE SPECIFICITY: Detected in kidney. {ECO:0000269|PubMed:8502223}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; S61960; AAB26845.1; -; mRNA.
DR EMBL; S74029; AAB32197.1; -; mRNA.
DR EMBL; Z49696; CAA89696.1; -; mRNA.
DR EMBL; AF100154; AAF06837.1; -; Genomic_DNA.
DR EMBL; AF267749; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S66270; S66270.
DR RefSeq; NP_001013182.3; NM_001013164.3.
DR AlphaFoldDB; Q08415; -.
DR SMR; Q08415; -.
DR STRING; 10116.ENSRNOP00000021865; -.
DR iPTMnet; Q08415; -.
DR PhosphoSitePlus; Q08415; -.
DR jPOST; Q08415; -.
DR PaxDb; Q08415; -.
DR PRIDE; Q08415; -.
DR GeneID; 311844; -.
DR KEGG; rno:311844; -.
DR UCSC; RGD:1306912; rat. [Q08415-2]
DR CTD; 883; -.
DR RGD; 1306912; Kyat1.
DR eggNOG; KOG0257; Eukaryota.
DR InParanoid; Q08415; -.
DR OrthoDB; 683031at2759; -.
DR PhylomeDB; Q08415; -.
DR BRENDA; 2.6.1.7; 5301.
DR Reactome; R-RNO-71240; Tryptophan catabolism.
DR Reactome; R-RNO-8964208; Phenylalanine metabolism.
DR Reactome; R-RNO-8964539; Glutamate and glutamine metabolism.
DR SABIO-RK; Q08415; -.
DR UniPathway; UPA00334; UER00726.
DR PRO; PR:Q08415; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IDA:RGD.
DR GO; GO:0047316; F:glutamine-phenylpyruvate transaminase activity; IDA:RGD.
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:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006575; P:cellular modified amino acid metabolic process; IEA:InterPro.
DR GO; GO:0070189; P:kynurenine metabolic process; ISS:UniProtKB.
DR GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0097052; P:L-kynurenine metabolic process; IDA:RGD.
DR GO; GO:0006090; P:pyruvate metabolic process; IDA:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR034614; KAT_I.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43807:SF14; PTHR43807:SF14; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Aminotransferase; Cytoplasm;
KW Direct protein sequencing; Lyase; Mitochondrion; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT CHAIN 1..423
FT /note="Kynurenine--oxoglutarate transaminase 1"
FT /id="PRO_0000452095"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT MOD_RES 82
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTY1"
FT MOD_RES 247
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT VAR_SEQ 1
FT /note="M -> MFRSAAALSVHLMWPLWGRKAGASLTRCLHQSLTM (in isoform
FT 1)"
FT /id="VSP_060909"
FT CONFLICT 107
FT /note="R -> A (in Ref. 2; AAB32197 and 4; AAF06837)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="I -> V (in Ref. 2; AAB32197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 47873 MW; CEE7194633F96AA1 CRC64;
MTKRLQARRL DGIDQNLWVE FGKLTKEYDV VNLGQGFPDF SPPDFATQAF QQATSGNFML
NQYTRAFGYP PLTNVLASFF GKLLGQEMDP LTNVLVTVGA YGALFTRFQA LVDEGDEVII
MEPAFDCYEP MTMMAGGCPV FVTLKPSPAP KGKLGASNDW QLDPAELASK FTPRTKILVL
NTPNNPLGKV FSRMELELVA NLCQQHDVVC ISDEVYQWLV YDGHQHVSIA SLPGMWDRTL
TIGSAGKSFS ATGWKVGWVM GPDNIMKHLR TVHQNSIFHC PTQAQAAVAQ CFEREQQHFG
QPSSYFLQLP QAMELNRDHM IRSLQSVGLK LWISQGSYFL IADISDFKSK MPDLPGAEDE
PYDRRFAKWM IKNMGLVGIP VSTFFSRPHQ KDFDHYIRFC FVKDKATLQA MDERLRKWKE
LQP
