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Kynurenine--oxoglutarate transaminase 1, mitochondrial (Kynurenine--oxoglutarate transaminase I) (EC 2.6.1.7) (Cysteine-S-conjugate beta-lyase) (EC 4.4.1.13) (Glutamine transaminase K) (GTK) (Glutamine--phenylpyruvate transaminase) (EC 2.6.1.64) (Kynurenine aminotransferase 1) (Kynurenine aminotransferase I) (KATI)

 KAT1_RAT                Reviewed;         457 AA.
Q08415; Q9R096;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 121.
RecName: Full=Kynurenine--oxoglutarate transaminase 1, mitochondrial;
Short=Kynurenine--oxoglutarate transaminase I;
EC=2.6.1.7;
AltName: Full=Cysteine-S-conjugate beta-lyase;
EC=4.4.1.13;
AltName: Full=Glutamine transaminase K;
Short=GTK;
AltName: Full=Glutamine--phenylpyruvate transaminase;
EC=2.6.1.64;
AltName: Full=Kynurenine aminotransferase 1 {ECO:0000312|RGD:1306912};
AltName: Full=Kynurenine aminotransferase I;
Short=KATI;
Flags: Precursor;
Name=Kyat1 {ECO:0000312|RGD:1306912}; Synonyms=Ccbl1, Kat;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 39-62;
228-259 AND 388-401, AND TISSUE SPECIFICITY.
TISSUE=Kidney;
PubMed=8502223;
Perry S.J., Schofield M.A., MacFarlane M., Lock E.A., King L.J.,
Gibson G.G., Goldfarb P.S.;
"Isolation and expression of a cDNA coding for rat kidney cytosolic
cysteine conjugate beta-lyase.";
Mol. Pharmacol. 43:660-665(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=7926014; DOI=10.1016/0014-5793(94)01003-X;
Mosca M., Cozzi L., Breton J., Speciale C., Okuno E., Schwarcz R.,
Benatti L.;
"Molecular cloning of rat kynurenine aminotransferase: identity with
glutamine transaminase K.";
FEBS Lett. 353:21-24(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Cerebellum;
PubMed=7796908; DOI=10.1016/0014-5793(95)00546-L;
Malherbe P., Alberati-Giani D., Koehler C., Cesura A.M.;
"Identification of a mitochondrial form of kynurenine
aminotransferase/glutamine transaminase K from rat brain.";
FEBS Lett. 367:141-144(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
PubMed=12850267; DOI=10.1016/S0167-4781(03)00071-X;
Mosca M., Croci C., Mostardini M., Breton J., Malyszko J., Avanzi N.,
Toma S., Benatti L., Gatti S.;
"Tissue expression and translational control of rat kynurenine
aminotransferase/glutamine transaminase K mRNAs.";
Biochim. Biophys. Acta 1628:1-10(2003).
[5]
CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT, AND PH DEPENDENCE.
PubMed=6783036; DOI=10.1042/bj1890581;
Okuno E., Minatogawa Y., Nakamura M., Kamoda N., Nakanishi J.,
Makino M., Kido R.;
"Crystallization and characterization of human liver kynurenine-
glyoxylate aminotransferase. Identity with alanine-glyoxylate
aminotransferase and serine-pyruvate aminotransferase.";
Biochem. J. 189:581-590(1980).
[6]
CATALYTIC ACTIVITY AS KYNURENINE--OXOGLUTARATE TRANSAMINASE, KINETIC
PARAMETERS, AND ENZYME REGULATION.
PubMed=2072101; DOI=10.1111/j.1471-4159.1991.tb03783.x;
Okuno E., Schmidt W., Parks D.A., Nakamura M., Schwarcz R.;
"Measurement of rat brain kynurenine aminotransferase at physiological
kynurenine concentrations.";
J. Neurochem. 57:533-540(1991).
-!- FUNCTION: Catalyzes the irreversible transamination of the L-
tryptophan metabolite L-kynurenine to form kynurenic acid (KA).
Metabolizes the cysteine conjugates of certain halogenated alkenes
and alkanes to form reactive metabolites. Catalyzes the beta-
elimination of S-conjugates and Se-conjugates of L-
(seleno)cysteine, resulting in the cleavage of the C-S or C-Se
bond (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: L-kynurenine + 2-oxoglutarate = 4-(2-
aminophenyl)-2,4-dioxobutanoate + L-glutamate.
-!- CATALYTIC ACTIVITY: L-glutamine + phenylpyruvate = 2-
oxoglutaramate + L-phenylalanine.
-!- CATALYTIC ACTIVITY: An L-cysteine-S-conjugate + H(2)O = RSH +
NH(3) + pyruvate.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- ENZYME REGULATION: Inhibited by aminooxyacetate (in vitro).
{ECO:0000269|PubMed:2072101}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=17 uM for L-kynurenine (with 2-oxoglutarate as cosubstrate)
{ECO:0000269|PubMed:2072101};
KM=910 uM for L-kynurenine (with pyruvate as cosubstrate)
{ECO:0000269|PubMed:2072101};
KM=150 uM for 2-oxoglutarate {ECO:0000269|PubMed:2072101};
KM=160 uM for pyruvate {ECO:0000269|PubMed:2072101};
pH dependence:
Optimum pH is 9-9.5. {ECO:0000269|PubMed:6783036};
-!- PATHWAY: Amino-acid degradation; L-kynurenine degradation;
kynurenate from L-kynurenine: step 1/2.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:6783036}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q08415-1; Sequence=Displayed;
Name=2;
IsoId=Q08415-2; Sequence=VSP_009878;
-!- TISSUE SPECIFICITY: Detected in kidney.
{ECO:0000269|PubMed:8502223}.
-!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; S61960; AAB26845.1; -; mRNA.
EMBL; S74029; AAB32197.1; -; mRNA.
EMBL; Z49696; CAA89696.1; -; mRNA.
EMBL; AF100154; AAF06837.1; -; Genomic_DNA.
EMBL; AF267749; -; NOT_ANNOTATED_CDS; mRNA.
PIR; S66270; S66270.
RefSeq; NP_001013182.3; NM_001013164.3.
UniGene; Rn.110564; -.
ProteinModelPortal; Q08415; -.
SMR; Q08415; -.
STRING; 10116.ENSRNOP00000021865; -.
iPTMnet; Q08415; -.
PhosphoSitePlus; Q08415; -.
PaxDb; Q08415; -.
PRIDE; Q08415; -.
GeneID; 311844; -.
KEGG; rno:311844; -.
UCSC; RGD:1306912; rat. [Q08415-1]
CTD; 883; -.
RGD; 1306912; Kyat1.
eggNOG; KOG0257; Eukaryota.
eggNOG; COG0436; LUCA.
HOGENOM; HOG000223045; -.
HOVERGEN; HBG008391; -.
InParanoid; Q08415; -.
KO; K00816; -.
PhylomeDB; Q08415; -.
BRENDA; 2.6.1.7; 5301.
UniPathway; UPA00334; UER00726.
PRO; PR:Q08415; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IDA:RGD.
GO; GO:0047316; F:glutamine-phenylpyruvate transaminase activity; IDA:RGD.
GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; ISS:UniProtKB.
GO; GO:0047945; F:L-glutamine:pyruvate aminotransferase activity; ISO:RGD.
GO; GO:0047312; F:L-phenylalanine:pyruvate aminotransferase activity; ISO:RGD.
GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
GO; GO:0006575; P:cellular modified amino acid metabolic process; IEA:InterPro.
GO; GO:0070189; P:kynurenine metabolic process; ISS:UniProtKB.
GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0097052; P:L-kynurenine metabolic process; IDA:RGD.
GO; GO:0006090; P:pyruvate metabolic process; IDA:RGD.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR004839; Aminotransferase_I/II.
InterPro; IPR034614; KAT_I.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
PANTHER; PTHR43807:SF14; PTHR43807:SF14; 1.
Pfam; PF00155; Aminotran_1_2; 1.
SUPFAM; SSF53383; SSF53383; 1.
1: Evidence at protein level;
Alternative splicing; Aminotransferase; Complete proteome; Cytoplasm;
Direct protein sequencing; Lyase; Mitochondrion; Pyridoxal phosphate;
Reference proteome; Transferase; Transit peptide.
TRANSIT 1 28 Mitochondrion. {ECO:0000255}.
CHAIN 29 457 Kynurenine--oxoglutarate transaminase 1,
mitochondrial.
/FTId=PRO_0000001221.
BINDING 70 70 Substrate; via amide nitrogen.
{ECO:0000250}.
BINDING 219 219 Substrate. {ECO:0000250}.
BINDING 432 432 Substrate. {ECO:0000250}.
MOD_RES 116 116 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8BTY1}.
MOD_RES 281 281 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
VAR_SEQ 1 34 Missing (in isoform 2).
{ECO:0000303|PubMed:7926014,
ECO:0000303|PubMed:8502223}.
/FTId=VSP_009878.
CONFLICT 141 141 R -> A (in Ref. 2; AAB32197 and 4;
AAF06837). {ECO:0000305}.
CONFLICT 211 211 I -> V (in Ref. 2; AAB32197).
{ECO:0000305}.
SEQUENCE 457 AA; 51652 MW; E792A6BA2EA08502 CRC64;
MFRSAAALSV HLMWPLWGRK AGASLTRCLH QSLTMTKRLQ ARRLDGIDQN LWVEFGKLTK
EYDVVNLGQG FPDFSPPDFA TQAFQQATSG NFMLNQYTRA FGYPPLTNVL ASFFGKLLGQ
EMDPLTNVLV TVGAYGALFT RFQALVDEGD EVIIMEPAFD CYEPMTMMAG GCPVFVTLKP
SPAPKGKLGA SNDWQLDPAE LASKFTPRTK ILVLNTPNNP LGKVFSRMEL ELVANLCQQH
DVVCISDEVY QWLVYDGHQH VSIASLPGMW DRTLTIGSAG KSFSATGWKV GWVMGPDNIM
KHLRTVHQNS IFHCPTQAQA AVAQCFEREQ QHFGQPSSYF LQLPQAMELN RDHMIRSLQS
VGLKLWISQG SYFLIADISD FKSKMPDLPG AEDEPYDRRF AKWMIKNMGL VGIPVSTFFS
RPHQKDFDHY IRFCFVKDKA TLQAMDERLR KWKELQP


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