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Protein

Kynurenine--oxoglutarate transaminase 1, mitochondrial

Gene

Kyat1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.
L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine.
An L-cysteine-S-conjugate + H2O = RSH + NH3 + pyruvate.

Cofactori

Enzyme regulationi

Inhibited by aminooxyacetate (in vitro).1 Publication

Kineticsi

  1. KM=17 µM for L-kynurenine (with 2-oxoglutarate as cosubstrate)1 Publication
  2. KM=910 µM for L-kynurenine (with pyruvate as cosubstrate)1 Publication
  3. KM=150 µM for 2-oxoglutarate1 Publication
  4. KM=160 µM for pyruvate1 Publication

    pH dependencei

    Optimum pH is 9-9.5.1 Publication

    Pathwayi: L-kynurenine degradation

    This protein is involved in step 1 of the subpathway that synthesizes kynurenate from L-kynurenine.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Kynurenine--oxoglutarate transaminase 1, mitochondrial (Kyat1)
    2. no protein annotated in this organism
    This subpathway is part of the pathway L-kynurenine degradation, which is itself part of Amino-acid degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes kynurenate from L-kynurenine, the pathway L-kynurenine degradation and in Amino-acid degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei70 – 701Substrate; via amide nitrogenBy similarity
    Binding sitei219 – 2191SubstrateBy similarity
    Binding sitei432 – 4321SubstrateBy similarity

    GO - Molecular functioni

    GO - Biological processi

    • biosynthetic process Source: InterPro
    • kynurenine metabolic process Source: UniProtKB
    • L-kynurenine catabolic process Source: UniProtKB-UniPathway
    • L-kynurenine metabolic process Source: RGD
    • pyruvate metabolic process Source: RGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Lyase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BRENDAi2.6.1.7. 5301.
    UniPathwayiUPA00334; UER00726.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kynurenine--oxoglutarate transaminase 1, mitochondrial (EC:2.6.1.7)
    Short name:
    Kynurenine--oxoglutarate transaminase I
    Alternative name(s):
    Cysteine-S-conjugate beta-lyase (EC:4.4.1.13)
    Glutamine transaminase K
    Short name:
    GTK
    Glutamine--phenylpyruvate transaminase (EC:2.6.1.64)
    Kynurenine aminotransferase 1Imported
    Kynurenine aminotransferase I
    Short name:
    KATI
    Gene namesi
    Name:Kyat1Imported
    Synonyms:Ccbl1, Kat
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    Proteomesi
    • UP000002494 Componenti: Unplaced

    Organism-specific databases

    RGDi1306912. Kyat1.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: RGD
    • mitochondrial matrix Source: UniProtKB-SubCell
    • mitochondrion Source: RGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2828MitochondrionSequence analysisAdd
    BLAST
    Chaini29 – 457429Kynurenine--oxoglutarate transaminase 1, mitochondrialPRO_0000001221Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei116 – 1161N6-succinyllysineBy similarity
    Modified residuei281 – 2811N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PaxDbiQ08415.
    PRIDEiQ08415.

    PTM databases

    iPTMnetiQ08415.
    PhosphoSiteiQ08415.

    Expressioni

    Tissue specificityi

    Detected in kidney.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000021865.

    Structurei

    3D structure databases

    ProteinModelPortaliQ08415.
    SMRiQ08415. Positions 38-453.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG0257. Eukaryota.
    COG0436. LUCA.
    HOGENOMiHOG000223045.
    HOVERGENiHBG008391.
    InParanoidiQ08415.
    KOiK00816.
    PhylomeDBiQ08415.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q08415-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MFRSAAALSV HLMWPLWGRK AGASLTRCLH QSLTMTKRLQ ARRLDGIDQN
    60 70 80 90 100
    LWVEFGKLTK EYDVVNLGQG FPDFSPPDFA TQAFQQATSG NFMLNQYTRA
    110 120 130 140 150
    FGYPPLTNVL ASFFGKLLGQ EMDPLTNVLV TVGAYGALFT RFQALVDEGD
    160 170 180 190 200
    EVIIMEPAFD CYEPMTMMAG GCPVFVTLKP SPAPKGKLGA SNDWQLDPAE
    210 220 230 240 250
    LASKFTPRTK ILVLNTPNNP LGKVFSRMEL ELVANLCQQH DVVCISDEVY
    260 270 280 290 300
    QWLVYDGHQH VSIASLPGMW DRTLTIGSAG KSFSATGWKV GWVMGPDNIM
    310 320 330 340 350
    KHLRTVHQNS IFHCPTQAQA AVAQCFEREQ QHFGQPSSYF LQLPQAMELN
    360 370 380 390 400
    RDHMIRSLQS VGLKLWISQG SYFLIADISD FKSKMPDLPG AEDEPYDRRF
    410 420 430 440 450
    AKWMIKNMGL VGIPVSTFFS RPHQKDFDHY IRFCFVKDKA TLQAMDERLR

    KWKELQP
    Length:457
    Mass (Da):51,652
    Last modified:November 1, 1996 - v1
    Checksum:iE792A6BA2EA08502
    GO
    Isoform 2 (identifier: Q08415-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-34: Missing.

    Show »
    Length:423
    Mass (Da):47,873
    Checksum:iCEE7194633F96AA1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti141 – 1411R → A in AAB32197 (PubMed:7926014).Curated
    Sequence conflicti141 – 1411R → A in AAF06837 (PubMed:12850267).Curated
    Sequence conflicti211 – 2111I → V in AAB32197 (PubMed:7926014).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3434Missing in isoform 2. 2 PublicationsVSP_009878Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    S61960 mRNA. Translation: AAB26845.1.
    S74029 mRNA. Translation: AAB32197.1.
    Z49696 mRNA. Translation: CAA89696.1.
    AF100154 Genomic DNA. Translation: AAF06837.1.
    AF267749 mRNA. No translation available.
    PIRiS66270.
    RefSeqiNP_001013182.3. NM_001013164.3.
    UniGeneiRn.110564.

    Genome annotation databases

    GeneIDi311844.
    KEGGirno:311844.
    UCSCiRGD:1306912. rat. [Q08415-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    S61960 mRNA. Translation: AAB26845.1.
    S74029 mRNA. Translation: AAB32197.1.
    Z49696 mRNA. Translation: CAA89696.1.
    AF100154 Genomic DNA. Translation: AAF06837.1.
    AF267749 mRNA. No translation available.
    PIRiS66270.
    RefSeqiNP_001013182.3. NM_001013164.3.
    UniGeneiRn.110564.

    3D structure databases

    ProteinModelPortaliQ08415.
    SMRiQ08415. Positions 38-453.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000021865.

    PTM databases

    iPTMnetiQ08415.
    PhosphoSiteiQ08415.

    Proteomic databases

    PaxDbiQ08415.
    PRIDEiQ08415.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi311844.
    KEGGirno:311844.
    UCSCiRGD:1306912. rat. [Q08415-1]

    Organism-specific databases

    CTDi70266.
    RGDi1306912. Kyat1.

    Phylogenomic databases

    eggNOGiKOG0257. Eukaryota.
    COG0436. LUCA.
    HOGENOMiHOG000223045.
    HOVERGENiHBG008391.
    InParanoidiQ08415.
    KOiK00816.
    PhylomeDBiQ08415.

    Enzyme and pathway databases

    UniPathwayiUPA00334; UER00726.
    BRENDAi2.6.1.7. 5301.

    Miscellaneous databases

    PROiQ08415.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "Isolation and expression of a cDNA coding for rat kidney cytosolic cysteine conjugate beta-lyase."
      Perry S.J., Schofield M.A., MacFarlane M., Lock E.A., King L.J., Gibson G.G., Goldfarb P.S.
      Mol. Pharmacol. 43:660-665(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 39-62; 228-259 AND 388-401, TISSUE SPECIFICITY.
      Tissue: Kidney.
    2. "Molecular cloning of rat kynurenine aminotransferase: identity with glutamine transaminase K."
      Mosca M., Cozzi L., Breton J., Speciale C., Okuno E., Schwarcz R., Benatti L.
      FEBS Lett. 353:21-24(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "Identification of a mitochondrial form of kynurenine aminotransferase/glutamine transaminase K from rat brain."
      Malherbe P., Alberati-Giani D., Koehler C., Cesura A.M.
      FEBS Lett. 367:141-144(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Cerebellum.
    4. "Tissue expression and translational control of rat kynurenine aminotransferase/glutamine transaminase K mRNAs."
      Mosca M., Croci C., Mostardini M., Breton J., Malyszko J., Avanzi N., Toma S., Benatti L., Gatti S.
      Biochim. Biophys. Acta 1628:1-10(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    5. "Crystallization and characterization of human liver kynurenine--glyoxylate aminotransferase. Identity with alanine--glyoxylate aminotransferase and serine--pyruvate aminotransferase."
      Okuno E., Minatogawa Y., Nakamura M., Kamoda N., Nakanishi J., Makino M., Kido R.
      Biochem. J. 189:581-590(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT, PH DEPENDENCE.
    6. "Measurement of rat brain kynurenine aminotransferase at physiological kynurenine concentrations."
      Okuno E., Schmidt W., Parks D.A., Nakamura M., Schwarcz R.
      J. Neurochem. 57:533-540(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY AS KYNURENINE--OXOGLUTARATE TRANSAMINASE, KINETIC PARAMETERS, ENZYME REGULATION.

    Entry informationi

    Entry nameiKAT1_RAT
    AccessioniPrimary (citable) accession number: Q08415
    Secondary accession number(s): Q9R096
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: November 1, 1996
    Last modified: July 6, 2016
    This is version 113 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.