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Q64602

- AADAT_RAT

UniProt

Q64602 - AADAT_RAT

Protein

Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial

Gene

Aadat

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro) By similarity.By similarity

    Catalytic activityi

    L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.
    L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate.

    Cofactori

    Pyridoxal phosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei20 – 201SubstrateBy similarity
    Binding sitei74 – 741SubstrateBy similarity
    Binding sitei142 – 1421SubstrateBy similarity
    Binding sitei202 – 2021SubstrateBy similarity
    Binding sitei399 – 3991SubstrateBy similarity

    GO - Molecular functioni

    1. 2-aminoadipate transaminase activity Source: UniProtKB
    2. kynurenine-oxoglutarate transaminase activity Source: UniProtKB
    3. pyridoxal phosphate binding Source: RGD
    4. transaminase activity Source: RGD

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: UniProtKB
    2. biosynthetic process Source: InterPro
    3. glutamate metabolic process Source: UniProtKB
    4. kynurenine metabolic process Source: UniProtKB
    5. L-kynurenine metabolic process Source: GOC
    6. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
    7. tryptophan catabolic process to kynurenine Source: RGD

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-12251.
    BRENDAi2.6.1.7. 5301.
    ReactomeiREACT_220761. Lysine catabolism.
    REACT_222206. Tryptophan catabolism.
    SABIO-RKQ64602.
    UniPathwayiUPA00868; UER00838.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
    Short name:
    KAT/AadAT
    Alternative name(s):
    2-aminoadipate aminotransferase
    2-aminoadipate transaminase (EC:2.6.1.39)
    Alpha-aminoadipate aminotransferase
    Short name:
    AadAT
    Kynurenine aminotransferase II
    Kynurenine--oxoglutarate aminotransferase II
    Kynurenine--oxoglutarate transaminase 2 (EC:2.6.1.7)
    Kynurenine--oxoglutarate transaminase II
    Gene namesi
    Name:Aadat
    Synonyms:Kat2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 16

    Organism-specific databases

    RGDi2948. Aadat.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: RGD

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2929MitochondrionSequence AnalysisAdd
    BLAST
    Chaini30 – 425396Kynurenine/alpha-aminoadipate aminotransferase, mitochondrialPRO_0000020604Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei172 – 1721N6-succinyllysineBy similarity
    Modified residuei179 – 1791N6-acetyllysineBy similarity
    Modified residuei263 – 2631N6-(pyridoxal phosphate)lysine; alternateBy similarity
    Modified residuei263 – 2631N6-acetyllysine; alternateBy similarity
    Modified residuei263 – 2631N6-succinyllysine; alternateBy similarity
    Modified residuei339 – 3391N6-acetyllysine; alternateBy similarity
    Modified residuei339 – 3391N6-succinyllysine; alternateBy similarity
    Modified residuei351 – 3511N6-acetyllysineBy similarity
    Modified residuei367 – 3671N6-acetyllysine; alternateBy similarity
    Modified residuei367 – 3671N6-succinyllysine; alternateBy similarity
    Modified residuei422 – 4221N6-acetyllysineBy similarity

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ64602.
    PRIDEiQ64602.

    PTM databases

    PhosphoSiteiQ64602.

    Expressioni

    Gene expression databases

    GenevestigatoriQ64602.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    MINTiMINT-4568866.
    STRINGi10116.ENSRNOP00000015974.

    Structurei

    3D structure databases

    ProteinModelPortaliQ64602.
    SMRiQ64602. Positions 1-423.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1167.
    GeneTreeiENSGT00390000004594.
    HOGENOMiHOG000223057.
    HOVERGENiHBG050429.
    InParanoidiQ64602.
    KOiK00825.
    OMAiKPLGCNI.
    OrthoDBiEOG7ZKSBF.
    PhylomeDBiQ64602.
    TreeFamiTF328598.

    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.

    Sequencei

    Sequence statusi: Complete.

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

    Q64602-1 [UniParc]FASTAAdd to Basket

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    MNYSRFLTAT SLARKTSPIR ATVEIMSRAP KDIISLAPGS PNPKVFPFKS    50
    AVFTVENGST IRFEGEMFQR ALQYSSSYGI PELLSWLKQL QIKLHNPPTV 100
    NYSPNEGQMD LCITSGCQDG LCKVFEMLIN PGDTVLVNEP LYSGALFAMK 150
    PLGCNFISVP SDDCGIIPEG LKKVLSQWKP EDSKDPTKRT PKFLYTIPNG 200
    NNPTGNSLTG DRKKEIYELA RKYDFLIIED DPYYFLQFTK PWEPTFLSMD 250
    VDGRVIRADS LSKVISSGLR VGFITGPKSL IQRIVLHTQI SSLHPCTLSQ 300
    LMISELLYQW GEEGFLAHVD RAIDFYKNQR DFILAAADKW LRGLAEWHVP 350
    KAGMFLWIKV NGISDAKKLI EEKAIEREIL LVPGNSFFVD NSAPSSFFRA 400
    SFSQVTPAQM DLVFQRLAQL IKDVS 425
    Length:425
    Mass (Da):47,784
    Last modified:November 1, 1996 - v1
    Checksum:iDDC33DBF21163564
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z50144 mRNA. Translation: CAA90507.1.
    BC078864 mRNA. Translation: AAH78864.1.
    RefSeqiNP_058889.1. NM_017193.1.
    UniGeneiRn.11133.

    Genome annotation databases

    EnsembliENSRNOT00000015974; ENSRNOP00000015974; ENSRNOG00000011861.
    GeneIDi29416.
    KEGGirno:29416.
    UCSCiRGD:2948. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z50144 mRNA. Translation: CAA90507.1 .
    BC078864 mRNA. Translation: AAH78864.1 .
    RefSeqi NP_058889.1. NM_017193.1.
    UniGenei Rn.11133.

    3D structure databases

    ProteinModelPortali Q64602.
    SMRi Q64602. Positions 1-423.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4568866.
    STRINGi 10116.ENSRNOP00000015974.

    Chemistry

    BindingDBi Q64602.
    ChEMBLi CHEMBL2662.

    PTM databases

    PhosphoSitei Q64602.

    Proteomic databases

    PaxDbi Q64602.
    PRIDEi Q64602.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000015974 ; ENSRNOP00000015974 ; ENSRNOG00000011861 .
    GeneIDi 29416.
    KEGGi rno:29416.
    UCSCi RGD:2948. rat.

    Organism-specific databases

    CTDi 51166.
    RGDi 2948. Aadat.

    Phylogenomic databases

    eggNOGi COG1167.
    GeneTreei ENSGT00390000004594.
    HOGENOMi HOG000223057.
    HOVERGENi HBG050429.
    InParanoidi Q64602.
    KOi K00825.
    OMAi KPLGCNI.
    OrthoDBi EOG7ZKSBF.
    PhylomeDBi Q64602.
    TreeFami TF328598.

    Enzyme and pathway databases

    UniPathwayi UPA00868 ; UER00838 .
    BioCyci MetaCyc:MONOMER-12251.
    BRENDAi 2.6.1.7. 5301.
    Reactomei REACT_220761. Lysine catabolism.
    REACT_222206. Tryptophan catabolism.
    SABIO-RK Q64602.

    Miscellaneous databases

    NextBioi 609096.
    PROi Q64602.

    Gene expression databases

    Genevestigatori Q64602.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR004839. Aminotransferase_I/II.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    Pfami PF00155. Aminotran_1_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and functional expression of a soluble form of kynurenine/alpha-aminoadipate aminotransferase from rat kidney."
      Buchli R., Alberati-Giani D., Malherbe P., Koehler C., Broger C., Cesura A.M.
      J. Biol. Chem. 270:29330-29335(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], HOMODIMERIZATION, PARTIAL PROTEIN SEQUENCE.
      Tissue: Kidney.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.

    Entry informationi

    Entry nameiAADAT_RAT
    AccessioniPrimary (citable) accession number: Q64602
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 106 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

    External Data

    Dasty 3