Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial

Gene

AADAT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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).1 Publication

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 5'-phosphate3 Publications

Enzyme regulationi

Kynurenine transaminase activity is competitively inhibited by aminoadipate, asparagine, glutamate, histidine, cysteine, lysine, 3-hydroxy-kynurenine and phenylalanine.1 Publication

Kineticsi

  1. KM=0.9 mM for aminoadipate1 Publication
  2. KM=4.7 mM for kynurenine1 Publication
  3. KM=1.7 mM for methionine1 Publication
  4. KM=1.6 mM for glutamate1 Publication
  5. KM=1.8 mM for tyrosine1 Publication
  6. KM=1.2 mM for 2-oxoglutarate1 Publication
  7. KM=1.5 mM for 2-oxocaproic acid1 Publication
  8. KM=1.8 mM for phenylpyruvate1 Publication
  9. KM=1.4 mM for ino-3-pyruvate1 Publication

    pH dependencei

    Optimum pH is 7-9.1 Publication

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius.1 Publication

    Pathwayi: L-lysine degradation via saccharopine pathway

    This protein is involved in step 4 of the subpathway that synthesizes glutaryl-CoA from L-lysine.
    Proteins known to be involved in the 6 steps of the subpathway in this organism are:
    1. Alpha-aminoadipic semialdehyde synthase, mitochondrial (AASS)
    2. Alpha-aminoadipic semialdehyde synthase, mitochondrial (AASS)
    3. no protein annotated in this organism
    4. Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (AADAT)
    5. no protein annotated in this organism
    6. Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (DLST)
    This subpathway is part of the pathway L-lysine degradation via saccharopine pathway, 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 glutaryl-CoA from L-lysine, the pathway L-lysine degradation via saccharopine pathway and in Amino-acid degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei20Substrate1
    Binding sitei74Substrate1
    Binding sitei142Substrate1
    Binding sitei202Substrate1
    Binding sitei399Substrate1

    GO - Molecular functioni

    • 2-aminoadipate transaminase activity Source: UniProtKB
    • kynurenine-oxoglutarate transaminase activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    • pyridoxal phosphate binding Source: Ensembl

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03239-MONOMER.
    ZFISH:HS03239-MONOMER.
    BRENDAi2.6.1.39. 2681.
    2.6.1.7. 2681.
    ReactomeiR-HSA-71064. Lysine catabolism.
    R-HSA-71240. Tryptophan catabolism.
    SABIO-RKQ8N5Z0.
    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:17929. AADAT.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    OpenTargetsiENSG00000109576.
    PharmGKBiPA24364.

    Chemistry databases

    ChEMBLiCHEMBL2046259.

    Polymorphism and mutation databases

    BioMutaiAADAT.
    DMDMi46395904.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 29MitochondrionSequence analysisAdd BLAST29
    ChainiPRO_000002060230 – 425Kynurenine/alpha-aminoadipate aminotransferase, mitochondrialAdd BLAST396

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei69N6-acetyllysineBy similarity1
    Modified residuei179N6-acetyllysineBy similarity1
    Modified residuei263N6-(pyridoxal phosphate)lysine; alternate1
    Modified residuei263N6-acetyllysine; alternateBy similarity1
    Modified residuei263N6-succinyllysine; alternateBy similarity1
    Modified residuei339N6-acetyllysine; alternateBy similarity1
    Modified residuei339N6-succinyllysine; alternateBy similarity1
    Modified residuei367N6-acetyllysine; alternateBy similarity1
    Modified residuei367N6-succinyllysine; alternateBy similarity1
    Modified residuei422N6-acetyllysineBy similarity1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiQ8N5Z0.
    MaxQBiQ8N5Z0.
    PaxDbiQ8N5Z0.
    PeptideAtlasiQ8N5Z0.
    PRIDEiQ8N5Z0.

    PTM databases

    iPTMnetiQ8N5Z0.
    PhosphoSitePlusiQ8N5Z0.

    Expressioni

    Tissue specificityi

    Higher expression in the liver. Also found in heart, brain, kidney, pancreas, prostate, testis and ovary.

    Gene expression databases

    BgeeiENSG00000109576.
    CleanExiHS_AADAT.
    ExpressionAtlasiQ8N5Z0. baseline and differential.
    GenevisibleiQ8N5Z0. HS.

    Organism-specific databases

    HPAiHPA037502.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    BioGridi119346. 1 interactor.
    STRINGi9606.ENSP00000226840.

    Chemistry databases

    BindingDBiQ8N5Z0.

    Structurei

    Secondary structure

    1425
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 6Combined sources4
    Helixi9 – 13Combined sources5
    Helixi19 – 21Combined sources3
    Beta strandi23 – 25Combined sources3
    Turni26 – 28Combined sources3
    Helixi43 – 45Combined sources3
    Beta strandi51 – 53Combined sources3
    Turni56 – 58Combined sources3
    Beta strandi61 – 63Combined sources3
    Helixi65 – 71Combined sources7
    Helixi81 – 95Combined sources15
    Turni98 – 101Combined sources4
    Helixi104 – 106Combined sources3
    Beta strandi109 – 116Combined sources8
    Helixi117 – 128Combined sources12
    Beta strandi134 – 137Combined sources4
    Helixi143 – 149Combined sources7
    Helixi150 – 152Combined sources3
    Beta strandi155 – 158Combined sources4
    Helixi168 – 175Combined sources8
    Helixi180 – 184Combined sources5
    Helixi186 – 188Combined sources3
    Beta strandi193 – 196Combined sources4
    Turni202 – 204Combined sources3
    Helixi210 – 222Combined sources13
    Beta strandi226 – 230Combined sources5
    Turni232 – 235Combined sources4
    Beta strandi239 – 241Combined sources3
    Helixi247 – 249Combined sources3
    Beta strandi251 – 253Combined sources3
    Beta strandi255 – 260Combined sources6
    Turni262 – 265Combined sources4
    Turni267 – 270Combined sources4
    Beta strandi272 – 277Combined sources6
    Helixi278 – 289Combined sources12
    Turni290 – 292Combined sources3
    Beta strandi293 – 295Combined sources3
    Helixi297 – 340Combined sources44
    Beta strandi342 – 347Combined sources6
    Beta strandi351 – 360Combined sources10
    Helixi367 – 371Combined sources5
    Helixi373 – 376Combined sources4
    Beta strandi381 – 383Combined sources3
    Helixi384 – 387Combined sources4
    Beta strandi388 – 390Combined sources3
    Beta strandi391 – 393Combined sources3
    Beta strandi397 – 401Combined sources5
    Turni402 – 404Combined sources3
    Helixi407 – 424Combined sources18

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2QLRX-ray2.30A/B/C/D1-425[»]
    2R2NX-ray1.95A/B/C/D1-425[»]
    2VGZX-ray2.30A/B2-425[»]
    2XH1X-ray2.10A/B1-425[»]
    3DC1X-ray2.50A/B/C/D1-425[»]
    3UE8X-ray3.22A/B1-425[»]
    4GDYX-ray2.89A/B1-425[»]
    4GE4X-ray2.41A/B1-425[»]
    4GE7X-ray2.10A/B1-425[»]
    4GE9X-ray2.43A/B/C/D1-425[»]
    4GEBX-ray2.15A/B1-425[»]
    5EFSX-ray1.83A1-425[»]
    5EUNX-ray1.82A1-425[»]
    5TF5X-ray1.81A/B1-425[»]
    ProteinModelPortaliQ8N5Z0.
    SMRiQ8N5Z0.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8N5Z0.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG0634. Eukaryota.
    COG1167. LUCA.
    GeneTreeiENSGT00390000004594.
    HOGENOMiHOG000223057.
    HOVERGENiHBG050429.
    InParanoidiQ8N5Z0.
    KOiK00825.
    OMAiQQWGEKG.
    OrthoDBiEOG091G0B8J.
    PhylomeDBiQ8N5Z0.
    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.

    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: Q8N5Z0-1) [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
    MNYARFITAA SAARNPSPIR TMTDILSRGP KSMISLAGGL PNPNMFPFKT
    60 70 80 90 100
    AVITVENGKT IQFGEEMMKR ALQYSPSAGI PELLSWLKQL QIKLHNPPTI
    110 120 130 140 150
    HYPPSQGQMD LCVTSGSQQG LCKVFEMIIN PGDNVLLDEP AYSGTLQSLH
    160 170 180 190 200
    PLGCNIINVA SDESGIVPDS LRDILSRWKP EDAKNPQKNT PKFLYTVPNG
    210 220 230 240 250
    NNPTGNSLTS ERKKEIYELA RKYDFLIIED DPYYFLQFNK FRVPTFLSMD
    260 270 280 290 300
    VDGRVIRADS FSKIISSGLR IGFLTGPKPL IERVILHIQV STLHPSTFNQ
    310 320 330 340 350
    LMISQLLHEW GEEGFMAHVD RVIDFYSNQK DAILAAADKW LTGLAEWHVP
    360 370 380 390 400
    AAGMFLWIKV KGINDVKELI EEKAVKMGVL MLPGNAFYVD SSAPSPYLRA
    410 420
    SFSSASPEQM DVAFQVLAQL IKESL
    Note: May be due to a competing donor splice site.
    Length:425
    Mass (Da):47,352
    Last modified:April 13, 2004 - v2
    Checksum:i448CCAAB2173A7BA
    GO
    Isoform 2 (identifier: Q8N5Z0-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         23-23: T → SEKRA

    Show »
    Length:429
    Mass (Da):47,822
    Checksum:i0C5A6E51F1BD6F53
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti103P → Q in AAH31068 (PubMed:15489334).Curated1
    Sequence conflicti380L → S in BAG51596 (PubMed:14702039).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_061005243V → I.Corresponds to variant rs56350236dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_00987423T → SEKRA in isoform 2. 1 Publication1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF097994 mRNA. Translation: AAF04623.1.
    AF481738 mRNA. Translation: AAM09683.1.
    AK055952 mRNA. Translation: BAG51596.1.
    BC031068 mRNA. Translation: AAH31068.1.
    CCDSiCCDS3814.1. [Q8N5Z0-1]
    CCDS75209.1. [Q8N5Z0-2]
    RefSeqiNP_001273611.1. NM_001286682.1. [Q8N5Z0-2]
    NP_001273612.1. NM_001286683.1. [Q8N5Z0-1]
    NP_057312.1. NM_016228.3. [Q8N5Z0-1]
    NP_872603.1. NM_182662.1. [Q8N5Z0-1]
    UniGeneiHs.529735.

    Genome annotation databases

    EnsembliENST00000337664; ENSP00000336808; ENSG00000109576. [Q8N5Z0-1]
    ENST00000353187; ENSP00000226840; ENSG00000109576. [Q8N5Z0-1]
    ENST00000509167; ENSP00000423190; ENSG00000109576. [Q8N5Z0-2]
    ENST00000515480; ENSP00000423341; ENSG00000109576. [Q8N5Z0-1]
    GeneIDi51166.
    KEGGihsa:51166.
    UCSCiuc003isr.4. human. [Q8N5Z0-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF097994 mRNA. Translation: AAF04623.1.
    AF481738 mRNA. Translation: AAM09683.1.
    AK055952 mRNA. Translation: BAG51596.1.
    BC031068 mRNA. Translation: AAH31068.1.
    CCDSiCCDS3814.1. [Q8N5Z0-1]
    CCDS75209.1. [Q8N5Z0-2]
    RefSeqiNP_001273611.1. NM_001286682.1. [Q8N5Z0-2]
    NP_001273612.1. NM_001286683.1. [Q8N5Z0-1]
    NP_057312.1. NM_016228.3. [Q8N5Z0-1]
    NP_872603.1. NM_182662.1. [Q8N5Z0-1]
    UniGeneiHs.529735.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2QLRX-ray2.30A/B/C/D1-425[»]
    2R2NX-ray1.95A/B/C/D1-425[»]
    2VGZX-ray2.30A/B2-425[»]
    2XH1X-ray2.10A/B1-425[»]
    3DC1X-ray2.50A/B/C/D1-425[»]
    3UE8X-ray3.22A/B1-425[»]
    4GDYX-ray2.89A/B1-425[»]
    4GE4X-ray2.41A/B1-425[»]
    4GE7X-ray2.10A/B1-425[»]
    4GE9X-ray2.43A/B/C/D1-425[»]
    4GEBX-ray2.15A/B1-425[»]
    5EFSX-ray1.83A1-425[»]
    5EUNX-ray1.82A1-425[»]
    5TF5X-ray1.81A/B1-425[»]
    ProteinModelPortaliQ8N5Z0.
    SMRiQ8N5Z0.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi119346. 1 interactor.
    STRINGi9606.ENSP00000226840.

    Chemistry databases

    BindingDBiQ8N5Z0.
    ChEMBLiCHEMBL2046259.

    PTM databases

    iPTMnetiQ8N5Z0.
    PhosphoSitePlusiQ8N5Z0.

    Polymorphism and mutation databases

    BioMutaiAADAT.
    DMDMi46395904.

    Proteomic databases

    EPDiQ8N5Z0.
    MaxQBiQ8N5Z0.
    PaxDbiQ8N5Z0.
    PeptideAtlasiQ8N5Z0.
    PRIDEiQ8N5Z0.

    Protocols and materials databases

    DNASUi51166.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000337664; ENSP00000336808; ENSG00000109576. [Q8N5Z0-1]
    ENST00000353187; ENSP00000226840; ENSG00000109576. [Q8N5Z0-1]
    ENST00000509167; ENSP00000423190; ENSG00000109576. [Q8N5Z0-2]
    ENST00000515480; ENSP00000423341; ENSG00000109576. [Q8N5Z0-1]
    GeneIDi51166.
    KEGGihsa:51166.
    UCSCiuc003isr.4. human. [Q8N5Z0-1]

    Organism-specific databases

    CTDi51166.
    GeneCardsiAADAT.
    HGNCiHGNC:17929. AADAT.
    HPAiHPA037502.
    MIMi611754. gene.
    neXtProtiNX_Q8N5Z0.
    OpenTargetsiENSG00000109576.
    PharmGKBiPA24364.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0634. Eukaryota.
    COG1167. LUCA.
    GeneTreeiENSGT00390000004594.
    HOGENOMiHOG000223057.
    HOVERGENiHBG050429.
    InParanoidiQ8N5Z0.
    KOiK00825.
    OMAiQQWGEKG.
    OrthoDBiEOG091G0B8J.
    PhylomeDBiQ8N5Z0.
    TreeFamiTF328598.

    Enzyme and pathway databases

    UniPathwayiUPA00868; UER00838.
    BioCyciMetaCyc:HS03239-MONOMER.
    ZFISH:HS03239-MONOMER.
    BRENDAi2.6.1.39. 2681.
    2.6.1.7. 2681.
    ReactomeiR-HSA-71064. Lysine catabolism.
    R-HSA-71240. Tryptophan catabolism.
    SABIO-RKQ8N5Z0.

    Miscellaneous databases

    ChiTaRSiAADAT. human.
    EvolutionaryTraceiQ8N5Z0.
    GenomeRNAii51166.
    PROiQ8N5Z0.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000109576.
    CleanExiHS_AADAT.
    ExpressionAtlasiQ8N5Z0. baseline and differential.
    GenevisibleiQ8N5Z0. HS.

    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...

    Entry informationi

    Entry nameiAADAT_HUMAN
    AccessioniPrimary (citable) accession number: Q8N5Z0
    Secondary accession number(s): B3KP84, Q9UL02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: April 13, 2004
    Last modified: November 30, 2016
    This is version 135 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. 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.