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Q64602 (AADAT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Aadat
Synonyms:Kat2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate.

Cofactor

Pyridoxal phosphate.

Pathway

Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 4/6.

Subunit structure

Homodimer. Ref.1

Subcellular location

Mitochondrion Potential.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion Potential
Chain30 – 425396Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
PRO_0000020604

Sites

Binding site201Substrate By similarity
Binding site741Substrate By similarity
Binding site1421Substrate By similarity
Binding site2021Substrate By similarity
Binding site3991Substrate By similarity

Amino acid modifications

Modified residue1721N6-succinyllysine By similarity
Modified residue1791N6-acetyllysine By similarity
Modified residue2631N6-(pyridoxal phosphate)lysine; alternate By similarity
Modified residue2631N6-acetyllysine; alternate By similarity
Modified residue2631N6-succinyllysine; alternate By similarity
Modified residue3391N6-acetyllysine; alternate By similarity
Modified residue3391N6-succinyllysine; alternate By similarity
Modified residue3511N6-acetyllysine By similarity
Modified residue3671N6-acetyllysine; alternate By similarity
Modified residue3671N6-succinyllysine; alternate By similarity
Modified residue4221N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64602 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: DDC33DBF21163564

FASTA42547,784
        10         20         30         40         50         60 
MNYSRFLTAT SLARKTSPIR ATVEIMSRAP KDIISLAPGS PNPKVFPFKS AVFTVENGST 

        70         80         90        100        110        120 
IRFEGEMFQR ALQYSSSYGI PELLSWLKQL QIKLHNPPTV NYSPNEGQMD LCITSGCQDG 

       130        140        150        160        170        180 
LCKVFEMLIN PGDTVLVNEP LYSGALFAMK PLGCNFISVP SDDCGIIPEG LKKVLSQWKP 

       190        200        210        220        230        240 
EDSKDPTKRT PKFLYTIPNG NNPTGNSLTG DRKKEIYELA RKYDFLIIED DPYYFLQFTK 

       250        260        270        280        290        300 
PWEPTFLSMD VDGRVIRADS LSKVISSGLR VGFITGPKSL IQRIVLHTQI SSLHPCTLSQ 

       310        320        330        340        350        360 
LMISELLYQW GEEGFLAHVD RAIDFYKNQR DFILAAADKW LRGLAEWHVP KAGMFLWIKV 

       370        380        390        400        410        420 
NGISDAKKLI EEKAIEREIL LVPGNSFFVD NSAPSSFFRA SFSQVTPAQM DLVFQRLAQL 


IKDVS 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z50144 mRNA. Translation: CAA90507.1.
BC078864 mRNA. Translation: AAH78864.1.
RefSeqNP_058889.1. NM_017193.1.
UniGeneRn.11133.

3D structure databases

ProteinModelPortalQ64602.
SMRQ64602. Positions 1-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4568866.
STRING10116.ENSRNOP00000015974.

Chemistry

BindingDBQ64602.
ChEMBLCHEMBL2662.

PTM databases

PhosphoSiteQ64602.

Proteomic databases

PaxDbQ64602.
PRIDEQ64602.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000015974; ENSRNOP00000015974; ENSRNOG00000011861.
GeneID29416.
KEGGrno:29416.
UCSCRGD:2948. rat.

Organism-specific databases

CTD51166.
RGD2948. Aadat.

Phylogenomic databases

eggNOGCOG1167.
GeneTreeENSGT00390000004594.
HOGENOMHOG000223057.
HOVERGENHBG050429.
InParanoidQ64602.
KOK00825.
OMANTFPFQS.
OrthoDBEOG7ZKSBF.
PhylomeDBQ64602.
TreeFamTF328598.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12251.
BRENDA2.6.1.7. 5301.
SABIO-RKQ64602.
UniPathwayUPA00868; UER00838.

Gene expression databases

GenevestigatorQ64602.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Other

NextBio609096.
PROQ64602.

Entry information

Entry nameAADAT_RAT
AccessionPrimary (citable) accession number: Q64602
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways