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Protein

Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial

Gene

Aadat

Organism
Rattus norvegicus (Rat)
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) (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

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 sitei20SubstrateBy similarity1
Binding sitei74SubstrateBy similarity1
Binding sitei142SubstrateBy similarity1
Binding sitei202SubstrateBy similarity1
Binding sitei399SubstrateBy similarity1

GO - Molecular functioni

  • 2-aminoadipate transaminase activity Source: UniProtKB
  • kynurenine-oxoglutarate transaminase activity Source: UniProtKB
  • pyridoxal phosphate binding Source: RGD
  • transaminase activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12251.
BRENDAi2.6.1.39. 5301.
2.6.1.7. 5301.
ReactomeiR-RNO-71064. Lysine catabolism.
R-RNO-71240. 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
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi2948. Aadat.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2662.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 29MitochondrionSequence analysisAdd BLAST29
ChainiPRO_000002060430 – 425Kynurenine/alpha-aminoadipate aminotransferase, mitochondrialAdd BLAST396

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40PhosphoserineCombined sources1
Modified residuei172N6-succinyllysineBy similarity1
Modified residuei179N6-acetyllysineBy similarity1
Modified residuei263N6-(pyridoxal phosphate)lysine; alternateBy similarity1
Modified residuei263N6-acetyllysine; alternateBy similarity1
Modified residuei263N6-succinyllysine; alternateBy similarity1
Modified residuei339N6-acetyllysine; alternateBy similarity1
Modified residuei339N6-succinyllysine; alternateBy similarity1
Modified residuei351N6-acetyllysineBy similarity1
Modified residuei367N6-acetyllysine; alternateBy similarity1
Modified residuei367N6-succinyllysine; alternateBy similarity1
Modified residuei422N6-acetyllysineBy similarity1

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ64602.
PRIDEiQ64602.

PTM databases

iPTMnetiQ64602.
PhosphoSitePlusiQ64602.

Expressioni

Gene expression databases

BgeeiENSRNOG00000011861.
ExpressionAtlasiQ64602. baseline and differential.
GenevisibleiQ64602. RN.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

MINTiMINT-4568866.
STRINGi10116.ENSRNOP00000015974.

Chemistry databases

BindingDBiQ64602.

Structurei

3D structure databases

ProteinModelPortaliQ64602.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0634. Eukaryota.
COG1167. LUCA.
GeneTreeiENSGT00390000004594.
HOGENOMiHOG000223057.
HOVERGENiHBG050429.
InParanoidiQ64602.
KOiK00825.
OMAiWMKNLQK.
OrthoDBiEOG091G0B8J.
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

« Hide

        10         20         30         40         50
MNYSRFLTAT SLARKTSPIR ATVEIMSRAP KDIISLAPGS PNPKVFPFKS
60 70 80 90 100
AVFTVENGST IRFEGEMFQR ALQYSSSYGI PELLSWLKQL QIKLHNPPTV
110 120 130 140 150
NYSPNEGQMD LCITSGCQDG LCKVFEMLIN PGDTVLVNEP LYSGALFAMK
160 170 180 190 200
PLGCNFISVP SDDCGIIPEG LKKVLSQWKP EDSKDPTKRT PKFLYTIPNG
210 220 230 240 250
NNPTGNSLTG DRKKEIYELA RKYDFLIIED DPYYFLQFTK PWEPTFLSMD
260 270 280 290 300
VDGRVIRADS LSKVISSGLR VGFITGPKSL IQRIVLHTQI SSLHPCTLSQ
310 320 330 340 350
LMISELLYQW GEEGFLAHVD RAIDFYKNQR DFILAAADKW LRGLAEWHVP
360 370 380 390 400
KAGMFLWIKV NGISDAKKLI EEKAIEREIL LVPGNSFFVD NSAPSSFFRA
410 420
SFSQVTPAQM DLVFQRLAQL IKDVS
Length:425
Mass (Da):47,784
Last modified:November 1, 1996 - v1
Checksum:iDDC33DBF21163564
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
Z50144 mRNA. Translation: CAA90507.1.
BC078864 mRNA. Translation: AAH78864.1.
RefSeqiNP_058889.1. NM_017193.1.
UniGeneiRn.11133.

3D structure databases

ProteinModelPortaliQ64602.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4568866.
STRINGi10116.ENSRNOP00000015974.

Chemistry databases

BindingDBiQ64602.
ChEMBLiCHEMBL2662.

PTM databases

iPTMnetiQ64602.
PhosphoSitePlusiQ64602.

Proteomic databases

PaxDbiQ64602.
PRIDEiQ64602.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51166.
RGDi2948. Aadat.

Phylogenomic databases

eggNOGiKOG0634. Eukaryota.
COG1167. LUCA.
GeneTreeiENSGT00390000004594.
HOGENOMiHOG000223057.
HOVERGENiHBG050429.
InParanoidiQ64602.
KOiK00825.
OMAiWMKNLQK.
OrthoDBiEOG091G0B8J.
PhylomeDBiQ64602.
TreeFamiTF328598.

Enzyme and pathway databases

UniPathwayiUPA00868; UER00838.
BioCyciMetaCyc:MONOMER-12251.
BRENDAi2.6.1.39. 5301.
2.6.1.7. 5301.
ReactomeiR-RNO-71064. Lysine catabolism.
R-RNO-71240. Tryptophan catabolism.
SABIO-RKQ64602.

Miscellaneous databases

PROiQ64602.

Gene expression databases

BgeeiENSRNOG00000011861.
ExpressionAtlasiQ64602. baseline and differential.
GenevisibleiQ64602. RN.

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_RAT
AccessioniPrimary (citable) accession number: Q64602
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 122 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.