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Protein

Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial

Gene

AADAT

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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)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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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_0000244427Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei69 – 691N6-acetyllysineBy 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 residuei422 – 4221N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ5E9N4.
PRIDEiQ5E9N4.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000013637.

Structurei

3D structure databases

ProteinModelPortaliQ5E9N4.
SMRiQ5E9N4. Positions 1-425.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0634. Eukaryota.
COG1167. LUCA.
HOGENOMiHOG000223057.
HOVERGENiHBG050429.
InParanoidiQ5E9N4.
KOiK00825.

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.

Q5E9N4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNYARFITAT SAARKPSTIR VMTEILSKAP KSVISLATGA PNPNTFPFKT
60 70 80 90 100
AVITIENGKP IQFNEQMMKR ALQYSQSAGI PELLSWLKQL QVKLHNPPTI
110 120 130 140 150
HYAPTQGQMD LCVTCGSQEG LCKVFEMIVN PGDNILVNEP IYSGTIHALQ
160 170 180 190 200
PLGCNMINVS SDEHGIIPDS LREILSKWKP EDSKNPKKNS PKFLYTVPNG
210 220 230 240 250
NNPSGNSLTA ERKREIYELA RKYDFLIIED DPYYFMQFNK PWAPTFLSMD
260 270 280 290 300
EDGRVIRADS FSKVLSSGLR IGFITGPKPL IERIVLHIQV STMHPSTFAQ
310 320 330 340 350
LLVSQLLYQW GEEGFLGHVD RVIDFYRKQR DALMAAADKW LSGLAEWHVP
360 370 380 390 400
TAGMFLWVKI KGIHDVRKLI EEKAFKKEIF MLPGCGFYTD SSAPCPYFRA
410 420
SFSSASPEQM DLAFQRLAQL IKESL
Length:425
Mass (Da):47,901
Last modified:March 15, 2005 - v1
Checksum:i693F7529FC9AF666
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111L → I in AAI09975 (Ref. 2) Curated
Sequence conflicti420 – 4201L → I in AAI09975 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020844 mRNA. Translation: AAX08861.1.
BT020886 mRNA. Translation: AAX08903.1.
BC109974 mRNA. Translation: AAI09975.1.
RefSeqiNP_001015551.1. NM_001015551.1.
UniGeneiBt.11485.

Genome annotation databases

GeneIDi508929.
KEGGibta:508929.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020844 mRNA. Translation: AAX08861.1.
BT020886 mRNA. Translation: AAX08903.1.
BC109974 mRNA. Translation: AAI09975.1.
RefSeqiNP_001015551.1. NM_001015551.1.
UniGeneiBt.11485.

3D structure databases

ProteinModelPortaliQ5E9N4.
SMRiQ5E9N4. Positions 1-425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000013637.

Proteomic databases

PaxDbiQ5E9N4.
PRIDEiQ5E9N4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi508929.
KEGGibta:508929.

Organism-specific databases

CTDi51166.

Phylogenomic databases

eggNOGiKOG0634. Eukaryota.
COG1167. LUCA.
HOGENOMiHOG000223057.
HOVERGENiHBG050429.
InParanoidiQ5E9N4.
KOiK00825.

Enzyme and pathway databases

UniPathwayiUPA00868; UER00838.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Liver.

Entry informationi

Entry nameiAADAT_BOVIN
AccessioniPrimary (citable) accession number: Q5E9N4
Secondary accession number(s): Q32KQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 15, 2005
Last modified: June 8, 2016
This is version 71 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, 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.