Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial precursor

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Q5E9N4 (AADAT_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 45. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial

Alternative name(s):
2-aminoadipate aminotransferase
2-aminoadipate transaminase
EC=2.6.1.39
Alpha-aminoadipate aminotransferase
Short name=AadAT
KAT/AadAT
EC=2.6.1.7
Kynurenine aminotransferase II
Kynurenine--oxoglutarate aminotransferase II
Kynurenine--oxoglutarate transaminase II

Gene names

Name:

AADAT

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	425 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 By similarity.
Pathway	Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 4/6.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion Potential.
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	2-oxoglutarate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB biosynthetic process Inferred from electronic annotation. Source: InterPro glutamate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB kynurenine metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2-aminoadipate transaminase activity Inferred from sequence or structural similarity. Source: UniProtKB kynurenine-oxoglutarate transaminase activity Inferred from sequence or structural similarity. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 29

Mitochondrion Potential

Chain

30 – 425

396

Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial

PRO_0000244427

Amino acid modifications

Modified residue

263

N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict

111

L → I in AAI09975. Ref.2

Sequence conflict

420

L → I in AAI09975. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q5E9N4 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 693F7529FC9AF666
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FASTA

425

47,901

        10         20         30         40         50         60 
MNYARFITAT SAARKPSTIR VMTEILSKAP KSVISLATGA PNPNTFPFKT AVITIENGKP 

        70         80         90        100        110        120 
IQFNEQMMKR ALQYSQSAGI PELLSWLKQL QVKLHNPPTI HYAPTQGQMD LCVTCGSQEG 

       130        140        150        160        170        180 
LCKVFEMIVN PGDNILVNEP IYSGTIHALQ PLGCNMINVS SDEHGIIPDS LREILSKWKP 

       190        200        210        220        230        240 
EDSKNPKKNS PKFLYTVPNG NNPSGNSLTA ERKREIYELA RKYDFLIIED DPYYFMQFNK 

       250        260        270        280        290        300 
PWAPTFLSMD EDGRVIRADS FSKVLSSGLR IGFITGPKPL IERIVLHIQV STMHPSTFAQ 

       310        320        330        340        350        360 
LLVSQLLYQW GEEGFLGHVD RVIDFYRKQR DALMAAADKW LSGLAEWHVP TAGMFLWVKI 

       370        380        390        400        410        420 
KGIHDVRKLI EEKAFKKEIF MLPGCGFYTD SSAPCPYFRA SFSSASPEQM DLAFQRLAQL 


IKESL

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References

[1]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BT020844 mRNA. Translation: AAX08861.1. BT020886 mRNA. Translation: AAX08903.1. BC109974 mRNA. Translation: AAI09975.1.
IPI	IPI00693391.
RefSeq	NP_001015551.1. NM_001015551.1.
UniGene	Bt.11485.
3D structure databases
ProteinModelPortal	Q5E9N4.
SMR	Q5E9N4. Positions 1-425.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5E9N4.
Proteomic databases
PRIDE	Q5E9N4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	508929.
KEGG	bta:508929.
Organism-specific databases
CTD	51166.
Phylogenomic databases
eggNOG	maNOG12559.
GeneTree	ENSGT00390000004594.
HOVERGEN	HBG050429.
InParanoid	Q5E9N4.
OrthoDB	EOG480HWQ.
PhylomeDB	Q5E9N4.
Family and domain databases
InterPro	IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KO	K00825.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AADAT_BOVIN

Accession

Primary (citable) accession number: Q5E9N4
Secondary accession number(s): Q32KQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	March 15, 2005
Last modified:	November 16, 2011
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents