Reviewed, UniProtKB/Swiss-Prot Q5E9N4 (AADAT_BOVIN)

Names and origin

Protein names

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

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	Shows activity also towards tryptophan, aspartate and hydroxykinurenine 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
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2-aminoadipate transaminase activity Inferred from electronic annotation. Source: EC kynurenine-oxoglutarate transaminase activity Inferred from electronic annotation. Source: EC 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	29	Mitochondrion Potential
	Chain	30 – 425	396	Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial		PRO_0000244427
Amino acid modifications
	Modified residue	263	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	111	1	L → I in AAI09975. Ref.2
	Sequence conflict	420	1	L → I in AAI09975. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q5E9N4-1 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 693F7529FC9AF666	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

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.
UniGene	Bt.11485
3D structure databases
SMR	Q5E9N4. Positions 1-425.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5E9N4.
Genome annotation databases
Ensembl	ENSBTAT00000013637; ENSBTAP00000013637; ENSBTAG00000010326; Bos taurus. [Genome view]
GeneID	508929.
KEGG	bta:508929.
Organism-specific databases
CTD	508929.
Phylogenomic databases
eggNOG	maNOG12559.
HOVERGEN	Q5E9N4.
InParanoid	Q5E9N4.
PhylomeDB	Q5E9N4.
Enzyme and pathway databases
BRENDA	2.6.1.39. 251. 2.6.1.7. 251.
Family and domain databases
InterPro	IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
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:	January 19, 2010
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)