Kynurenine/alpha-aminoadipate aminotransferase mitochondrial precursor

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Reviewed, UniProtKB/Swiss-Prot Q8N5Z0 (AADAT_HUMAN)

Last modified July 22, 2008. Version 47. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
Synonyms:	KAT2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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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 protein level.

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General annotation (Comments)

Function	Shows activity also towards tryptophan, aspartate and hydroxykinurenine.
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 By similarity.
Subcellular location	MitochondrionPotential.
Tissue specificity	Higher expression in the liver. Also found in heart, brain, kidney, pancreas, prostate, testis and ovary.
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

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Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Multifunctional enzyme
Gene Ontology (GO)
Cellular component	cytosol Ref.2 Inferred from Experiment. Source: Reactome
Molecular function	kynurenine-oxoglutarate transaminase activity Ref.2 Inferred from Experiment. Source: Reactome
Complete GO annotation...

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8N5Z0-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Notes: May be due to a competing donnor splice site.

Isoform 2 (identifier: Q8N5Z0-2) The sequence of this isoform differs from the canonical sequence as follows: 23-23: T → SEKRA

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Transit peptide

1 – 29

Mitochondrion Potential

Chain

30 – 425

396

Kynurenine/alpha-aminoadipate aminotransferase mitochondrial

Sites

Binding site

263

Pyridoxal phosphate (covalent) By similarity

Natural variations

Alternative sequence

T → SEKRA in isoform 2.

Experimental info

Sequence conflict

103

P → Q in AAH31068. Ref.4

Sequence conflict

380

L → S Ref.3

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Sequences

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified April 13, 2004. Version 2. Checksum: 448CCAAB2173A7BA Show »	FASTA	425	47,352
10 20 30 40 50 60 MNYARFITAA SAARNPSPIR TMTDILSRGP KSMISLAGGL PNPNMFPFKT AVITVENGKT 70 80 90 100 110 120 IQFGEEMMKR ALQYSPSAGI PELLSWLKQL QIKLHNPPTI HYPPSQGQMD LCVTSGSQQG 130 140 150 160 170 180 LCKVFEMIIN PGDNVLLDEP AYSGTLQSLH PLGCNIINVA SDESGIVPDS LRDILSRWKP 190 200 210 220 230 240 EDAKNPQKNT PKFLYTVPNG NNPTGNSLTS ERKKEIYELA RKYDFLIIED DPYYFLQFNK 250 260 270 280 290 300 FRVPTFLSMD VDGRVIRADS FSKIISSGLR IGFLTGPKPL IERVILHIQV STLHPSTFNQ 310 320 330 340 350 360 LMISQLLHEW GEEGFMAHVD RVIDFYSNQK DAILAAADKW LTGLAEWHVP AAGMFLWIKV 370 380 390 400 410 420 KGINDVKELI EEKAVKMGVL MLPGNAFYVD SSAPSPYLRA SFSSASPEQM DVAFQVLAQL IKESL « Hide
Isoform 2 [UniParc]. Checksum: 0C5A6E51F1BD6F53 Show »		429	47,822
10 20 30 40 50 60 MNYARFITAA SAARNPSPIR TMSEKRADIL SRGPKSMISL AGGLPNPNMF PFKTAVITVE 70 80 90 100 110 120 NGKTIQFGEE MMKRALQYSP SAGIPELLSW LKQLQIKLHN PPTIHYPPSQ GQMDLCVTSG 130 140 150 160 170 180 SQQGLCKVFE MIINPGDNVL LDEPAYSGTL QSLHPLGCNI INVASDESGI VPDSLRDILS 190 200 210 220 230 240 RWKPEDAKNP QKNTPKFLYT VPNGNNPTGN SLTSERKKEI YELARKYDFL IIEDDPYYFL 250 260 270 280 290 300 QFNKFRVPTF LSMDVDGRVI RADSFSKIIS SGLRIGFLTG PKPLIERVIL HIQVSTLHPS 310 320 330 340 350 360 TFNQLMISQL LHEWGEEGFM AHVDRVIDFY SNQKDAILAA ADKWLTGLAE WHVPAAGMFL 370 380 390 400 410 420 WIKVKGINDV KELIEEKAVK MGVLMLPGNA FYVDSSAPSP YLRASFSSAS PEQMDVAFQV LAQLIKESL « Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of human L-kynurenine/alpha-aminoadipate aminotransferase cDNA from brain tissue." Gatti S., Breton J., Mostardini M., Mosca M., Tarroni P., Schwarcz R., Speciale C., Okuno E., Toma S., Benatti L. Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"Characterization of the human gene encoding alpha-aminoadipate aminotransferase (AADAT)." Goh D.L.M., Patel A., Thomas G.H., Salomons G.S., Schor D.S.M., Jakobs C., Geraghty M.T. Mol. Genet. Metab. 76:172-180(2002) [PubMed: 12126930] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

AF097994 mRNA. Translation: AAF04623.1.
AF481738 mRNA. Translation: AAM09683.1.
AK055952 mRNA. No translation available.
BC031068 mRNA. Translation: AAH31068.1.

RefSeq

NP_057312.1.
NP_872603.1.

UniGene

Hs.529735

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QLR	X-ray	2.30	A/B/C/D	1-425	[»]
2R2N	X-ray	1.95	A/B/C/D	1-425	[»]
2VGZ	X-ray	2.30	A/B	2-425	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSG00000109576. Homo sapiens. [Contig view]

GeneID

51166.

KEGG

hsa:51166.

Organism-specific databases

H-InvDB

HIX0004636.

HGNC

HGNC:17929. AADAT.

PharmGKB

PA24364.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOVERGEN

Q8N5Z0.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-12252.

Reactome

REACT_13. Metabolism of amino acids.

Gene expression databases

ArrayExpress

Q8N5Z0.

CleanEx

HS_AADAT.

GermOnline

ENSG00000109576. Homo sapiens.

Family and domain databases

InterPro

IPR004839. Aminotrans_I/II.
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]

ProDom

Q8N5Z0.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

DrugBank

DB00142. L-Glutamic Acid.
DB00114. Pyridoxal Phosphate.

ProtoNet

Search...

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Entry information

Entry name

AADAT_HUMAN

Accession

Primary (citable) accession number: Q8N5Z0
Secondary accession number(s): Q9UL02

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	April 13, 2004
Last modified:	July 22, 2008
This is version 47 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Alternative products

Sequence annotation (Features)

Molecule processing

Sites

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents