Reviewed, UniProtKB/Swiss-Prot Q8N5Z0 (AADAT_HUMAN)

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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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.

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	Mitochondrion Potential.
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.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Ref.2 Inferred from Experiment. Source: Reactome mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2-aminoadipate transaminase activity Inferred from electronic annotation. Source: EC kynurenine-oxoglutarate transaminase activity Ref.2 Inferred from Experiment. Source: Reactome pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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.

Note: 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

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_0000020602

Amino acid modifications

Modified residue

263

1

N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Alternative sequence

23

1

T → SEKRA in isoform 2.

VSP_009874

Natural variant

243

1

V → I: dbSNP rs56350236.

VAR_061005

Experimental info

Sequence conflict

103

1

P → Q in AAH31068. Ref.4

Sequence conflict

380

1

L → S in BAG51596. Ref.3

Secondary structure

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425

Helix Strand Turn

Details...

Helix

3 – 6

4

Helix

9 – 12

4

Beta strand

23 – 29

7

Helix

43 – 45

3

Beta strand

46 – 58

13

Beta strand

61 – 63

3

Helix

65 – 71

7

Helix

81 – 95

15

Turn

98 – 101

4

Helix

104 – 106

3

Beta strand

109 – 116

8

Helix

117 – 128

12

Beta strand

134 – 137

4

Helix

143 – 149

7

Helix

150 – 152

3

Beta strand

155 – 158

4

Helix

168 – 175

8

Helix

182 – 184

3

Helix

186 – 188

3

Beta strand

193 – 196

4

Turn

202 – 204

3

Helix

210 – 222

13

Beta strand

226 – 230

5

Helix

234 – 236

3

Beta strand

237 – 241

5

Turn

246 – 249

4

Beta strand

255 – 261

7

Turn

262 – 265

4

Beta strand

272 – 277

6

Helix

278 – 290

13

Helix

297 – 340

44

Beta strand

342 – 347

6

Beta strand

352 – 360

9

Helix

367 – 371

5

Helix

373 – 376

4

Helix

384 – 387

4

Beta strand

388 – 390

3

Beta strand

397 – 401

5

Helix

407 – 422

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 13, 2004. Version 2. Checksum: 448CCAAB2173A7BA	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
	Isoform 2. Checksum: 0C5A6E51F1BD6F53	FASTA	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

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. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF097994 mRNA. Translation: AAF04623.1.
AF481738 mRNA. Translation: AAM09683.1.
AK055952 mRNA. Translation: BAG51596.1.
BC031068 mRNA. Translation: AAH31068.1.

IPI

IPI00395929.
IPI00410702.

RefSeq

NP_057312.1.
NP_872603.1.

UniGene

Hs.529735

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3DC1	X-ray	2.50	A/B/C/D	1-425	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q8N5Z0.

Proteomic databases

PRIDE

Q8N5Z0.

Genome annotation databases

Ensembl

ENST00000337664; ENSP00000336808; ENSG00000109576; Homo sapiens. [Genome view]
ENST00000353187; ENSP00000226840; ENSG00000109576; Homo sapiens. [Genome view]

GeneID

51166.

KEGG

hsa:51166.

UCSC

uc003isr.1. human.
uc003ist.1. human.

Organism-specific databases

CTD

51166.

GeneCards

GC04M171218.

H-InvDB

HIX0004636.

HGNC

HGNC:17929. AADAT.

PharmGKB

PA24364.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q8N5Z0.

InParanoid

Q8N5Z0.

OMA

RYAGEPQ.

OrthoDB

EOG9C8BC9.

PhylomeDB

Q8N5Z0.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-12252.

BRENDA

2.6.1.39. 247.
2.6.1.7. 247.

Reactome

REACT_13. Metabolism of amino acids.

Gene expression databases

ArrayExpress

Q8N5Z0.

Bgee

Q8N5Z0.

CleanEx

HS_AADAT.

Genevestigator

Q8N5Z0.

GermOnline

ENSG00000109576. Homo sapiens.

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...

Other Resources

DrugBank

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

NextBio

54097.

Entry information

Entry name

AADAT_HUMAN

Accession

Primary (citable) accession number: Q8N5Z0
Secondary accession number(s): B3KP84, Q9UL02

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	April 13, 2004
Last modified:	January 19, 2010
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.