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UniProtKB/Swiss-Prot entry Q8N5Z0


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AADAT_HUMAN
Primary accession number Q8N5Z0
Secondary accession number Q9UL02
Integrated into Swiss-Prot on April 13, 2004
Sequence was last modified on April 13, 2004 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 51)
Name and origin of the protein
Protein name Kynurenine/alpha-aminoadipate aminotransferase mitochondrial [Precursor]
Synonyms 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
AadAT
Gene name
Name: AADAT
Synonyms: KAT2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Gatti S., Breton J., Mostardini M., Mosca M., Tarroni P., Schwarcz R., Speciale C., Okuno E., Toma S., Benatti L.;
"Cloning of human L-kynurenine/alpha-aminoadipate aminotransferase cDNA from brain tissue.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1016/S1096-7192(02)00037-9; PubMed=12126930 [NCBI, ExPASy, EBI, Israel, Japan]
Goh D.L.M., Patel A., Thomas G.H., Salomons G.S., Schor D.S.M., Jakobs C., Geraghty M.T.;
"Characterization of the human gene encoding alpha-aminoadipate aminotransferase (AADAT).";
Mol. Genet. Metab. 76:172-180(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF097994; AAF04623.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF481738; AAM09683.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK055952; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
BC031068; AAH31068.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_057312.1; -.
NP_872603.1; -.
UniGene Hs.529735
3D structure databases
PDB
2QLR; X-ray; 2.30 A; A/B/C/D=1-425.[ExPASy / RCSB / EBI]
2R2N; X-ray; 1.95 A; A/B/C/D=1-425.[ExPASy / RCSB / EBI]
2VGZ; X-ray; 2.30 A; A/B=2-425.[ExPASy / RCSB / EBI]
3DC1; X-ray; 2.50 A; A/B/C/D=1-425.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2QLR; -.
2R2N; -.
2VGZ; -.
3DC1; -.
ModBase Q8N5Z0.
PTM databases
PhosphoSite Q8N5Z0; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-12252; -.
Reactome REACT_13; Metabolism of amino acids.
Organism-specific databases
H-InvDB HIX0004636; -.
HGNC HGNC:17929; AADAT.
GenAtlas AADAT.
PharmGKB PA24364; -.
GeneCards Q8N5Z0.
Gene expression databases
ArrayExpress Q8N5Z0; -.
CleanEx HS_AADAT; -.
GermOnline ENSG00000109576; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0047536; Molecular function: 2-aminoadipate transaminase activity (inferred from electronic annotation from EC).
GO:0016212; Molecular function: kynurenine-oxoglutarate transaminase activity (inferred from electronic annotation from EC).
GO:0030170; Molecular function: pyridoxal phosphate binding (inferred from electronic annotation from InterPro).
GO:0009058; Biological process: biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR004839; Aminotrans_I/II.
IPR015421; PyrdxlP-dep_Trfase_major_sub1.
Graphical view of domain structure.
Gene3D G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
Pfam PF00155; Aminotran_1_2; 1.
Pfam graphical view of domain structure.
ProtoNet Q8N5Z0.
Genome annotation databases
Ensembl ENSG00000109576; Homo sapiens. [Contig view]
GeneID 51166; -.
KEGG hsa:51166; -.
Phylogenomic databases
HOVERGEN Q8N5Z0; -.
Other
DrugBank DB00142; L-Glutamic Acid.
DB00114; Pyridoxal Phosphate.
NextBio 54097; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Aminotransferase; Mitochondrion; Pyridoxal phosphate; Transferase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    29  29     Mitochondrion (Potential). 
CHAIN   30   425  396     Kynurenine/alpha-aminoadipate aminotransferase mitochondrial. PRO_0000020602
BINDING   263   263        Pyridoxal phosphate (covalent) (By similarity). 
VAR_SEQ   23    23        T -> SEKRA (in isoform 2). VSP_009874
CONFLICT   103   103        P -> Q (in Ref. 4; AAH31068). 
CONFLICT   380   380        L -> S (in Ref. 3). 
HELIX   3     6  4      
HELIX   9    12  4      
STRAND   23    29  7      
HELIX   43    45  3      
STRAND   46    58  13      
STRAND   61    63  3      
HELIX   65    71  7      
HELIX   81    95  15      
TURN   98   101  4      
HELIX   104   106  3      
STRAND   109   116  8      
HELIX   117   128  12      
STRAND   134   137  4      
HELIX   143   149  7      
HELIX   150   152  3      
STRAND   155   158  4      
HELIX   168   175  8      
HELIX   182   184  3      
HELIX   186   188  3      
STRAND   193   196  4      
TURN   202   204  3      
HELIX   210   222  13      
STRAND   226   230  5      
HELIX   234   236  3      
STRAND   237   241  5      
TURN   246   249  4      
STRAND   255   261  7      
TURN   262   265  4      
STRAND   272   277  6      
HELIX   278   290  13      
HELIX   297   340  44      
STRAND   342   347  6      
STRAND   352   360  9      
HELIX   367   371  5      
HELIX   373   376  4      
HELIX   384   387  4      
STRAND   388   390  3      
STRAND   397   401  5      
HELIX   407   422  16      
Sequence information
Length: 425 AA [This is the length of the unprocessed precursor] Molecular weight: 47352 Da [This is the MW of the unprocessed precursor] CRC64: 448CCAAB2173A7BA [This is a checksum on the sequence]
        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 

Q8N5Z0 in FASTA format

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