GenomeNet

Database: RefSeq
Entry: NP_001273611
LinkDB: NP_001273611
Original site: NP_001273611 
LOCUS       NP_001273611             429 aa            linear   PRI 21-SEP-2024
DEFINITION  kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
            isoform a [Homo sapiens].
ACCESSION   NP_001273611
VERSION     NP_001273611.1
DBSOURCE    REFSEQ: accession NM_001286682.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Higazi,A.M., Kamel,H.M., Abdel-Naeem,E.A., Abdullah,N.M.,
            Mahrous,D.M. and Osman,A.M.
  TITLE     Expression analysis of selected genes involved in tryptophan
            metabolic pathways in Egyptian children with Autism Spectrum
            Disorder and learning disabilities
  JOURNAL   Sci Rep 11 (1), 6931 (2021)
   PUBMED   33767242
  REMARK    GeneRIF: Expression analysis of selected genes involved in
            tryptophan metabolic pathways in Egyptian children with Autism
            Spectrum Disorder and learning disabilities.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Blanco-Ayala,T., Sathyasaikumar,K.V., Uys,J.D.,
            Perez-de-la-Cruz,V., Pidugu,L.S. and Schwarcz,R.
  TITLE     N-Acetylcysteine Inhibits Kynurenine Aminotransferase II
  JOURNAL   Neuroscience 444, 160-169 (2020)
   PUBMED   32768617
  REMARK    GeneRIF: N-Acetylcysteine Inhibits Kynurenine Aminotransferase II.
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Teumer,A., Chaker,L., Groeneweg,S., Li,Y., Di Munno,C.,
            Barbieri,C., Schultheiss,U.T., Traglia,M., Ahluwalia,T.S.,
            Akiyama,M., Appel,E.V.R., Arking,D.E., Arnold,A., Astrup,A.,
            Beekman,M., Beilby,J.P., Bekaert,S., Boerwinkle,E., Brown,S.J., De
            Buyzere,M., Campbell,P.J., Ceresini,G., Cerqueira,C., Cucca,F.,
            Deary,I.J., Deelen,J., Eckardt,K.U., Ekici,A.B., Eriksson,J.G.,
            Ferrrucci,L., Fiers,T., Fiorillo,E., Ford,I., Fox,C.S.,
            Fuchsberger,C., Galesloot,T.E., Gieger,C., Gogele,M., De Grandi,A.,
            Grarup,N., Greiser,K.H., Haljas,K., Hansen,T., Harris,S.E., van
            Heemst,D., den Heijer,M., Hicks,A.A., den Hollander,W., Homuth,G.,
            Hui,J., Ikram,M.A., Ittermann,T., Jensen,R.A., Jing,J.,
            Jukema,J.W., Kajantie,E., Kamatani,Y., Kasbohm,E., Kaufman,J.M.,
            Kiemeney,L.A., Kloppenburg,M., Kronenberg,F., Kubo,M., Lahti,J.,
            Lapauw,B., Li,S., Liewald,D.C.M., Lim,E.M., Linneberg,A.,
            Marina,M., Mascalzoni,D., Matsuda,K., Medenwald,D., Meisinger,C.,
            Meulenbelt,I., De Meyer,T., Meyer Zu Schwabedissen,H.E.,
            Mikolajczyk,R., Moed,M., Netea-Maier,R.T., Nolte,I.M., Okada,Y.,
            Pala,M., Pattaro,C., Pedersen,O., Petersmann,A., Porcu,E.,
            Postmus,I., Pramstaller,P.P., Psaty,B.M., Ramos,Y.F.M., Rawal,R.,
            Redmond,P., Richards,J.B., Rietzschel,E.R., Rivadeneira,F.,
            Roef,G., Rotter,J.I., Sala,C.F., Schlessinger,D., Selvin,E.,
            Slagboom,P.E., Soranzo,N., Sorensen,T.I.A., Spector,T.D.,
            Starr,J.M., Stott,D.J., Taes,Y., Taliun,D., Tanaka,T., Thuesen,B.,
            Tiller,D., Toniolo,D., Uitterlinden,A.G., Visser,W.E., Walsh,J.P.,
            Wilson,S.G., Wolffenbuttel,B.H.R., Yang,Q., Zheng,H.F., Cappola,A.,
            Peeters,R.P., Naitza,S., Volzke,H., Sanna,S., Kottgen,A.,
            Visser,T.J. and Medici,M.
  CONSRTM   Lifelines Cohort Study
  TITLE     Genome-wide analyses identify a role for SLC17A4 and AADAT in
            thyroid hormone regulation
  JOURNAL   Nat Commun 9 (1), 4455 (2018)
   PUBMED   30367059
  REMARK    GeneRIF: The free thyroxine(FT4)-associated variant
            rs6854291-influences transcript levels of
            kynurenine/alpha-aminoadipate aminotransferase (AADAT) in thyroid,
            implicating AADAT as the causal gene underlying the FT4 association
            at this locus. AADAT-rs6854291 is associated with both the
            3,3',5-triiodothyronine (T3) levels and T3/T4 ratio.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Wigner,P., Czarny,P., Synowiec,E., Bijak,M., Talarowska,M.,
            Galecki,P., Szemraj,J. and Sliwinski,T.
  TITLE     Variation of genes encoding KAT1, AADAT and IDO1 as a potential
            risk of depression development
  JOURNAL   Eur Psychiatry 52, 95-103 (2018)
   PUBMED   29777939
  REMARK    GeneRIF: In this work, we assessed the relationship between
            single-nucleotide polymorphisms (SNPs) of KAT1, KAT2 and IDO1 gene
            encoding, and the risk of depression development. Our study was
            performed on the DNA isolated from peripheral blood of 281
            depressed patients and 236 controls. We genotyped, by using TaqMan
            probes, four polymorphism.
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Han,Q., Robinson,H. and Li,J.
  TITLE     Crystal structure of human kynurenine aminotransferase II
  JOURNAL   J Biol Chem 283 (6), 3567-3573 (2008)
   PUBMED   18056995
  REMARK    GeneRIF: analysis of the crystal structure of kynurenine
            aminotransferase II
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Goh,D.L., Patel,A., Thomas,G.H., Salomons,G.S., Schor,D.S.,
            Jakobs,C. and Geraghty,M.T.
  TITLE     Characterization of the human gene encoding alpha-aminoadipate
            aminotransferase (AADAT)
  JOURNAL   Mol Genet Metab 76 (3), 172-180 (2002)
   PUBMED   12126930
  REMARK    GeneRIF: A human cDNA encodes a 425-residue protein with a
            mitochondrial cleavage signal and a pyridoxal-phosphate binding
            site, ~70% identical to the mouse and rat AADAT orthologs.
            Bacterial expression studies confirm that the gene encodes AADAT
            activity.
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Yu,P., Mosbrook,D.M. and Tagle,D.A.
  TITLE     Genomic organization and expression analysis of mouse kynurenine
            aminotransferase II, a possible factor in the pathophysiology of
            Huntington's disease
  JOURNAL   Mamm Genome 10 (9), 845-852 (1999)
   PUBMED   10441733
REFERENCE   9  (residues 1 to 429)
  AUTHORS   Okuno,E., Tsujimoto,M., Nakamura,M. and Kido,R.
  TITLE     2-Aminoadipate-2-oxoglutarate aminotransferase isoenzymes in human
            liver: a plausible physiological role in lysine and tryptophan
            metabolism
  JOURNAL   Enzyme Protein 47 (3), 136-148 (1993)
   PUBMED   8087205
REFERENCE   10 (residues 1 to 429)
  AUTHORS   Mawal,M.R., Mukhopadhyay,A. and Deshmukh,D.R.
  TITLE     Purification and properties of alpha-aminoadipate aminotransferase
            from rat liver and kidney mitochondria
  JOURNAL   Prep Biochem 21 (2-3), 151-162 (1991)
   PUBMED   1798692
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC084866.5, AK055952.1,
            BC031068.1 and AK314729.1.
            
            Summary: This gene encodes a protein that is highly similar to
            mouse and rat kynurenine aminotransferase II. The rat protein is a
            homodimer with two transaminase activities. One activity is the
            transamination of alpha-aminoadipic acid, a final step in the
            saccaropine pathway which is the major pathway for L-lysine
            catabolism. The other activity involves the transamination of
            kynurenine to produce kynurenine acid, the precursor of kynurenic
            acid which has neuroprotective properties. Several transcript
            variants encoding two different isoforms have been found for this
            gene. [provided by RefSeq, Nov 2013].
            
            Transcript Variant: This variant (3) encodes the longer isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC031068.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q33"
     Protein         1..429
                     /product="kynurenine/alpha-aminoadipate aminotransferase,
                     mitochondrial isoform a"
                     /EC_number="2.6.1.7"
                     /EC_number="2.6.1.39"
                     /EC_number="2.6.1.63"
                     /EC_number="2.6.1.4"
                     /EC_number="2.6.1.73"
                     /note="kynurenine aminotransferase II; L kynurenine/alpha
                     aminoadipate aminotransferase; glycine transaminase AADAT;
                     kynurenine--glyoxylate transaminase AADAT;
                     methionine--glyoxylate transaminase AADAT;
                     kynurenine/alpha-aminoadipate aminotransferase,
                     mitochondrial; KAT/AadAT; 2-aminoadipate transaminase;
                     2-aminoadipate aminotransferase; kynurenine--oxoglutarate
                     transaminase II; kynurenine--oxoglutarate aminotransferase
                     II; kynurenine--oxoglutarate transaminase 2"
                     /calculated_mol_wt=47691
     Region          6..429
                     /region_name="ARO8"
                     /note="DNA-binding transcriptional regulator, MocR family,
                     contains an aminotransferase domain [Transcription, Amino
                     acid transport and metabolism]; COG1167"
                     /db_xref="CDD:440781"
     CDS             1..429
                     /gene="AADAT"
                     /gene_synonym="KAT2; KATII; KYAT2"
                     /coded_by="NM_001286682.2:144..1433"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS75209.1"
                     /db_xref="GeneID:51166"
                     /db_xref="HGNC:HGNC:17929"
                     /db_xref="MIM:611754"
ORIGIN      
        1 mnyarfitaa saarnpspir tmsekradil srgpksmisl agglpnpnmf pfktavitve
       61 ngktiqfgee mmkralqysp sagipellsw lkqlqiklhn pptihyppsq gqmdlcvtsg
      121 sqqglckvfe miinpgdnvl ldepaysgtl qslhplgcni invasdesgi vpdslrdils
      181 rwkpedaknp qkntpkflyt vpngnnptgn sltserkkei yelarkydfl iieddpyyfl
      241 qfnkfrvptf lsmdvdgrvi radsfskiis sglrigfltg pkpliervil hiqvstlhps
      301 tfnqlmisql lhewgeegfm ahvdrvidfy snqkdailaa adkwltglae whvpaagmfl
      361 wikvkgindv kelieekavk mgvlmlpgna fyvdssapsp ylrasfssas peqmdvafqv
      421 laqlikesl
//
DBGET integrated database retrieval system