GenomeNet

Database: RefSeq
Entry: NP_001273611
LinkDB: NP_001273611
Original site: NP_001273611 
LOCUS       NP_001273611             429 aa            linear   PRI 13-AUG-2020
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   Teumer A, Chaker L, Groeneweg S, Li Y, Di Munno C, Barbieri C,
            Schultheiss UT, Traglia M, Ahluwalia TS, Akiyama M, Appel EVR,
            Arking DE, Arnold A, Astrup A, Beekman M, Beilby JP, Bekaert S,
            Boerwinkle E, Brown SJ, De Buyzere M, Campbell PJ, Ceresini G,
            Cerqueira C, Cucca F, Deary IJ, Deelen J, Eckardt KU, Ekici AB,
            Eriksson JG, Ferrrucci L, Fiers T, Fiorillo E, Ford I, Fox CS,
            Fuchsberger C, Galesloot TE, Gieger C, Gogele M, De Grandi A,
            Grarup N, Greiser KH, Haljas K, Hansen T, Harris SE, van Heemst D,
            den Heijer M, Hicks AA, den Hollander W, Homuth G, Hui J, Ikram MA,
            Ittermann T, Jensen RA, Jing J, Jukema JW, Kajantie E, Kamatani Y,
            Kasbohm E, Kaufman JM, Kiemeney LA, Kloppenburg M, Kronenberg F,
            Kubo M, Lahti J, Lapauw B, Li S, Liewald DCM, Lim EM, Linneberg A,
            Marina M, Mascalzoni D, Matsuda K, Medenwald D, Meisinger C,
            Meulenbelt I, De Meyer T, Meyer Zu Schwabedissen HE, Mikolajczyk R,
            Moed M, Netea-Maier RT, Nolte IM, Okada Y, Pala M, Pattaro C,
            Pedersen O, Petersmann A, Porcu E, Postmus I, Pramstaller PP, Psaty
            BM, Ramos YFM, Rawal R, Redmond P, Richards JB, Rietzschel ER,
            Rivadeneira F, Roef G, Rotter JI, Sala CF, Schlessinger D, Selvin
            E, Slagboom PE, Soranzo N, Sorensen TIA, Spector TD, Starr JM,
            Stott DJ, Taes Y, Taliun D, Tanaka T, Thuesen B, Tiller D, Toniolo
            D, Uitterlinden AG, Visser WE, Walsh JP, Wilson SG, Wolffenbuttel
            BHR, Yang Q, Zheng HF, Cappola A, Peeters RP, Naitza S, Volzke H,
            Sanna S, Kottgen A, Visser TJ 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   2  (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   3  (residues 1 to 429)
  AUTHORS   Matysik-Wozniak A, Junemann A, Turski WA, Wnorowski A, Jozwiak K,
            Paduch R, Okuno E, Moneta-Wielgos J, Choragiewicz T, Maciejewski R
            and Rejdak R.
  TITLE     The presence of kynurenine aminotransferases in the human cornea:
            Evidence from bioinformatics analysis of gene expression and
            immunohistochemical staining
  JOURNAL   Mol. Vis. 23, 364-371 (2017)
   PUBMED   28706436
  REMARK    GeneRIF: Immunohistochemical analysis revealed the presence of KAT
            I, II, and III in all examined corneal sections.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Sun G, Nematollahi A, Nadvi NA, Kwan AH, Jeffries CM and Church WB.
  TITLE     Expression, purification and crystallization of human kynurenine
            aminotransferase 2 exploiting a highly optimized codon set
  JOURNAL   Protein Expr. Purif. 121, 41-45 (2016)
   PUBMED   26773745
  REMARK    GeneRIF: he optimised method of protein production provides a fast
            and reliable technique to generate large quantities of active human
            KAT2 suitable for future small-molecule lead compound screening and
            structural design work.
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Hennings A, Schwarz MJ, Riemer S, Stapf TM, Selberdinger VB and
            Rief W.
  TITLE     Exercise affects symptom severity but not biological measures in
            depression and somatization - results on IL-6, neopterin,
            tryptophan, kynurenine and 5-HIAA
  JOURNAL   Psychiatry Res 210 (3), 925-933 (2013)
   PUBMED   24140252
  REMARK    GeneRIF: Participants with major depression had lower levels of
            kynurenine compared to controls, with intermediate concentrations
            in somatoform patients.
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 DL, Patel A, Thomas GH, Salomons GS, Schor DS, Jakobs C and
            Geraghty MT.
  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 DM and Tagle DA.
  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 MR, Mukhopadhyay A and Deshmukh DR.
  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]
            ##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"
                     /note="kynurenine aminotransferase II; L kynurenine/alpha
                     aminoadipate aminotransferase;
                     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          38..423
                     /region_name="AAT_like"
                     /note="Aspartate aminotransferase family. This family
                     belongs to pyridoxal phosphate (PLP)-dependent aspartate
                     aminotransferase superfamily (fold I). Pyridoxal phosphate
                     combines with an alpha-amino acid to form a compound
                     called a Schiff base or aldimine...; cd00609"
                     /db_xref="CDD:99734"
     Region          71..421
                     /region_name="Aminotran_1_2"
                     /note="Aminotransferase class I and II; pfam00155"
                     /db_xref="CDD:278580"
     Site            order(120..122,146,206,237,264,266..267,274)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(123,156,230,272..274,303,306)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            267
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
     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
//
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