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
//
