LOCUS NP_001273612 425 aa linear PRI 27-APR-2025
DEFINITION kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
isoform b [Homo sapiens].
ACCESSION NP_001273612
VERSION NP_001273612.1
DBSOURCE REFSEQ: accession NM_001286683.1
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 425)
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 425)
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 425)
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 425)
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 425)
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 425)
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 425)
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 425)
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 425)
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 425)
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 AK314729.1 and BC031068.1.
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 (4) differs in the 5' UTR and uses
an alternate in-frame splice junction at the 3' end of the first
coding exon compared to variant 3. The resulting isoform (b) has
the same N- and C-termini but is shorter compared to isoform a.
Variants 1, 2, and 4 all encode the same isoform (b).
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 :: AK314729.1 [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..425
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="4"
/map="4q33"
Protein 1..425
/product="kynurenine/alpha-aminoadipate aminotransferase,
mitochondrial isoform b"
/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=44187
transit_peptide 1..29
/note="Mitochondrion. /evidence=ECO:0000255; propagated
from UniProtKB/Swiss-Prot (Q8N5Z0.2)"
/calculated_mol_wt=3183
Region 6..425
/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"
mat_peptide 30..425
/product="Kynurenine/alpha-aminoadipate aminotransferase,
mitochondrial. /id=PRO_0000020602"
/note="propagated from UniProtKB/Swiss-Prot (Q8N5Z0.2)"
/calculated_mol_wt=44187
Site 69
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q9WVM8; propagated from
UniProtKB/Swiss-Prot (Q8N5Z0.2)"
Site 179
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q9WVM8; propagated from
UniProtKB/Swiss-Prot (Q8N5Z0.2)"
Region 181..208
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q8N5Z0.2)"
Site 263
/site_type="acetylation"
/note="N6-acetyllysine, alternate.
/evidence=ECO:0000250|UniProtKB:Q9WVM8; propagated from
UniProtKB/Swiss-Prot (Q8N5Z0.2)"
Site 339
/site_type="acetylation"
/note="N6-acetyllysine, alternate.
/evidence=ECO:0000250|UniProtKB:Q9WVM8; propagated from
UniProtKB/Swiss-Prot (Q8N5Z0.2)"
Site 367
/site_type="acetylation"
/note="N6-acetyllysine, alternate.
/evidence=ECO:0000250|UniProtKB:Q9WVM8; propagated from
UniProtKB/Swiss-Prot (Q8N5Z0.2)"
Site 422
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q9WVM8; propagated from
UniProtKB/Swiss-Prot (Q8N5Z0.2)"
CDS 1..425
/gene="AADAT"
/gene_synonym="KAT2; KATII; KYAT2"
/coded_by="NM_001286683.1:210..1487"
/note="isoform b is encoded by transcript variant 4"
/db_xref="CCDS:CCDS3814.1"
/db_xref="GeneID:51166"
/db_xref="HGNC:HGNC:17929"
/db_xref="MIM:611754"
ORIGIN
1 mnyarfitaa saarnpspir tmtdilsrgp ksmislaggl pnpnmfpfkt avitvengkt
61 iqfgeemmkr alqyspsagi pellswlkql qiklhnppti hyppsqgqmd lcvtsgsqqg
121 lckvfemiin pgdnvlldep aysgtlqslh plgcniinva sdesgivpds lrdilsrwkp
181 edaknpqknt pkflytvpng nnptgnslts erkkeiyela rkydfliied dpyyflqfnk
241 frvptflsmd vdgrvirads fskiissglr igfltgpkpl iervilhiqv stlhpstfnq
301 lmisqllhew geegfmahvd rvidfysnqk dailaaadkw ltglaewhvp aagmflwikv
361 kgindvkeli eekavkmgvl mlpgnafyvd ssapspylra sfssaspeqm dvafqvlaql
421 ikesl
//
