AADAT_HUMAN
ID AADAT_HUMAN Reviewed; 425 AA.
AC Q8N5Z0; B3KP84; Q9UL02;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial {ECO:0000305};
DE Short=KAT/AadAT;
DE AltName: Full=2-aminoadipate aminotransferase;
DE AltName: Full=2-aminoadipate transaminase;
DE EC=2.6.1.39 {ECO:0000269|PubMed:12126930, ECO:0000269|PubMed:18620547};
DE AltName: Full=Alpha-aminoadipate aminotransferase;
DE Short=AadAT;
DE AltName: Full=Glycine transaminase AADAT {ECO:0000305};
DE EC=2.6.1.4 {ECO:0000269|PubMed:18620547};
DE AltName: Full=Kynurenine aminotransferase II;
DE AltName: Full=Kynurenine--glyoxylate transaminase AADAT {ECO:0000305};
DE EC=2.6.1.63 {ECO:0000269|PubMed:18620547};
DE AltName: Full=Kynurenine--oxoglutarate aminotransferase II;
DE AltName: Full=Kynurenine--oxoglutarate transaminase 2;
DE EC=2.6.1.7 {ECO:0000269|PubMed:18056995, ECO:0000269|PubMed:18620547};
DE AltName: Full=Kynurenine--oxoglutarate transaminase II;
DE AltName: Full=Methionine--glyoxylate transaminase AADAT {ECO:0000305};
DE EC=2.6.1.73 {ECO:0000269|PubMed:18620547};
DE Flags: Precursor;
GN Name=AADAT {ECO:0000312|HGNC:HGNC:17929};
GN Synonyms=KAT2 {ECO:0000312|HGNC:HGNC:17929},
GN KYAT2 {ECO:0000312|HGNC:HGNC:17929};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Gatti S., Breton J., Mostardini M., Mosca M., Tarroni P., Schwarcz R.,
RA Speciale C., Okuno E., Toma S., Benatti L.;
RT "Cloning of human L-kynurenine/alpha-aminoadipate aminotransferase cDNA
RT from brain tissue.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP COFACTOR.
RX PubMed=12126930; DOI=10.1016/s1096-7192(02)00037-9;
RA Goh D.L.M., Patel A., Thomas G.H., Salomons G.S., Schor D.S.M., Jakobs C.,
RA Geraghty M.T.;
RT "Characterization of the human gene encoding alpha-aminoadipate
RT aminotransferase (AADAT).";
RL Mol. Genet. Metab. 76:172-180(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH 2-OXOGLUTARATE,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP SUBUNIT, AND FUNCTION.
RX PubMed=18620547; DOI=10.1042/bsr20080085;
RA Han Q., Cai T., Tagle D.A., Robinson H., Li J.;
RT "Substrate specificity and structure of human aminoadipate
RT aminotransferase/kynurenine aminotransferase II.";
RL Biosci. Rep. 28:205-215(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
RP AND KYRUNENINE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, AND SUBUNIT.
RX PubMed=18056995; DOI=10.1074/jbc.m708358200;
RA Han Q., Robinson H., Li J.;
RT "Crystal structure of human kynurenine aminotransferase II.";
RL J. Biol. Chem. 283:3567-3573(2008).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP SUBUNIT, AND COFACTOR.
RX PubMed=18056996; DOI=10.1074/jbc.m707925200;
RA Rossi F., Garavaglia S., Montalbano V., Walsh M.A., Rizzi M.;
RT "Crystal structure of human kynurenine aminotransferase II, a drug target
RT for the treatment of schizophrenia.";
RL J. Biol. Chem. 283:3559-3566(2008).
CC -!- FUNCTION: Transaminase with broad substrate specificity. Has
CC transaminase activity towards aminoadipate, kynurenine, methionine and
CC glutamate. Shows activity also towards tryptophan, aspartate and
CC hydroxykynurenine. Accepts a variety of oxo-acids as amino-group
CC acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid,
CC phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use
CC glyoxylate as amino-group acceptor (in vitro).
CC {ECO:0000269|PubMed:12126930, ECO:0000269|PubMed:18056995,
CC ECO:0000269|PubMed:18620547}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + glycine = glyoxylate + L-glutamate;
CC Xref=Rhea:RHEA:14089, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57305; EC=2.6.1.4;
CC Evidence={ECO:0000269|PubMed:18620547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-
CC glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959,
CC ChEBI:CHEBI:58454; EC=2.6.1.7; Evidence={ECO:0000269|PubMed:18056995,
CC ECO:0000269|PubMed:18620547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65561;
CC Evidence={ECO:0000305|PubMed:18056995, ECO:0000305|PubMed:18620547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-kynurenine = glycine + H2O + kynurenate;
CC Xref=Rhea:RHEA:65896, ChEBI:CHEBI:15377, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.63;
CC Evidence={ECO:0000269|PubMed:18620547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65897;
CC Evidence={ECO:0000305|PubMed:18620547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-L-kynurenine + glyoxylate = glycine + H2O +
CC xanthurenate; Xref=Rhea:RHEA:65900, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:58125,
CC ChEBI:CHEBI:71201; EC=2.6.1.63;
CC Evidence={ECO:0000269|PubMed:18620547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxohexanoate + L-kynurenine = H2O + kynurenate + L-2-
CC aminohexanoate; Xref=Rhea:RHEA:66060, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:35177, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454,
CC ChEBI:CHEBI:58455; Evidence={ECO:0000269|PubMed:18620547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66061;
CC Evidence={ECO:0000305|PubMed:18620547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenylpyruvate + L-kynurenine = H2O + kynurenate + L-
CC phenylalanine; Xref=Rhea:RHEA:66092, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18005, ChEBI:CHEBI:57959, ChEBI:CHEBI:58095,
CC ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:18620547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66093;
CC Evidence={ECO:0000305|PubMed:18620547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methylsulfanyl-2-oxobutanoate + L-kynurenine = H2O +
CC kynurenate + L-methionine; Xref=Rhea:RHEA:69096, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16723, ChEBI:CHEBI:57844, ChEBI:CHEBI:57959,
CC ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:18620547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69097;
CC Evidence={ECO:0000305|PubMed:18620547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxo-3-sulfanylpropanoate + L-kynurenine = H2O + kynurenate +
CC L-cysteine; Xref=Rhea:RHEA:69104, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:57678, ChEBI:CHEBI:57959,
CC ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:18620547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69105;
CC Evidence={ECO:0000305|PubMed:18620547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=indole-3-pyruvate + L-kynurenine = H2O + kynurenate + L-
CC tryptophan; Xref=Rhea:RHEA:66052, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17640, ChEBI:CHEBI:57912, ChEBI:CHEBI:57959,
CC ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:18620547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66053;
CC Evidence={ECO:0000305|PubMed:18620547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxopentanoate + L-kynurenine = H2O + kynurenate + L-2-
CC aminopentanoate; Xref=Rhea:RHEA:66076, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28644, ChEBI:CHEBI:57959, ChEBI:CHEBI:58441,
CC ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:18620547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66077;
CC Evidence={ECO:0000305|PubMed:18620547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methyl-2-oxopentanoate + L-kynurenine = H2O + kynurenate +
CC L-leucine; Xref=Rhea:RHEA:66068, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:57427, ChEBI:CHEBI:57959,
CC ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:18620547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66069;
CC Evidence={ECO:0000305|PubMed:18620547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-2-aminoadipate = 2-oxoadipate + L-
CC glutamate; Xref=Rhea:RHEA:12601, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57499, ChEBI:CHEBI:58672; EC=2.6.1.39;
CC Evidence={ECO:0000269|PubMed:12126930, ECO:0000269|PubMed:18620547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12602;
CC Evidence={ECO:0000305|PubMed:12126930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-methionine = 4-methylsulfanyl-2-oxobutanoate +
CC glycine; Xref=Rhea:RHEA:22884, ChEBI:CHEBI:16723, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57844; EC=2.6.1.73;
CC Evidence={ECO:0000269|PubMed:18620547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-2-aminoadipate = 2-oxoadipate + glycine;
CC Xref=Rhea:RHEA:69112, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:57499, ChEBI:CHEBI:58672;
CC Evidence={ECO:0000269|PubMed:18620547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69113;
CC Evidence={ECO:0000305|PubMed:18620547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate +
CC glycine; Xref=Rhea:RHEA:69116, ChEBI:CHEBI:36242, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:58315;
CC Evidence={ECO:0000269|PubMed:18620547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-phenylalanine = 3-phenylpyruvate + glycine;
CC Xref=Rhea:RHEA:69120, ChEBI:CHEBI:18005, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:58095;
CC Evidence={ECO:0000269|PubMed:18620547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-tryptophan = glycine + indole-3-pyruvate;
CC Xref=Rhea:RHEA:69124, ChEBI:CHEBI:17640, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57912;
CC Evidence={ECO:0000269|PubMed:18620547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-leucine = 4-methyl-2-oxopentanoate + glycine;
CC Xref=Rhea:RHEA:69128, ChEBI:CHEBI:17865, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57427;
CC Evidence={ECO:0000269|PubMed:18620547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxobutanoate + L-kynurenine = (2S)-2-aminobutanoate + H2O +
CC kynurenate; Xref=Rhea:RHEA:66044, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16763, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454,
CC ChEBI:CHEBI:74359; Evidence={ECO:0000250|UniProtKB:Q64602};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66045;
CC Evidence={ECO:0000250|UniProtKB:Q64602};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoadipate + L-kynurenine = H2O + kynurenate + L-2-
CC aminoadipate; Xref=Rhea:RHEA:70047, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57499, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454,
CC ChEBI:CHEBI:58672; Evidence={ECO:0000250|UniProtKB:Q64602};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70048;
CC Evidence={ECO:0000250|UniProtKB:Q64602};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:12126930, ECO:0000269|PubMed:18056995,
CC ECO:0000269|PubMed:18056996};
CC -!- ACTIVITY REGULATION: Kynurenine transaminase activity is competitively
CC inhibited by aminoadipate, asparagine, glutamate, histidine, cysteine,
CC lysine, 3-hydroxy-kynurenine and phenylalanine.
CC {ECO:0000269|PubMed:18620547}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.9 mM for aminoadipate {ECO:0000269|PubMed:18620547};
CC KM=4.7 mM for kynurenine {ECO:0000269|PubMed:18620547};
CC KM=1.7 mM for methionine {ECO:0000269|PubMed:18620547};
CC KM=1.6 mM for glutamate {ECO:0000269|PubMed:18620547};
CC KM=1.8 mM for tyrosine {ECO:0000269|PubMed:18620547};
CC KM=1.2 mM for 2-oxoglutarate {ECO:0000269|PubMed:18620547};
CC KM=1.5 mM for 2-oxocaproic acid {ECO:0000269|PubMed:18620547};
CC KM=1.8 mM for phenylpyruvate {ECO:0000269|PubMed:18620547};
CC KM=1.4 mM for ino-3-pyruvate {ECO:0000269|PubMed:18620547};
CC pH dependence:
CC Optimum pH is 7-9. {ECO:0000269|PubMed:18620547};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:18620547};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 4/6.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18056995,
CC ECO:0000269|PubMed:18056996, ECO:0000269|PubMed:18620547}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N5Z0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N5Z0-2; Sequence=VSP_009874;
CC -!- TISSUE SPECIFICITY: Higher expression in the liver. Also found in
CC heart, brain, kidney, pancreas, prostate, testis and ovary.
CC -!- MISCELLANEOUS: [Isoform 1]: May be due to a competing donor splice
CC site.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AF097994; AAF04623.1; -; mRNA.
DR EMBL; AF481738; AAM09683.1; -; mRNA.
DR EMBL; AK055952; BAG51596.1; -; mRNA.
DR EMBL; BC031068; AAH31068.1; -; mRNA.
DR CCDS; CCDS3814.1; -. [Q8N5Z0-1]
DR CCDS; CCDS75209.1; -. [Q8N5Z0-2]
DR RefSeq; NP_001273611.1; NM_001286682.1. [Q8N5Z0-2]
DR RefSeq; NP_001273612.1; NM_001286683.1. [Q8N5Z0-1]
DR RefSeq; NP_057312.1; NM_016228.3. [Q8N5Z0-1]
DR RefSeq; NP_872603.1; NM_182662.1. [Q8N5Z0-1]
DR PDB; 2QLR; X-ray; 2.30 A; A/B/C/D=1-425.
DR PDB; 2R2N; X-ray; 1.95 A; A/B/C/D=1-425.
DR PDB; 2VGZ; X-ray; 2.30 A; A/B=2-425.
DR PDB; 2XH1; X-ray; 2.10 A; A/B=1-425.
DR PDB; 3DC1; X-ray; 2.50 A; A/B/C/D=1-425.
DR PDB; 3UE8; X-ray; 3.22 A; A/B=1-425.
DR PDB; 4GDY; X-ray; 2.89 A; A/B=1-425.
DR PDB; 4GE4; X-ray; 2.41 A; A/B=1-425.
DR PDB; 4GE7; X-ray; 2.10 A; A/B=1-425.
DR PDB; 4GE9; X-ray; 2.43 A; A/B/C/D=1-425.
DR PDB; 4GEB; X-ray; 2.15 A; A/B=1-425.
DR PDB; 5EFS; X-ray; 1.83 A; A=1-425.
DR PDB; 5EUN; X-ray; 1.82 A; A=1-425.
DR PDB; 5TF5; X-ray; 1.81 A; A/B=1-425.
DR PDB; 6D0A; X-ray; 1.47 A; A=1-425.
DR PDB; 6T8P; X-ray; 2.02 A; A/B=1-425.
DR PDB; 6T8Q; X-ray; 2.51 A; A=1-425.
DR PDBsum; 2QLR; -.
DR PDBsum; 2R2N; -.
DR PDBsum; 2VGZ; -.
DR PDBsum; 2XH1; -.
DR PDBsum; 3DC1; -.
DR PDBsum; 3UE8; -.
DR PDBsum; 4GDY; -.
DR PDBsum; 4GE4; -.
DR PDBsum; 4GE7; -.
DR PDBsum; 4GE9; -.
DR PDBsum; 4GEB; -.
DR PDBsum; 5EFS; -.
DR PDBsum; 5EUN; -.
DR PDBsum; 5TF5; -.
DR PDBsum; 6D0A; -.
DR PDBsum; 6T8P; -.
DR PDBsum; 6T8Q; -.
DR AlphaFoldDB; Q8N5Z0; -.
DR SMR; Q8N5Z0; -.
DR BioGRID; 119346; 21.
DR IntAct; Q8N5Z0; 1.
DR STRING; 9606.ENSP00000423190; -.
DR BindingDB; Q8N5Z0; -.
DR ChEMBL; CHEMBL2046259; -.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR iPTMnet; Q8N5Z0; -.
DR PhosphoSitePlus; Q8N5Z0; -.
DR BioMuta; AADAT; -.
DR DMDM; 46395904; -.
DR EPD; Q8N5Z0; -.
DR jPOST; Q8N5Z0; -.
DR MassIVE; Q8N5Z0; -.
DR MaxQB; Q8N5Z0; -.
DR PaxDb; Q8N5Z0; -.
DR PeptideAtlas; Q8N5Z0; -.
DR PRIDE; Q8N5Z0; -.
DR ProteomicsDB; 72114; -. [Q8N5Z0-1]
DR ProteomicsDB; 72115; -. [Q8N5Z0-2]
DR Antibodypedia; 17143; 331 antibodies from 35 providers.
DR DNASU; 51166; -.
DR Ensembl; ENST00000337664.9; ENSP00000336808.4; ENSG00000109576.14. [Q8N5Z0-1]
DR Ensembl; ENST00000353187.6; ENSP00000226840.4; ENSG00000109576.14. [Q8N5Z0-1]
DR Ensembl; ENST00000509167.5; ENSP00000423190.1; ENSG00000109576.14. [Q8N5Z0-2]
DR Ensembl; ENST00000515480.5; ENSP00000423341.1; ENSG00000109576.14. [Q8N5Z0-1]
DR GeneID; 51166; -.
DR KEGG; hsa:51166; -.
DR MANE-Select; ENST00000337664.9; ENSP00000336808.4; NM_016228.4; NP_057312.1.
DR UCSC; uc003isr.4; human. [Q8N5Z0-1]
DR CTD; 51166; -.
DR DisGeNET; 51166; -.
DR GeneCards; AADAT; -.
DR HGNC; HGNC:17929; AADAT.
DR HPA; ENSG00000109576; Tissue enriched (liver).
DR MIM; 611754; gene.
DR neXtProt; NX_Q8N5Z0; -.
DR OpenTargets; ENSG00000109576; -.
DR PharmGKB; PA24364; -.
DR VEuPathDB; HostDB:ENSG00000109576; -.
DR eggNOG; KOG0634; Eukaryota.
DR GeneTree; ENSGT00390000004594; -.
DR HOGENOM; CLU_017584_0_6_1; -.
DR InParanoid; Q8N5Z0; -.
DR OMA; MRLNFTY; -.
DR OrthoDB; 1241781at2759; -.
DR PhylomeDB; Q8N5Z0; -.
DR TreeFam; TF328598; -.
DR BioCyc; MetaCyc:HS03239-MON; -.
DR BRENDA; 2.6.1.39; 2681.
DR BRENDA; 2.6.1.7; 2681.
DR PathwayCommons; Q8N5Z0; -.
DR Reactome; R-HSA-71064; Lysine catabolism.
DR Reactome; R-HSA-71240; Tryptophan catabolism.
DR SABIO-RK; Q8N5Z0; -.
DR SignaLink; Q8N5Z0; -.
DR UniPathway; UPA00868; UER00838.
DR BioGRID-ORCS; 51166; 23 hits in 1074 CRISPR screens.
DR ChiTaRS; AADAT; human.
DR EvolutionaryTrace; Q8N5Z0; -.
DR GenomeRNAi; 51166; -.
DR Pharos; Q8N5Z0; Tchem.
DR PRO; PR:Q8N5Z0; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8N5Z0; protein.
DR Bgee; ENSG00000109576; Expressed in right lobe of liver and 141 other tissues.
DR ExpressionAtlas; Q8N5Z0; baseline and differential.
DR Genevisible; Q8N5Z0; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0047536; F:2-aminoadipate transaminase activity; IDA:UniProtKB.
DR GO; GO:0047958; F:glycine:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
DR GO; GO:0047315; F:kynurenine-glyoxylate transaminase activity; IDA:UniProtKB.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IDA:UniProtKB.
DR GO; GO:0050094; F:methionine-glyoxylate transaminase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:UniProtKB.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006536; P:glutamate metabolic process; IDA:UniProtKB.
DR GO; GO:0070189; P:kynurenine metabolic process; IDA:UniProtKB.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Aminotransferase;
KW Mitochondrion; Pyridoxal phosphate; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..425
FT /note="Kynurenine/alpha-aminoadipate aminotransferase,
FT mitochondrial"
FT /id="PRO_0000020602"
FT REGION 181..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20
FT /ligand="substrate"
FT BINDING 74
FT /ligand="substrate"
FT BINDING 142
FT /ligand="substrate"
FT BINDING 202
FT /ligand="substrate"
FT BINDING 399
FT /ligand="substrate"
FT MOD_RES 69
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT MOD_RES 263
FT /note="N6-(pyridoxal phosphate)lysine; alternate"
FT MOD_RES 263
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT MOD_RES 263
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT MOD_RES 339
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT MOD_RES 339
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT MOD_RES 367
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT MOD_RES 367
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT MOD_RES 422
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT VAR_SEQ 23
FT /note="T -> SEKRA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009874"
FT VARIANT 243
FT /note="V -> I (in dbSNP:rs56350236)"
FT /id="VAR_061005"
FT CONFLICT 103
FT /note="P -> Q (in Ref. 4; AAH31068)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="L -> S (in Ref. 3; BAG51596)"
FT /evidence="ECO:0000305"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:6D0A"
FT HELIX 9..13
FT /evidence="ECO:0007829|PDB:6D0A"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:2R2N"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:6D0A"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:6D0A"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:6D0A"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:4GEB"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6D0A"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:6D0A"
FT HELIX 81..95
FT /evidence="ECO:0007829|PDB:6D0A"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:6D0A"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:6D0A"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:6D0A"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:6D0A"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:6D0A"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:6D0A"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:6D0A"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:6D0A"
FT HELIX 168..175
FT /evidence="ECO:0007829|PDB:6D0A"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:6D0A"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:6D0A"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:6D0A"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:6D0A"
FT HELIX 210..223
FT /evidence="ECO:0007829|PDB:6D0A"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:6D0A"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:6D0A"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:6D0A"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:6D0A"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:5TF5"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:6D0A"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:6D0A"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:4GE9"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:6D0A"
FT HELIX 278..289
FT /evidence="ECO:0007829|PDB:6D0A"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:6D0A"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:4GE7"
FT HELIX 297..340
FT /evidence="ECO:0007829|PDB:6D0A"
FT TURN 341..344
FT /evidence="ECO:0007829|PDB:6D0A"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:6D0A"
FT STRAND 351..360
FT /evidence="ECO:0007829|PDB:6D0A"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:6D0A"
FT TURN 372..378
FT /evidence="ECO:0007829|PDB:6D0A"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:6T8P"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:6D0A"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:5TF5"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:3UE8"
FT STRAND 397..401
FT /evidence="ECO:0007829|PDB:6D0A"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:3UE8"
FT HELIX 407..422
FT /evidence="ECO:0007829|PDB:6D0A"
SQ SEQUENCE 425 AA; 47352 MW; 448CCAAB2173A7BA CRC64;
MNYARFITAA SAARNPSPIR TMTDILSRGP KSMISLAGGL PNPNMFPFKT AVITVENGKT
IQFGEEMMKR ALQYSPSAGI PELLSWLKQL QIKLHNPPTI HYPPSQGQMD LCVTSGSQQG
LCKVFEMIIN PGDNVLLDEP AYSGTLQSLH PLGCNIINVA SDESGIVPDS LRDILSRWKP
EDAKNPQKNT PKFLYTVPNG NNPTGNSLTS ERKKEIYELA RKYDFLIIED DPYYFLQFNK
FRVPTFLSMD VDGRVIRADS FSKIISSGLR IGFLTGPKPL IERVILHIQV STLHPSTFNQ
LMISQLLHEW GEEGFMAHVD RVIDFYSNQK DAILAAADKW LTGLAEWHVP AAGMFLWIKV
KGINDVKELI EEKAVKMGVL MLPGNAFYVD SSAPSPYLRA SFSSASPEQM DVAFQVLAQL
IKESL
