AADAT_BOVIN
ID AADAT_BOVIN Reviewed; 425 AA.
AC Q5E9N4; Q32KQ6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial {ECO:0000250|UniProtKB:Q8N5Z0};
DE Short=KAT/AadAT;
DE AltName: Full=2-aminoadipate aminotransferase;
DE AltName: Full=2-aminoadipate transaminase;
DE EC=2.6.1.39 {ECO:0000250|UniProtKB:Q8N5Z0};
DE AltName: Full=Alpha-aminoadipate aminotransferase;
DE Short=AadAT;
DE AltName: Full=Glycine transaminase AADAT {ECO:0000250|UniProtKB:Q8N5Z0};
DE EC=2.6.1.4 {ECO:0000250|UniProtKB:Q8N5Z0};
DE AltName: Full=Kynurenine aminotransferase II;
DE AltName: Full=Kynurenine--glyoxylate transaminase AADAT {ECO:0000250|UniProtKB:Q8N5Z0};
DE EC=2.6.1.63 {ECO:0000250|UniProtKB:Q8N5Z0};
DE AltName: Full=Kynurenine--oxoglutarate aminotransferase II;
DE AltName: Full=Kynurenine--oxoglutarate transaminase 2;
DE EC=2.6.1.7 {ECO:0000250|UniProtKB:Q8N5Z0};
DE AltName: Full=Kynurenine--oxoglutarate transaminase II;
DE AltName: Full=Methionine--glyoxylate transaminase AADAT {ECO:0000250|UniProtKB:Q8N5Z0};
DE EC=2.6.1.73 {ECO:0000250|UniProtKB:Q8N5Z0};
DE Flags: Precursor;
GN Name=AADAT {ECO:0000250|UniProtKB:Q8N5Z0};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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) (By similarity).
CC {ECO:0000250|UniProtKB:Q8N5Z0}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65561;
CC Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
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:0000250|UniProtKB:Q8N5Z0};
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:0000250|UniProtKB:Q8N5Z0};
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:0000250|UniProtKB:Q8N5Z0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65897;
CC Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
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:0000250|UniProtKB:Q8N5Z0};
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:0000250|UniProtKB:Q8N5Z0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66061;
CC Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
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:0000250|UniProtKB:Q8N5Z0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66093;
CC Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
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:0000250|UniProtKB:Q8N5Z0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69097;
CC Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
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:0000250|UniProtKB:Q8N5Z0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69105;
CC Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
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:0000250|UniProtKB:Q8N5Z0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66053;
CC Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
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:0000250|UniProtKB:Q8N5Z0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66077;
CC Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
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:0000250|UniProtKB:Q8N5Z0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66069;
CC Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
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:0000250|UniProtKB:Q8N5Z0};
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:0000250|UniProtKB:Q8N5Z0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69113;
CC Evidence={ECO:0000250|UniProtKB:Q8N5Z0};
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:0000250|UniProtKB:Q8N5Z0};
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:0000250|UniProtKB:Q8N5Z0};
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:0000250|UniProtKB:Q8N5Z0};
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:0000250|UniProtKB:Q8N5Z0};
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:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 4/6.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; BT020844; AAX08861.1; -; mRNA.
DR EMBL; BT020886; AAX08903.1; -; mRNA.
DR EMBL; BC109974; AAI09975.1; -; mRNA.
DR RefSeq; NP_001015551.1; NM_001015551.1.
DR AlphaFoldDB; Q5E9N4; -.
DR SMR; Q5E9N4; -.
DR PaxDb; Q5E9N4; -.
DR PRIDE; Q5E9N4; -.
DR GeneID; 508929; -.
DR KEGG; bta:508929; -.
DR CTD; 51166; -.
DR eggNOG; KOG0634; Eukaryota.
DR InParanoid; Q5E9N4; -.
DR OrthoDB; 1241781at2759; -.
DR UniPathway; UPA00868; UER00838.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0047536; F:2-aminoadipate transaminase activity; ISS:UniProtKB.
DR GO; GO:0047958; F:glycine:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
DR GO; GO:0047315; F:kynurenine-glyoxylate transaminase activity; ISS:UniProtKB.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; ISS:UniProtKB.
DR GO; GO:0050094; F:methionine-glyoxylate transaminase activity; ISS: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; ISS: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; ISS:UniProtKB.
DR GO; GO:0070189; P:kynurenine metabolic process; ISS: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 2: Evidence at transcript level;
KW Acetylation; Aminotransferase; Mitochondrion; Pyridoxal phosphate;
KW Reference proteome; Transferase; 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_0000244427"
FT REGION 178..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 /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
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 422
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVM8"
FT CONFLICT 111
FT /note="L -> I (in Ref. 2; AAI09975)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="L -> I (in Ref. 2; AAI09975)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 425 AA; 47901 MW; 693F7529FC9AF666 CRC64;
MNYARFITAT SAARKPSTIR VMTEILSKAP KSVISLATGA PNPNTFPFKT AVITIENGKP
IQFNEQMMKR ALQYSQSAGI PELLSWLKQL QVKLHNPPTI HYAPTQGQMD LCVTCGSQEG
LCKVFEMIVN PGDNILVNEP IYSGTIHALQ PLGCNMINVS SDEHGIIPDS LREILSKWKP
EDSKNPKKNS PKFLYTVPNG NNPSGNSLTA ERKREIYELA RKYDFLIIED DPYYFMQFNK
PWAPTFLSMD EDGRVIRADS FSKVLSSGLR IGFITGPKPL IERIVLHIQV STMHPSTFAQ
LLVSQLLYQW GEEGFLGHVD RVIDFYRKQR DALMAAADKW LSGLAEWHVP TAGMFLWVKI
KGIHDVRKLI EEKAFKKEIF MLPGCGFYTD SSAPCPYFRA SFSSASPEQM DLAFQRLAQL
IKESL
