AADAT_RAT
ID AADAT_RAT Reviewed; 425 AA.
AC Q64602;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
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:7493966};
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:0000269|PubMed:7493966};
DE AltName: Full=Kynurenine--oxoglutarate aminotransferase II;
DE AltName: Full=Kynurenine--oxoglutarate transaminase 2;
DE EC=2.6.1.7 {ECO:0000269|PubMed:7493966};
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:0000312|RGD:2948}; Synonyms=Kat2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND HOMODIMERIZATION.
RC TISSUE=Kidney;
RX PubMed=7493966; DOI=10.1074/jbc.270.49.29330;
RA Buchli R., Alberati-Giani D., Malherbe P., Koehler C., Broger C.,
RA Cesura A.M.;
RT "Cloning and functional expression of a soluble form of kynurenine/alpha-
RT aminoadipate aminotransferase from rat kidney.";
RL J. Biol. Chem. 270:29330-29335(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:7493966}.
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:7493966};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65561;
CC Evidence={ECO:0000305|PubMed:7493966};
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:7493966};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12602;
CC Evidence={ECO:0000305|PubMed:7493966};
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:0000269|PubMed:7493966};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65901;
CC Evidence={ECO:0000305|PubMed:7493966};
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:0000269|PubMed:7493966};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66093;
CC Evidence={ECO:0000305|PubMed:7493966};
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:0000269|PubMed:7493966};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66045;
CC Evidence={ECO:0000305|PubMed:7493966};
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:0000269|PubMed:7493966};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70048;
CC Evidence={ECO:0000305|PubMed:7493966};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoadipate + L-kynurenine = 4-(2-aminophenyl)-2,4-
CC dioxobutanoate + L-2-aminoadipate; Xref=Rhea:RHEA:70051,
CC ChEBI:CHEBI:57499, ChEBI:CHEBI:57959, ChEBI:CHEBI:58147,
CC ChEBI:CHEBI:58672; Evidence={ECO:0000269|PubMed:7493966};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70052;
CC Evidence={ECO:0000305|PubMed:7493966};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.33 mM for L-kynurenine {ECO:0000269|PubMed:7493966};
CC KM=1.36 mM for 3-hydroxy-L-kynurenine {ECO:0000269|PubMed:7493966};
CC KM=45.5 uM for 2-oxoglutarate {ECO:0000269|PubMed:7493966};
CC KM=5.6 mM for L-glutamate {ECO:0000269|PubMed:7493966};
CC Vmax=135 nmol/min/mg enzyme toward L-kynurenine
CC {ECO:0000269|PubMed:7493966};
CC Vmax=166 nmol/min/mg enzyme toward 3-hydroxy-L-kynurenine
CC {ECO:0000269|PubMed:7493966};
CC Vmax=910 nmol/min/mg enzyme toward 3-hydroxy-L-kynurenine
CC {ECO:0000269|PubMed:7493966};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 4/6.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; Z50144; CAA90507.1; -; mRNA.
DR EMBL; BC078864; AAH78864.1; -; mRNA.
DR RefSeq; NP_058889.1; NM_017193.1.
DR AlphaFoldDB; Q64602; -.
DR SMR; Q64602; -.
DR STRING; 10116.ENSRNOP00000015974; -.
DR BindingDB; Q64602; -.
DR ChEMBL; CHEMBL2662; -.
DR iPTMnet; Q64602; -.
DR PhosphoSitePlus; Q64602; -.
DR PaxDb; Q64602; -.
DR PRIDE; Q64602; -.
DR GeneID; 29416; -.
DR KEGG; rno:29416; -.
DR UCSC; RGD:2948; rat.
DR CTD; 51166; -.
DR RGD; 2948; Aadat.
DR VEuPathDB; HostDB:ENSRNOG00000011861; -.
DR eggNOG; KOG0634; Eukaryota.
DR InParanoid; Q64602; -.
DR OMA; MRLNFTY; -.
DR OrthoDB; 1241781at2759; -.
DR PhylomeDB; Q64602; -.
DR TreeFam; TF328598; -.
DR BioCyc; MetaCyc:MON-12251; -.
DR BRENDA; 2.6.1.39; 5301.
DR BRENDA; 2.6.1.7; 5301.
DR Reactome; R-RNO-71064; Lysine catabolism.
DR Reactome; R-RNO-71240; Tryptophan catabolism.
DR SABIO-RK; Q64602; -.
DR UniPathway; UPA00868; UER00838.
DR PRO; PR:Q64602; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000011861; Expressed in kidney and 16 other tissues.
DR ExpressionAtlas; Q64602; baseline and differential.
DR Genevisible; Q64602; RN.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0047536; F:2-aminoadipate transaminase activity; IDA:UniProtKB.
DR GO; GO:0047958; F:glycine:2-oxoglutarate aminotransferase activity; ISS: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; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Aminotransferase; Direct protein sequencing; Mitochondrion;
KW Phosphoprotein; 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_0000020604"
FT REGION 179..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..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 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 172
FT /note="N6-succinyllysine"
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 351
FT /note="N6-acetyllysine"
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"
SQ SEQUENCE 425 AA; 47784 MW; DDC33DBF21163564 CRC64;
MNYSRFLTAT SLARKTSPIR ATVEIMSRAP KDIISLAPGS PNPKVFPFKS AVFTVENGST
IRFEGEMFQR ALQYSSSYGI PELLSWLKQL QIKLHNPPTV NYSPNEGQMD LCITSGCQDG
LCKVFEMLIN PGDTVLVNEP LYSGALFAMK PLGCNFISVP SDDCGIIPEG LKKVLSQWKP
EDSKDPTKRT PKFLYTIPNG NNPTGNSLTG DRKKEIYELA RKYDFLIIED DPYYFLQFTK
PWEPTFLSMD VDGRVIRADS LSKVISSGLR VGFITGPKSL IQRIVLHTQI SSLHPCTLSQ
LMISELLYQW GEEGFLAHVD RAIDFYKNQR DFILAAADKW LRGLAEWHVP KAGMFLWIKV
NGISDAKKLI EEKAIEREIL LVPGNSFFVD NSAPSSFFRA SFSQVTPAQM DLVFQRLAQL
IKDVS
