CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008594
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aromatic/aminoadipate aminotransferase 1 
Protein Synonyms/Alias
 2-aminoadipate aminotransferase; 2-aminoadipate transaminase; Alpha-aminoadipate aminotransferase; AadAT; Aromatic amino acid aminotransferase 1; Aromatic amino acid aminotransferase I; Aromatic amino acid-requiring protein 8 
Gene Name
 ARO8 
Gene Synonyms/Alias
 YGL202W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
89VNKDYADKSANPSNDacetylation[1]
89VNKDYADKSANPSNDubiquitination[2]
123NFIRDHTKIIHDLKYacetylation[1]
129TKIIHDLKYKDWDVLacetylation[1]
371LRHEYTLKRDCAIDAacetylation[1]
415VHPEFKTKYNSDPYQacetylation[1]
430LEQSLYHKVVERGVLubiquitination[2]
445VVPGSWFKSEGETEPubiquitination[2]
480YAAVSPEKLTEGLKRacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 General aromatic amino acid transaminase involved in several otherwise unrelated metabolic pathways. Responsible for phenylalanine and tyrosine biosynthesis. Active with glutamate, phenylalanine, tyrosine and tryptophan as amino donors and with phenylpyruvate, hydroxyphenylpyruvate, 2-oxoglutarate and pyruvate as amino acceptors. Also active with methionine, alpha- aminoadipate and leucine as amino donors when phenylpyruvate is the amino acceptor and in the reverse reactions with the corresponding oxo acids and phenylalanine as amino donor. Catalyzes the formation of methionine from 2-keto-4- methylthiobutyrate (KMTB) in the methionine salvage pathway primarily using aromatic amino acids (tyrosine, phenylalanine and tryptophan) as the amino donors. Catalyzes the formation of alpha- aminoadipate from alpha-ketoadipate in the lysine biosyntheic pathway. 
Sequence Annotation
 MOD_RES 100 100 Phosphoserine.  
Keyword
 Aminotransferase; Complete proteome; Cytoplasm; Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 500 AA 
Protein Sequence
MTLPESKDFS YLFSDETNAR KPSPLKTCIH LFQDPNIIFL GGGLPLKDYF PWDNLSVDSP 60
KPPFPQGIGA PIDEQNCIKY TVNKDYADKS ANPSNDIPLS RALQYGFSAG QPELLNFIRD 120
HTKIIHDLKY KDWDVLATAG NTNAWESTLR VFCNRGDVIL VEAHSFSSSL ASAEAQGVIT 180
FPVPIDADGI IPEKLAKVME NWTPGAPKPK LLYTIPTGQN PTGTSIADHR KEAIYKIAQK 240
YDFLIVEDEP YYFLQMNPYI KDLKEREKAQ SSPKQDHDEF LKSLANTFLS LDTEGRVIRM 300
DSFSKVLAPG TRLGWITGSS KILKPYLSLH EMTIQAPAGF TQVLVNATLS RWGQKGYLDW 360
LLGLRHEYTL KRDCAIDALY KYLPQSDAFV INPPIAGMFF TVNIDASVHP EFKTKYNSDP 420
YQLEQSLYHK VVERGVLVVP GSWFKSEGET EPPQPAESKE VSNPNIIFFR GTYAAVSPEK 480
LTEGLKRLGD TLYEEFGISK 500 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0047536; F:2-aminoadipate transaminase activity; IDA:SGD.
 GO:0008793; F:aromatic-amino-acid:2-oxoglutarate aminotransferase activity; IDA:SGD.
 GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:EC.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0009072; P:aromatic amino acid family metabolic process; IGI:SGD.
 GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
 GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
 GO:0006571; P:tyrosine biosynthetic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR004839; Aminotransferase_I/II.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 
Pfam
 PF00155; Aminotran_1_2 
SMART
  
PROSITE
  
PRINTS