CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015642
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Kynurenine--oxoglutarate transaminase 3 
Protein Synonyms/Alias
 Cysteine-S-conjugate beta-lyase 2; Kynurenine aminotransferase III; KATIII; Kynurenine--glyoxylate transaminase; Kynurenine--oxoglutarate transaminase III 
Gene Name
 Ccbl2 
Gene Synonyms/Alias
 Kat3 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
83ISPPSYVKEELSKAAubiquitination[1]
88YVKEELSKAAFIDNMubiquitination[1]
109FGHPALVKALSCLYGacetylation[2, 3, 4]
117ALSCLYGKIYQRQIDacetylation[2, 3, 4, 5, 6, 7, 8]
117ALSCLYGKIYQRQIDsuccinylation[8]
117ALSCLYGKIYQRQIDubiquitination[1]
182VFIPLRSKPTDGMKWacetylation[2]
204DPRELESKFSSKTKAacetylation[2]
210SKFSSKTKAIILNTPubiquitination[1]
289TFSVTGWKLGWSIGPacetylation[4]
404KFVKWMTKHKKLTAIacetylation[4]
420VSAFCDSKSKPHFEKacetylation[8]
420VSAFCDSKSKPHFEKsuccinylation[8]
420VSAFCDSKSKPHFEKubiquitination[1]
436VRFCFIKKDSTLDAAubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [5] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [6] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [7] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [8] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337
Functional Description
 Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se- conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity). Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2- oxoglutarate as amino group acceptor (in vitro). 
Sequence Annotation
 BINDING 54 54 Substrate.
 BINDING 72 72 Substrate; via amide nitrogen.
 BINDING 219 219 Substrate.
 BINDING 430 430 Substrate.
 MOD_RES 117 117 N6-acetyllysine (By similarity).
 MOD_RES 281 281 N6-(pyridoxal phosphate)lysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Aminotransferase; Complete proteome; Lyase; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 455 AA 
Protein Sequence
MLLAQRRLIS LGCRSKPIKT IYSSSKVLGL CTSAKMALKF KNAKRIEGLD SNVWVEFTKL 60
AADPSVVNLG QGFPDISPPS YVKEELSKAA FIDNMNQYTR GFGHPALVKA LSCLYGKIYQ 120
RQIDPNEEIL VAVGAYGSLF NSIQGLVDPG DEVIIMVPFY DCYEPMVRMA GAVPVFIPLR 180
SKPTDGMKWT SSDWTFDPRE LESKFSSKTK AIILNTPHNP LGKVYTRQEL QVIADLCVKH 240
DTLCISDEVY EWLVYTGHTH VKIATLPGMW ERTITIGSAG KTFSVTGWKL GWSIGPAHLI 300
KHLQTVQQNS FYTCATPLQA ALAEAFWIDI KRMDDPECYF NSLPKELEVK RDRMVRLLNS 360
VGLKPIVPDG GYFIIADVSS LGADLSDMNS DEPYDYKFVK WMTKHKKLTA IPVSAFCDSK 420
SKPHFEKLVR FCFIKKDSTL DAAEEIFRAW NSQKS 455 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:EC.
 GO:0047315; F:kynurenine-glyoxylate transaminase activity; IDA:UniProtKB.
 GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IDA:UniProtKB.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0006103; P:2-oxoglutarate metabolic process; IDA:UniProtKB.
 GO:0009058; P:biosynthetic process; IEA:InterPro. 
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