CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017286
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Kynurenine formamidase 
Protein Synonyms/Alias
 KFA; KFase; Arylformamidase; N-formylkynurenine formamidase; FKF 
Gene Name
 Afmid 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
23LSSEELEKQYSPSRWubiquitination[1]
256PEFHRQSKEFYETLLubiquitination[1]
299VLTQIILKTVFQKL*acetylation[2, 3, 4]
299VLTQIILKTVFQKL*succinylation[3]
299VLTQIILKTVFQKL*ubiquitination[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] 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]
 [3] 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]
 [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
Functional Description
 Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites. 
Sequence Annotation
 MOTIF 93 97 HGGXW.
 ACT_SITE 162 162 Nucleophile (Probable).
 ACT_SITE 247 247 Probable.
 ACT_SITE 279 279 Probable.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Nucleus; Reference proteome; Tryptophan catabolism. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 305 AA 
Protein Sequence
MAFPSLSAGQ NPWRNLSSEE LEKQYSPSRW VIHTKPEEVV GNFVQIGSQA TQKARATRRN 60
QLDVPYGDGE GEKLDIYFPD EDSKAFPLFL FLHGGYWQSG SKDDSAFMVN PLTAQGIVVV 120
IVAYDIAPKG TLDQMVDQVT RSVVFLQRRY PSNEGIYLCG HSAGAHLAAM VLLARWTKHG 180
VTPNLQGFLL VSGIYDLEPL IATSQNDPLR MTLEDAQRNS PQRHLDVVPA QPVAPACPVL 240
VLVGQHDSPE FHRQSKEFYE TLLRVGWKAS FQQLRGVDHF DIIENLTRED DVLTQIILKT 300
VFQKL 305 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0004061; F:arylformamidase activity; IEA:HAMAP.
 GO:0034354; P:de novo NAD biosynthetic process from tryptophan; IEA:HAMAP.
 GO:0019441; P:tryptophan catabolic process to kynurenine; IDA:MGI. 
Interpro
 IPR013094; AB_hydrolase_3.
 IPR027519; KFase. 
Pfam
 PF07859; Abhydrolase_3 
SMART
  
PROSITE
  
PRINTS