CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018544
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pyridoxine-5'-phosphate oxidase 
Protein Synonyms/Alias
 Pyridoxamine-phosphate oxidase 
Gene Name
 Pnpo 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
100SARMLLLKGFGKDGFacetylation[1, 2]
100SARMLLLKGFGKDGFsuccinylation[2]
100SARMLLLKGFGKDGFubiquitination[3]
104LLLKGFGKDGFRFFTacetylation[4]
104LLLKGFGKDGFRFFTubiquitination[3]
152PVKKLPEKEAENYFHubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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
Functional Description
 Catalyzes the oxidation of either pyridoxine 5'- phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) (By similarity). 
Sequence Annotation
 NP_BIND 110 111 FMN (By similarity).
 NP_BIND 174 175 FMN (By similarity).
 REGION 225 227 Substrate binding (By similarity).
 BINDING 95 95 FMN (By similarity).
 BINDING 98 98 FMN; via amide nitrogen (By similarity).
 BINDING 100 100 Substrate (By similarity).
 BINDING 117 117 FMN (By similarity).
 BINDING 157 157 Substrate (By similarity).
 BINDING 161 161 Substrate (By similarity).
 BINDING 165 165 Substrate (By similarity).
 MOD_RES 165 165 Phosphoserine.
 MOD_RES 241 241 Phosphoserine.  
Keyword
 Complete proteome; Direct protein sequencing; Flavoprotein; FMN; Oxidoreductase; Phosphoprotein; Pyridoxal phosphate; Pyridoxine biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 261 AA 
Protein Sequence
MTCGLLSVTV TFRRPAKWTG YLRHLCCRGA VMDLGPMRKS YRGDREAFEE THLTSLDPMK 60
QFASWFDEAV QCPDIGEANA MCVATCTRDG KPSARMLLLK GFGKDGFRFF TNYESRKGKE 120
LDSNPFASLV FYWEPLNRQV RVEGPVKKLP EKEAENYFHS RPKSSQIGAV VSRQSSVIPD 180
REYLRKKNEE LGQLYQDQEV PKPEYWGGYI LYPQVMEFWQ GQTNRLHDRI VFRRGLATGD 240
SPLGPMTHHG EEDWVYERLA P 261 
Gene Ontology
 GO:0010181; F:FMN binding; IEA:InterPro.
 GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:EC.
 GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW. 
Interpro
 IPR000659; Pyridox_Oxase.
 IPR019740; Pyridox_Oxase_CS.
 IPR011576; Pyridox_Oxase_FMN-bd.
 IPR019576; Pyridoxamine_oxidase_dimer_C.
 IPR012349; Split_barrel_FMN-bd. 
Pfam
 PF10590; PNPOx_C
 PF01243; Pyridox_oxidase 
SMART
  
PROSITE
 PS01064; PYRIDOX_OXIDASE 
PRINTS