CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014496
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dihydropyrimidinase 
Protein Synonyms/Alias
 DHP; DHPase; Dihydropyrimidine amidohydrolase; Hydantoinase 
Gene Name
 Dpys 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
287DGTQYWNKEWRHAAHacetylation[1]
339TCQKALGKDDFTKIPacetylation[1]
362RMSVIWEKGVHSGKMacetylation[1]
368EKGVHSGKMDENRFVacetylation[1]
501KGEVITLKPRETKEDacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 Catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Can catalyze the ring opening of 5,6- dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate. 
Sequence Annotation
 METAL 67 67 Zinc 1 (By similarity).
 METAL 69 69 Zinc 1 (By similarity).
 METAL 159 159 Zinc 1; via carbamate group (By
 METAL 159 159 Zinc 2; via carbamate group (By
 METAL 192 192 Zinc 2 (By similarity).
 METAL 248 248 Zinc 2 (By similarity).
 METAL 326 326 Zinc 1 (By similarity).
 BINDING 164 164 Substrate (By similarity).
 BINDING 347 347 Substrate; via carbonyl oxygen (By
 MOD_RES 159 159 N6-carboxylysine (By similarity).  
Keyword
 Complete proteome; Direct protein sequencing; Hydrolase; Metal-binding; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 519 AA 
Protein Sequence
MAPQERLLIR GGRVVNDDFS QVADVLVEDG VVRALGRDLL PPGDTSRGLR ILDAAGKLVL 60
PGGIDTHTHM QFPFMGSQSV DDFHQGTKAA LAGGTTMIID FAIPQKGSSL IEAFETWRNW 120
ADPKVCCDYS LHVAVTWWSD KVKEEMKTLA QDKGVNSFKM FMAYKDLYMV QDQQMYAAFS 180
QCKEIGAIAQ VHAENGDLIA EGAKKMLALG ITGPEGHELC RPEAVEAEAT LRAITIASAV 240
NCPLYIVHVM SKSAAKVIAD AKREGKVVYG EPIAAGLGTD GTQYWNKEWR HAAHHVMGPP 300
LRPDPSTPGF LMNLLANGDL TTTGSDNCTF NTCQKALGKD DFTKIPNGVN GVEDRMSVIW 360
EKGVHSGKMD ENRFVAVTST NAAKIFNLYP KKGRIAVGSD ADIVIWDPEA TRTISAKTHH 420
QAVNFNIFEG MVCHGVPLVT ISRGRVVYEA GVFDVTAGHG KFIPRQPFAE FIYKRVKQRD 480
QTCTPIPVKR APYKGEVITL KPRETKEDDT AGTRMQGHS 519 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016597; F:amino acid binding; IDA:RGD.
 GO:0004157; F:dihydropyrimidinase activity; IDA:UniProtKB.
 GO:0002059; F:thymine binding; IDA:RGD.
 GO:0002058; F:uracil binding; IDA:RGD.
 GO:0008270; F:zinc ion binding; IDA:UniProtKB.
 GO:0019482; P:beta-alanine metabolic process; IDA:RGD.
 GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
 GO:0006210; P:thymine catabolic process; IDA:UniProtKB.
 GO:0006212; P:uracil catabolic process; IDA:UniProtKB. 
Interpro
 IPR011778; Hydantoinase/dihydroPyrase.
 IPR011059; Metal-dep_hydrolase_composite. 
Pfam
  
SMART
  
PROSITE
  
PRINTS