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Q63150 (DPYS_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydropyrimidinase

Short name=DHP
Short name=DHPase
EC=3.5.2.2
Alternative name(s):
Dihydropyrimidine amidohydrolase
Hydantoinase
Gene names
Name:Dpys
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Can catalyzes the ring opening of 5,6-dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate.

Catalytic activity

5,6-dihydrouracil + H2O = 3-ureidopropanoate.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homotetramer By similarity.

Post-translational modification

Carbamylation allows a single lysine to coordinate two zinc ions By similarity.

Sequence similarities

Belongs to the DHOase family. Hydantoinase/dihydropyrimidinase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 519519Dihydropyrimidinase
PRO_0000165908

Sites

Metal binding671Zinc 1 By similarity
Metal binding691Zinc 1 By similarity
Metal binding1591Zinc 1; via carbamate group By similarity
Metal binding1591Zinc 2; via carbamate group By similarity
Metal binding1921Zinc 2 By similarity
Metal binding2481Zinc 2 By similarity
Metal binding3261Zinc 1 By similarity
Binding site1641Substrate By similarity
Binding site3471Substrate; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue1591N6-carboxylysine By similarity

Experimental info

Sequence conflict4031I → M in BAA09833. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q63150 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: 9A4CEB468303B990

FASTA51956,815
        10         20         30         40         50         60 
MAPQERLLIR GGRVVNDDFS QVADVLVEDG VVRALGRDLL PPGDTSRGLR ILDAAGKLVL 

        70         80         90        100        110        120 
PGGIDTHTHM QFPFMGSQSV DDFHQGTKAA LAGGTTMIID FAIPQKGSSL IEAFETWRNW 

       130        140        150        160        170        180 
ADPKVCCDYS LHVAVTWWSD KVKEEMKTLA QDKGVNSFKM FMAYKDLYMV QDQQMYAAFS 

       190        200        210        220        230        240 
QCKEIGAIAQ VHAENGDLIA EGAKKMLALG ITGPEGHELC RPEAVEAEAT LRAITIASAV 

       250        260        270        280        290        300 
NCPLYIVHVM SKSAAKVIAD AKREGKVVYG EPIAAGLGTD GTQYWNKEWR HAAHHVMGPP 

       310        320        330        340        350        360 
LRPDPSTPGF LMNLLANGDL TTTGSDNCTF NTCQKALGKD DFTKIPNGVN GVEDRMSVIW 

       370        380        390        400        410        420 
EKGVHSGKMD ENRFVAVTST NAAKIFNLYP KKGRIAVGSD ADIVIWDPEA TRTISAKTHH 

       430        440        450        460        470        480 
QAVNFNIFEG MVCHGVPLVT ISRGRVVYEA GVFDVTAGHG KFIPRQPFAE FIYKRVKQRD 

       490        500        510 
QTCTPIPVKR APYKGEVITL KPRETKEDDT AGTRMQGHS 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and sequencing of a cDNA encoding dihydropyrimidinase from the rat liver."
Matsuda K., Sakata S., Kaneko M., Hamajima N., Nonaka M., Sasaki M., Tamaki N.
Biochim. Biophys. Acta 1307:140-144(1996) [PubMed: 8679696] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Brown Norway.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D63704 mRNA. Translation: BAA09833.1.
BC081768 mRNA. Translation: AAH81768.1.
IPIIPI00205906.
PIRS70581.
RefSeqNP_113893.1. NM_031705.1.
UniGeneRn.10586.

3D structure databases

ProteinModelPortalQ63150.
SMRQ63150. Positions 6-493.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ63150.

Protein family/group databases

MEROPSM38.973.

Proteomic databases

PRIDEQ63150.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000006004; ENSRNOP00000006004; ENSRNOG00000004298.
GeneID65135.
KEGGrno:65135.
NMPDRfig|10116.3.peg.27008.
UCSCNM_031705. rat.

Organism-specific databases

CTD1807.
RGD68376. Dpys.

Phylogenomic databases

eggNOGmaNOG15500.
GeneTreeENSGT00550000074371.
HOVERGENHBG000806.
InParanoidQ63150.
OMAKSASDYG.
OrthoDBEOG45HRX7.
PhylomeDBQ63150.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15404.

Gene expression databases

ArrayExpressQ63150.
GenevestigatorQ63150.
GermOnlineENSRNOG00000004298. Rattus norvegicus.

Family and domain databases

InterProIPR006680. Amidohydro_1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
KOK01464.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 2 hits.
TIGRFAMsTIGR02033. D-hydantoinase. 1 hit.
ProtoNetSearch...

Other

NextBio613947.

Entry information

Entry nameDPYS_RAT
AccessionPrimary (citable) accession number: Q63150
Secondary accession number(s): Q642F0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 4, 2005
Last modified: November 16, 2011
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families