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Protein

Dihydropyrimidinase

Gene

Dpys

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi67 – 671Zinc 1By similarity
Metal bindingi69 – 691Zinc 1By similarity
Metal bindingi159 – 1591Zinc 1; via carbamate groupBy similarity
Metal bindingi159 – 1591Zinc 2; via carbamate groupBy similarity
Binding sitei164 – 1641SubstrateBy similarity
Metal bindingi192 – 1921Zinc 2By similarity
Metal bindingi248 – 2481Zinc 2By similarity
Metal bindingi326 – 3261Zinc 1By similarity
Binding sitei347 – 3471Substrate; via carbonyl oxygenBy similarity

GO - Molecular functioni

  • amino acid binding Source: RGD
  • dihydropyrimidinase activity Source: UniProtKB
  • thymine binding Source: RGD
  • uracil binding Source: RGD
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • beta-alanine metabolic process Source: RGD
  • protein homooligomerization Source: RGD
  • protein homotetramerization Source: UniProtKB
  • thymine catabolic process Source: UniProtKB
  • uracil catabolic process Source: UniProtKB
  • uracil metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15404.
ReactomeiR-RNO-73621. Pyrimidine catabolism.
SABIO-RKQ63150.

Protein family/group databases

MEROPSiM38.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydropyrimidinase (EC:3.5.2.2By similarity)
Short name:
DHP
Short name:
DHPase
Alternative name(s):
Dihydropyrimidine amidohydrolase
Hydantoinase
Gene namesi
Name:Dpys
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi68376. Dpys.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • extracellular exosome Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 519519DihydropyrimidinasePRO_0000165908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791PhosphoserineBy similarity
Modified residuei159 – 1591N6-carboxylysineBy similarity
Modified residuei256 – 2561N6-succinyllysineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ63150.
PRIDEiQ63150.

PTM databases

iPTMnetiQ63150.
PhosphoSiteiQ63150.

Expressioni

Gene expression databases

GenevisibleiQ63150. RN.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

MINTiMINT-4566707.
STRINGi10116.ENSRNOP00000006004.

Structurei

3D structure databases

ProteinModelPortaliQ63150.
SMRiQ63150. Positions 6-493.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2584. Eukaryota.
COG0044. LUCA.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiQ63150.
KOiK01464.
OMAiVDYNIFE.
OrthoDBiEOG7SJD48.
PhylomeDBiQ63150.
TreeFamiTF314706.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro-rel.
IPR030633. Dihydropyrimidinase.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR11647:SF50. PTHR11647:SF50. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q63150-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPQERLLIR GGRVVNDDFS QVADVLVEDG VVRALGRDLL PPGDTSRGLR
60 70 80 90 100
ILDAAGKLVL PGGIDTHTHM QFPFMGSQSV DDFHQGTKAA LAGGTTMIID
110 120 130 140 150
FAIPQKGSSL IEAFETWRNW ADPKVCCDYS LHVAVTWWSD KVKEEMKTLA
160 170 180 190 200
QDKGVNSFKM FMAYKDLYMV QDQQMYAAFS QCKEIGAIAQ VHAENGDLIA
210 220 230 240 250
EGAKKMLALG ITGPEGHELC RPEAVEAEAT LRAITIASAV NCPLYIVHVM
260 270 280 290 300
SKSAAKVIAD AKREGKVVYG EPIAAGLGTD GTQYWNKEWR HAAHHVMGPP
310 320 330 340 350
LRPDPSTPGF LMNLLANGDL TTTGSDNCTF NTCQKALGKD DFTKIPNGVN
360 370 380 390 400
GVEDRMSVIW EKGVHSGKMD ENRFVAVTST NAAKIFNLYP KKGRIAVGSD
410 420 430 440 450
ADIVIWDPEA TRTISAKTHH QAVNFNIFEG MVCHGVPLVT ISRGRVVYEA
460 470 480 490 500
GVFDVTAGHG KFIPRQPFAE FIYKRVKQRD QTCTPIPVKR APYKGEVITL
510
KPRETKEDDT AGTRMQGHS
Length:519
Mass (Da):56,815
Last modified:January 4, 2005 - v2
Checksum:i9A4CEB468303B990
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti403 – 4031I → M in BAA09833 (PubMed:8679696).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63704 mRNA. Translation: BAA09833.1.
BC081768 mRNA. Translation: AAH81768.1.
PIRiS70581.
RefSeqiNP_113893.1. NM_031705.1.
UniGeneiRn.10586.

Genome annotation databases

EnsembliENSRNOT00000006004; ENSRNOP00000006004; ENSRNOG00000004298.
GeneIDi65135.
KEGGirno:65135.
UCSCiRGD:68376. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63704 mRNA. Translation: BAA09833.1.
BC081768 mRNA. Translation: AAH81768.1.
PIRiS70581.
RefSeqiNP_113893.1. NM_031705.1.
UniGeneiRn.10586.

3D structure databases

ProteinModelPortaliQ63150.
SMRiQ63150. Positions 6-493.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4566707.
STRINGi10116.ENSRNOP00000006004.

Protein family/group databases

MEROPSiM38.973.

PTM databases

iPTMnetiQ63150.
PhosphoSiteiQ63150.

Proteomic databases

PaxDbiQ63150.
PRIDEiQ63150.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000006004; ENSRNOP00000006004; ENSRNOG00000004298.
GeneIDi65135.
KEGGirno:65135.
UCSCiRGD:68376. rat.

Organism-specific databases

CTDi1807.
RGDi68376. Dpys.

Phylogenomic databases

eggNOGiKOG2584. Eukaryota.
COG0044. LUCA.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiQ63150.
KOiK01464.
OMAiVDYNIFE.
OrthoDBiEOG7SJD48.
PhylomeDBiQ63150.
TreeFamiTF314706.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15404.
ReactomeiR-RNO-73621. Pyrimidine catabolism.
SABIO-RKQ63150.

Miscellaneous databases

NextBioi613947.
PROiQ63150.

Gene expression databases

GenevisibleiQ63150. RN.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro-rel.
IPR030633. Dihydropyrimidinase.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR11647:SF50. PTHR11647:SF50. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Brown Norway.
    Tissue: Kidney.

Entry informationi

Entry nameiDPYS_RAT
AccessioniPrimary (citable) accession number: Q63150
Secondary accession number(s): Q642F0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 4, 2005
Last modified: January 20, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.