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Protein

Dihydropyrimidinase

Gene

Dpys

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi67Zinc 1By similarity1
Metal bindingi69Zinc 1By similarity1
Metal bindingi159Zinc 1; via carbamate groupBy similarity1
Metal bindingi159Zinc 2; via carbamate groupBy similarity1
Binding sitei164SubstrateBy similarity1
Metal bindingi192Zinc 2By similarity1
Metal bindingi248Zinc 2By similarity1
Metal bindingi326Zinc 1By similarity1
Binding sitei347Substrate; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15404
ReactomeiR-RNO-73621 Pyrimidine catabolism
SABIO-RKiQ63150

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi68376 Dpys

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001659081 – 519DihydropyrimidinaseAdd BLAST519

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei79PhosphoserineBy similarity1
Modified residuei159N6-carboxylysineBy similarity1
Modified residuei256N6-succinyllysineBy similarity1
Modified residuei510PhosphothreonineBy similarity1

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
PhosphoSitePlusiQ63150

Expressioni

Gene expression databases

BgeeiENSRNOG00000004298 Expressed in 4 organ(s), highest expression level in liver
GenevisibleiQ63150 RN

Interactioni

Subunit structurei

Homotetramer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000006004

Structurei

3D structure databases

ProteinModelPortaliQ63150
SMRiQ63150
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2584 Eukaryota
COG0044 LUCA
GeneTreeiENSGT00760000119241
HOGENOMiHOG000219145
HOVERGENiHBG000806
InParanoidiQ63150
KOiK01464
OMAiIDPQVHF
OrthoDBiEOG091G05F3
PhylomeDBiQ63150
TreeFamiTF314706

Family and domain databases

CDDicd01314 D-HYD, 1 hit
Gene3Di2.30.40.10, 2 hits
InterProiView protein in InterPro
IPR006680 Amidohydro-rel
IPR011778 Hydantoinase/dihydroPyrase
IPR011059 Metal-dep_hydrolase_composite
IPR032466 Metal_Hydrolase
PfamiView protein in Pfam
PF01979 Amidohydro_1, 1 hit
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)DescriptionActionsGraphical viewLength
Sequence conflicti403I → M in BAA09833 (PubMed:8679696).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiDPYS_RAT
AccessioniPrimary (citable) accession number: Q63150
Secondary accession number(s): Q642F0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 4, 2005
Last modified: September 12, 2018
This is version 130 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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