Dihydropyrimidinase - Rattus norvegicus (Rat)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q63150 (DPYS_RAT)

Last modified June 16, 2009. Version 62. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Dihydropyrimidinase
      Short name=DHPase
      Short name=DHP
    EC=3.5.2.2
Alternative name(s):
    Dihydropyrimidine amidohydrolase
    Hydantoinase

Gene names

Name:

Dpys

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Hide | Top

Protein attributes

Sequence length	519 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

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.

Hide | Top

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	beta-alanine metabolic process Inferred from direct assay. Source: RGD protein homotetramerization Inferred from direct assay. Source: UniProtKB thymine catabolic process Inferred from direct assay. Source: UniProtKB uracil catabolic process Inferred from direct assay. Source: UniProtKB
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB soluble fraction Inferred from direct assay. Source: RGD
Molecular function	amino acid binding Inferred from direct assay. Source: RGD dihydropyrimidinase activity Inferred from direct assay. Source: UniProtKB thymine binding Inferred from direct assay. Source: RGD uracil binding Inferred from direct assay. Source: RGD zinc ion binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 519

519

Dihydropyrimidinase

PRO_0000165908

Sites

Metal binding

Zinc 1 By similarity

Metal binding

Zinc 1 By similarity

Metal binding

159

Zinc 1; via carbamate group By similarity

Metal binding

159

Zinc 2; via carbamate group By similarity

Metal binding

192

Zinc 2 By similarity

Metal binding

248

Zinc 2 By similarity

Metal binding

326

Zinc 1 By similarity

Binding site

164

Substrate By similarity

Binding site

347

Substrate; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue

159

N6-carboxylysine By similarity

Experimental info

Sequence conflict

403

I → M in BAA09833. Ref.1

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q63150-1 [UniParc].

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

FASTA

519

56,815

        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

Hide | Top

References

	« Hide 'large scale' referencesShow '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.

Hide | Top

Cross-references

Sequence databases
	D63704 mRNA. Translation: BAA09833.1. BC081768 mRNA. Translation: AAH81768.1.
IPI	IPI00205906.
PIR	S70581.
RefSeq	NP_113893.1.
UniGene	Rn.10586
3D structure databases
HSSP	HSSP built from PDB template 1K1D based on UniProtKB Q45515.
ModBase	Search...
Protein family/group databases
MEROPS	M38.973.
Genome annotation databases
Ensembl	ENSRNOG00000004298. Rattus norvegicus. [Contig view]
GeneID	65135.
KEGG	rno:65135.
NMPDR	fig\|10116.3.peg.27008.
Organism-specific databases
RGD	68376. Dpys.
Phylogenomic databases
HOVERGEN	Q63150.
OMA	Q63150. YEAGVFS.
Enzyme and pathway databases
BRENDA	3.5.2.2. 248.
Gene expression databases
ArrayExpress	Q63150.
GermOnline	ENSRNOG00000004298. Rattus norvegicus.
Family and domain databases
InterPro	IPR006680. Amidohydro_1. IPR011778. D-hydantoinase. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
ProDom	PD000518. DHOase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR02033. D-hydantoinase. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	613947.

Hide | Top

Entry information

Entry name

DPYS_RAT

Accession

Primary (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:	June 16, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents