Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q28943 (DPYD_PIG)

Last modified November 25, 2008. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Names and origin

Protein namesRecommended name:
    Dihydropyrimidine dehydrogenase [NADP+]
      Short name=DHPDHase
      Short name=DPD
    EC=1.3.1.2
Alternative name(s):
    Dihydrouracil dehydrogenase
    Dihydrothymine dehydrogenase
Gene names
Name: DPYD
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length1025 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine.

Catalytic activity

5,6-dihydrouracil + NADP(+) = uracil + NADPH.

Cofactor

Binds 2 4Fe-4S clusters. Contains approximately 30 iron atoms per molecule.

FAD.

FMN.

Pathway

Amino-acid biosynthesis; beta-alanine biosynthesis.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the dihydropyrimidine dehydrogenase family.

Contains 3 4Fe-4S ferredoxin-type domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 33
PRO_0000021116
Chain4 – 10251022Dihydropyrimidine dehydrogenase [NADP+]
PRO_0000021117

Regions

Domain69 – 100324Fe-4S ferredoxin-type 1
Domain944 – 976334Fe-4S ferredoxin-type 2
Domain978 – 1007304Fe-4S ferredoxin-type 3
Nucleotide binding335 – 35117NADP Potential
Nucleotide binding471 – 48111FAD Potential
Region661 – 67818Uracil binding Potential

Sites

Metal binding9531Iron-sulfur 1 (4Fe-4S) Potential
Metal binding9561Iron-sulfur 1 (4Fe-4S) Potential
Metal binding9591Iron-sulfur 1 (4Fe-4S) Potential
Metal binding9631Iron-sulfur 1 (4Fe-4S) Potential
Metal binding9861Iron-sulfur 2 (4Fe-4S) Potential
Metal binding9891Iron-sulfur 2 (4Fe-4S) Potential
Metal binding9921Iron-sulfur 2 (4Fe-4S) Potential
Metal binding9961Iron-sulfur 2 (4Fe-4S) Potential

Amino acid modifications

Modified residue5771Phosphoserine By similarity

Secondary structure

.............................................................................................................................................................................. 1025
Helix Strand Turn

Details...