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Reviewed, UniProtKB/Swiss-Prot Q28943 (DPYD_PIG)

Last modified June 16, 2009. Version 75. 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

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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 lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

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

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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.

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Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRepeat
   Ligand4Fe-4S
FAD
FMN
Flavoprotein
Iron
Iron-sulfur
Metal-binding
NADP
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological process'de novo' pyrimidine base biosynthetic process

Inferred from electronic annotation. Source: InterPro

UMP biosynthetic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

thymidine catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

uracil catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

FAD binding

Inferred from direct assay. Source: UniProtKB

FMN binding

Inferred from direct assay. Source: UniProtKB

NADP or NADPH binding

Inferred from direct assay. Source: UniProtKB

dihydroorotate oxidase activity

Inferred from electronic annotation. Source: InterPro

dihydropyrimidine dehydrogenase (NADP+) activity

Inferred from direct assay. Source: UniProtKB

electron carrier activity

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein homodimerization activity

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

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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

1 .............................................................................................................................................................................. 1025
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q28943-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: B8D553AD862845D0

FASTA1,025111,424
        10         20         30         40         50         60 
MAPVLSKDVA DIESILALNP RTQSHAALHS TLAKKLDKKH WKRNPDKNCF HCEKLENNFG 

        70         80         90        100        110        120 
DIKHTTLGER GALREAMRCL KCADAPCQKS CPTHLDIKSF ITSISNKNYY GAAKMIFSDN 

       130        140        150        160        170        180 
PLGLTCGMVC PTSDLCVGGC NLYATEEGSI NIGGLQQFAS EVFKAMNIPQ IRNPCLPSQE 

       190        200        210        220        230        240 
KMPEAYSAKI ALLGAGPASI SCASFLARLG YSDITIFEKQ EYVGGLSTSE IPQFRLPYDV 

       250        260        270        280        290        300 
VNFEIELMKD LGVKIICGKS LSENEITLNT LKEEGYKAAF IGIGLPEPKT DDIFQGLTQD 

       310        320        330        340        350        360 
QGFYTSKDFL PLVAKSSKAG MCACHSPLPS IRGAVIVLGA GDTAFDCATS ALRCGARRVF 

       370        380        390        400        410        420 
LVFRKGFVNI RAVPEEVELA KEEKCEFLPF LSPRKVIVKG GRIVAVQFVR TEQDETGKWN 

       430        440        450        460        470        480 
EDEDQIVHLK ADVVISAFGS VLRDPKVKEA LSPIKFNRWD LPEVDPETMQ TSEPWVFAGG 

       490        500        510        520        530        540 
DIVGMANTTV ESVNDGKQAS WYIHKYIQAQ YGASVSAKPE LPLFYTPVDL VDISVEMAGL 

       550        560        570        580        590        600 
KFINPFGLAS AAPTTSSSMI RRAFEAGWGF ALTKTFSLDK DIVTNVSPRI VRGTTSGPMY 

       610        620        630        640        650        660 
GPGQSSFLNI ELISEKTAAY WCQSVTELKA DFPDNIVIAS IMCSYNKNDW MELSRKAEAS 

       670        680        690        700        710        720 
GADALELNLS CPHGMGERGM GLACGQDPEL VRNICRWVRQ AVQIPFFAKL TPNVTDIVSI 

       730        740        750        760        770        780 
ARAAKEGGAD GVTATNTVSG LMGLKADGTP WPAVGAGKRT TYGGVSGTAI RPIALRAVTT 

       790        800        810        820        830        840 
IARALPGFPI LATGGIDSAE SGLQFLHSGA SVLQVCSAVQ NQDFTVIQDY CTGLKALLYL 

       850        860        870        880        890        900 
KSIEELQGWD GQSPGTESHQ KGKPVPRIAE LMGKKLPNFG PYLEQRKKII AEEKMRLKEQ 

       910        920        930        940        950        960 
NAAFPPLERK PFIPKKPIPA IKDVIGKALQ YLGTFGELSN IEQVVAVIDE EMCINCGKCY 

       970        980        990       1000       1010       1020 
MTCNDSGYQA IQFDPETHLP TVTDTCTGCT LCLSVCPIID CIRMVSRTTP YEPKRGLPLA 


VNPVC

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References

[1]"cDNA cloning and chromosome mapping of human dihydropyrimidine dehydrogenase, an enzyme associated with 5-fluorouracil toxicity and congenital thymine uraciluria."
Yokota H., Fernandez-Salguero P., Furuya H., Lin K., McBride O.W., Podschun B., Schnackerz K.D., Gonzalez F.J.
J. Biol. Chem. 269:23192-23196(1994) [PubMed: 8083224] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
+Additional computationally mapped references.

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Cross-references

Sequence databases

U09179 mRNA. Translation: AAA57475.1.
PIRB54718.
RefSeqNP_999209.1.
UniGeneSsc.153

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GT8X-ray3.30A/B/C/D1-1025[»]
1GTEX-ray1.65A/B/C/D1-1025[»]
1GTHX-ray2.25A/B/C/D1-1025[»]
1H7WX-ray1.90A/B/C/D1-1025[»]
1H7XX-ray2.01A/B/C/D1-1025[»]
ModBaseSearch...

Genome annotation databases

GeneID397109.
KEGGssc:397109.

Phylogenomic databases

HOVERGENQ28943.

Enzyme and pathway databases

BRENDA1.3.1.2. 249.

Family and domain databases

InterProIPR017896. 4Fe4S_Fe-S-bd.
IPR001450. 4Fe4S_Fe_S_bd_subgr.
IPR017900. 4Fe4S_Fe_S_CS.
IPR000759. Adrndx_reductase.
IPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005720. Dihydroorotate_DH_1_core.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR012285. Fum_reductase_C.
IPR016040. NAD(P)-bd_dom.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF01180. DHO_dh. 1 hit.
PF00037. Fer4. 1 hit.
PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00419. ADXRDTASE.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01037. pyrD_sub1_fam. 1 hit.
PROSITEPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00544. Fluorouracil.

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Entry information

Entry nameDPYD_PIG
AccessionPrimary (citable) accession number: Q28943
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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