Probable dihydropyrimidine dehydrogenase [NADP+]

Preferred order of sections

Names and origin

Protein names

Recommended name:
Probable dihydropyrimidine dehydrogenase [NADP+]
Short name=DHPDHase
Short name=DPD
EC=1.3.1.2

Alternative name(s):
Dihydrothymine dehydrogenase
Dihydrouracil dehydrogenase

Gene names

Name:	dpyd-1
ORF Names:	CBG14689

Organism

Caenorhabditis briggsae

Taxonomic identifier

6238 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	1053 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil By similarity. UniProtKB Q12882
Catalytic activity	5,6-dihydrouracil + NADP⁺ = uracil + NADPH. UniProtKB Q12882
Cofactor	Binds 2 4Fe-4S clusters By similarity. UniProtKB Q12882 FAD By similarity. UniProtKB Q12882 FMN By similarity. UniProtKB Q12882
Pathway	Amino-acid biosynthesis; beta-alanine biosynthesis. UniProtKB Q12882
Sequence similarities	Belongs to the dihydropyrimidine dehydrogenase family. Contains 3 4Fe-4S ferredoxin-type domains.

Ontologies

Keywords
Domain	Repeat
Ligand	4Fe-4S FAD FMN Flavoprotein Iron Iron-sulfur Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
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
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW dihydroorotate oxidase activity Inferred from electronic annotation. Source: InterPro dihydropyrimidine dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1053

1053

Probable dihydropyrimidine dehydrogenase [NADP+]

PRO_0000355577

Regions

Domain

84 – 115

32

4Fe-4S ferredoxin-type 1

Domain

949 – 981

33

4Fe-4S ferredoxin-type 2

Domain

983 – 1013

31

4Fe-4S ferredoxin-type 3

Sites

Metal binding

958

1

Iron-sulfur 1 (4Fe-4S) Potential

Metal binding

961

1

Iron-sulfur 1 (4Fe-4S) Potential

Metal binding

964

1

Iron-sulfur 1 (4Fe-4S) Potential

Metal binding

968

1

Iron-sulfur 1 (4Fe-4S) Potential

Metal binding

992

1

Iron-sulfur 2 (4Fe-4S) Potential

Metal binding

995

1

Iron-sulfur 2 (4Fe-4S) Potential

Metal binding

998

1

Iron-sulfur 2 (4Fe-4S) Potential

Metal binding

1002

1

Iron-sulfur 2 (4Fe-4S) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

A8XKG6 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: AF22FB28C82FD43E
Show »

FASTA

1,053

114,672

        10         20         30         40         50         60 
MTPKPNTSNP NVGLPLLSKD SPDIESLLIL NPKVQSKANA VPSAVTKKNK HNWKRNEEKG 

        70         80         90        100        110        120 
CGASCGESKL KNDFRDIKHT TLSERGALKE AMRCLKCADA PCQKSCPTQL DIKSFITSIS 

       130        140        150        160        170        180 
NKNYYGAARA ILSDNPLGLT CGMICPTSDL CVGSCNLQAS EEGAINIGGL QQYACDVFKQ 

       190        200        210        220        230        240 
MNVRQIVSKE VRENRNASHK EQIALIGCGP ASISCASFLA RLGYTDITIY EKRAYIGGLS 

       250        260        270        280        290        300 
SAEIPQFRLP YDVVDFEIQL ARDVGVKIET NRSLCKEDIT LDKLKSQGAA AVFIGIGNPE 

       310        320        330        340        350        360 
PKIDPLFEGL TIENGFYTSK NYLPAVAAAS KPGMCGCKRT PLPTMRGRVV VLGAGDTAMD 

       370        380        390        400        410        420 
CATSALRCGA SRVTIAFRKG FTGIRAVPEE MEAAKEEKCE FLPFSAPRKI NVKDGRIVSI 

       430        440        450        460        470        480 
EFNKTEQDDN GKWYEDEEQI VILKCDYVIS AFGSTLKEDT VLSALQPCKL NKWGGIEVDS 

       490        500        510        520        530        540 
TTQQTSEAWV FAGGDVAGVA ETTVESVNDG KTLMDLTFKI QIAAWNMHRY IQAKHGNVLG 

       550        560        570        580        590        600 
ETPELPKFFT PIDEVDISVD MCGVKFENPF GLASAPPTTS GPMCRRAFEQ GWGFILTKTY 

       610        620        630        640        650        660 
GLDKDLVTNV SPRIVRGSTS GPLYGPNQGS FMNIELISEK SCEYWLQCIR ELKRDHPTKI 

       670        680        690        700        710        720 
VVASIMCVYN KEDWIELATK SEAAGADILE LNLSCPHGMG EKGMGLACGQ SPEIVKEICR 

       730        740        750        760        770        780 
WVRACVKIPF FPKMTPNITD VREIARAARD GGASGVTATN TVSSLMHMKA DGNAWPAIGN 

       790        800        810        820        830        840 
TKRTTYGGMS GSAIRPIAMK AVSSIANELD GFPIMATGGI ESAETGLGFL MAGASVLQVC 

       850        860        870        880        890        900 
SAVQNQDFTV VEDYCTGLKA LLYLSGAESL KEWDGQSPPV EKHQKGKPIL LQGQKNMPFF 

       910        920        930        940        950        960 
GKFRDEREKL EALKLSESNL LDTDNYHFAS RPDTQVARVP TVEDVIEHEV AIIDHDMCIN 

       970        980        990       1000       1010       1020 
CGKCYMTCND SGYQAITFDA VTHQPHVTED DCTGCTLCYS VCPIPECIQM VPRKGPWKAP 

      1030       1040       1050 
KRGVKPTVEP GTPKVVKVDQ RGRVILESTG GMQ

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References

[1]

"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics."
Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W.

Waterston R.H.
PLoS Biol. 1:166-192(2003) [PubMed: 14624247] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AF16.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CAAC02000521 Genomic DNA. Translation: CAP33140.2.
3D structure databases
ProteinModelPortal	A8XKG6.
ModBase	Search...
Protein-protein interaction databases
STRING	A8XKG6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
WormBase	CBG14689; CBP27928; WBGene00035110.
Phylogenomic databases
HOGENOM	HBG314257.
Family and domain databases
InterPro	IPR001450. 4Fe4S-bd_dom. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR013785. Aldolase_TIM. IPR005720. Dihydroorotate_DH. IPR012135. Dihydroorotate_DH_1_2. IPR012285. Fum_reductase_C. IPR009051. Helical_ferredxn. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA: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.
Pfam	PF01180. DHO_dh. 1 hit. PF12838. Fer4_7. 1 hit. [Graphical view]
SUPFAM	SSF46548. Helical_ferredxn. 1 hit.
TIGRFAMs	TIGR01037. PyrD_sub1_fam. 1 hit.
PROSITE	PS00198. 4FE4S_FER_1. 1 hit. PS51379. 4FE4S_FER_2. 3 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DPYD_CAEBR

Accession

Primary (citable) accession number: A8XKG6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	December 16, 2008
Last modified:	January 25, 2012
This is version 36 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents