Reviewed, UniProtKB/Swiss-Prot Q5R895 (DPYD_PONAB)

Names and origin

Protein names

Recommended 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

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	1025 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine By similarity.
Catalytic activity	5,6-dihydrouracil + NADP+ = uracil + NADPH.
Cofactor	Binds 2 4Fe-4S clusters By similarity. FAD By similarity. FMN By similarity.
Enzyme regulation	Inactivated by 5-iodouracil By similarity.
Pathway	Amino-acid biosynthesis; beta-alanine biosynthesis.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the dihydropyrimidine dehydrogenase family. Contains 3 4Fe-4S ferredoxin-type domains.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Repeat
Ligand	4Fe-4S FAD FMN Flavoprotein Iron Iron-sulfur Metal-binding NADP
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
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
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 sequence or structural similarity. Source: UniProtKB electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1025	1025	Dihydropyrimidine dehydrogenase [NADP+]		PRO_0000327503
Regions
	Domain	69 – 100	32	4Fe-4S ferredoxin-type 1
	Domain	944 – 976	33	4Fe-4S ferredoxin-type 2
	Domain	978 – 1007	30	4Fe-4S ferredoxin-type 3
Sites
	Metal binding	953	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	956	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	959	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	963	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	986	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	989	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	992	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	996	1	Iron-sulfur 2 (4Fe-4S) Potential
Amino acid modifications
	Modified residue	384	1	N6-acetyllysine By similarity
	Modified residue	577	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5R895-1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 39FAE483BA9983B6	FASTA	1,025	111,468
	10 20 30 40 50 60 MAPVLSKDSA DIESILALNP RTQTHATLRS TSAKKLDKKH WKRNPDKNCF NCEKLENNFD 70 80 90 100 110 120 DIKHTTLGER GALREAMRCL KCADAPCQKS CPTNLDIKSF ITSIANKNYY GAAKMIFSDN 130 140 150 160 170 180 PLGLTCGMVC PTPDLCVGGC NLYATEEGPI NIGGLQQFAT EVFKAMSIPQ IRNPFLPPPE 190 200 210 220 230 240 KMSEAYSAKI ALFGAGPASI SCASFLARLG YSDITIFEKQ EYVGGLSTSE IPQFRLPYDV 250 260 270 280 290 300 VNFEIELMKD LGVKIICGKS LSVNEMTLST LKEKGYKAAF IGIGLPEPNK DAIFQGLTQD 310 320 330 340 350 360 QGFYTSKDFL PLVAKGSKAG MCACHSPLPS IRGVVIVLGA GDTAFDCATS ALRCGARRVF 370 380 390 400 410 420 IVFRKGFVNI RAVPEEMELA KEEKCEFLPF LSPRKVIVKG GRIVAMQFVR TEQDETGKWN 430 440 450 460 470 480 EDEDQMVHLK ADVVISAFGS VLSDPKVKEA MSPIKFNRWG LPEVDPETMQ TSEAWVFAGG 490 500 510 520 530 540 DVVGLANTTV ESVNDGKQAS WYIHKYIQSQ YGASVSAKPE LPLFYTAIDL VDISVEMAGL 550 560 570 580 590 600 KFINPFGLAS ATPATSTSMI RRAFEAGWGF ALTKTFSLDK DIVTNVSPRI VRGTTSGPMY 610 620 630 640 650 660 GPGQSSFLNI ELISEKTAAY WCQSVTELKA DFPDNIVIAS IMCSYNKNDW TELAKKSEDS 670 680 690 700 710 720 GADALELNLS CPHGMGERGM GLACGQDPEL VRNICRWVRQ AVQIPFFAKL TPNVTDIVSI 730 740 750 760 770 780 ARAAKEGGAN GVTATNTVSG LMGLKSDGTP WPAVGIAKRT TYGGVSGTAI RPIALRAVTS 790 800 810 820 830 840 TARALPGFPI LATGGIDSAE SGLQFLHSGA SVLQVCSAIQ NQDFTVIEDY CTGLKALLYL 850 860 870 880 890 900 KSIEELQDWD GQSPATVSHQ KGKPVPRIAE LMDKKLPSFG PYLEQRKKII AENKIRLKEQ 910 920 930 940 950 960 NIASSPHKRN CFIPKRPVPT IKDVIGKALQ YLGTFGELSN VEQVVAMIDE EMCINCGKCY 970 980 990 1000 1010 1020 MTCNDSGYQA IQFDPETHLP TITDTCTGCT LCLSVCPIVD CIKMVSRTTP YEPKRGVPLS VNPVC

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR859859 mRNA. Translation: CAH92015.1.
RefSeq	NP_001126169.1.
UniGene	Pab.11422
3D structure databases
SMR	Q5R895. Positions 2-1017.
ModBase	Search...
Genome annotation databases
GeneID	100173131.
Organism-specific databases
CTD	100173131.
Phylogenomic databases
HOVERGEN	Q5R895.
Enzyme and pathway databases
BRENDA	1.3.1.2. 269192.
Family and domain databases
InterPro	IPR017896. 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. [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. PF00037. Fer4. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PRINTS	PR00419. ADXRDTASE.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
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_PONAB

Accession

Primary (citable) accession number: Q5R895

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	December 21, 2004
Last modified:	October 13, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)