Reviewed, UniProtKB/Swiss-Prot Q28007 (DPYD_BOVIN)

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

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	1025 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. FAD. FMN.
Enzyme regulation	Inactivated by 5-iodouracil.
Pathway	Amino-acid biosynthesis; beta-alanine biosynthesis.
Subunit structure	Homodimer By similarity.
Subcellular location	CytoplasmBy 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	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	'de novo' pyrimidine base 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 component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADP 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1025	1025	Dihydropyrimidine dehydrogenase [NADP+]		PRO_0000079996
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	577	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q28007-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 5B55F93A06C47F4F	FASTA	1,025	111,697
	10 20 30 40 50 60 MAPVLSKDVA DIESILALNP RTQSRATLRS TLAKKLDKKH WKRNPDKNCF NCEKLENNFD 70 80 90 100 110 120 DIKHTTLGER GALREAMRCL KCADAPCQKS CPTNLDIKSF ITSISNKNYY GAAKMIFSDN 130 140 150 160 170 180 PLGLTCGMVC PTSDLCVGGC NLYATEEGPI NIGGLQQYAT EVFKAMNIPQ IRNPSLPPPE 190 200 210 220 230 240 KMPEAYSAKI ALLGAGPASI SCASFLARLG YNDITIFEKQ EYVGGISTSE IPQFRLPYDV 250 260 270 280 290 300 VNFEIELMKD LGVKIICGKS LSVNDITLST LKEEGYKAAF IGIGLPEPKK DHIFQGLTQD 310 320 330 340 350 360 QGFYTSKDFL PLVAKSSKAG MCACHSPLLS IRGTVIVLGA GDTAFDCATS ALRCGARRVF 370 380 390 400 410 420 IVFRKGFVNI RAVPEEVELA REEKCEFLPF LSPRKVIVKG GRIVAMQFVR TEQDETGKWN 430 440 450 460 470 480 EDGDQIACLK ADVVISAFGS VLSDPKVKEA LSPIKFNRWD LPEVDPETMQ TSEPWVFAGG 490 500 510 520 530 540 DVVGIANTTV EAVNDGKQAS WYIHRYIQSQ YGASVSAKPE LPLFYTPIDL VDISVEMAAL 550 560 570 580 590 600 KFTNPFGLAS ATPTTSSSMI RRAFEAGWAF ALTKTFSLDK DIVTNVSPRI IRGTTSGPMY 610 620 630 640 650 660 GPGQSSFLNI ELISEKTAAY WCQSVTELKA DFPDNIVIAS IMCSYNRNDW MELSRKAEAS 670 680 690 700 710 720 GADALELNLS CPHGMGERGM GLACGQDPEL VRNICRWVRQ AVRIPFFAKL TPNVTDIVSI 730 740 750 760 770 780 ARAAKEGGAN GVTATNTVSG LMGLKADGTP WPAVGREKRT TYGGVSGTAI RPIALRAVTT 790 800 810 820 830 840 IARALPEFPI LATGGIDSAE SGLQFLHGGA SVLQVCSAIQ NQDFTIIQDY CTGLKALLYL 850 860 870 880 890 900 KSIEELQDWD GQSPATKSHQ KGKPVPCIAE LVGKKLPSFG PYLEKCKKII AEEKLRLKKE 910 920 930 940 950 960 NVTVLPLERN HFIPKKPIPS VKDVIGKALQ YLGTYGELNN TEQVVAVIDE EMCINCGKCY 970 980 990 1000 1010 1020 MTCNDSGYQA IQFDPETHLP TVTDTCTGCT LCLSVCPIID CIKMVSRTTP YEPKRGLPLA VNPVS

References

[1]	"cDNA cloning of bovine liver dihydropyrimidine dehydrogenase." Albin N., Johnson M.R., Diasio R.B. DNA Seq. 6:243-250(1996) [PubMed: 8912928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Inactivation of dihydropyrimidine dehydrogenase by 5-iodouracil." Porter D.J.T., Chestnut W.G., Taylor L.C.E., Merrill B.M., Spector T. J. Biol. Chem. 266:19988-19994(1991) [PubMed: 1939061] [Abstract] Cited for: PROTEIN SEQUENCE OF 668-678, ENZYME REGULATION. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U20981 mRNA. Translation: AAB40985.1.
PIR	A44626.
RefSeq	NP_776466.1.
UniGene	Bt.97060
3D structure databases
HSSP	HSSP built from PDB template 1GTE based on UniProtKB Q28943.
SMR	Q28007. Positions 2-1017.
ModBase	Search...
Genome annotation databases
Ensembl	ENSBTAG00000031358. Bos taurus. [Contig view]
GeneID	281124.
KEGG	bta:281124.
Phylogenomic databases
HOVERGEN	Q28007.
Family and domain databases
InterPro	IPR001450. 4Fe4S_Fe_S_bd. IPR000759. Adrndx_reductase. IPR013785. Aldolase_TIM. IPR005720. DHO_DHase_1_core. IPR001295. Dihydroorotate_DHase_core. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR012285. Fum_reductase_C. IPR016040. NAD(P)-bd. IPR000103. Pyridine_nuc-diS_OxRdtase_2. [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	PR00353. 4FE4SFRDOXIN. PR00419. ADXRDTASE. PR00368. FADPNR. PR00469. PNDRDTASEII.
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_BOVIN

Accession

Primary (citable) accession number: Q28007
Secondary accession number(s): Q9TRV4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	November 25, 2008
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)