Reviewed, UniProtKB/Swiss-Prot Q55FT1 (DPYD_DICDI)

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:	pyd1
ORF Names:	DDB_G0267966

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	1009 AA.
Sequence status	Complete.
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.
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
Technical term	Complete 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 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 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 – 1009	1009	Dihydropyrimidine dehydrogenase [NADP+]		PRO_0000327500
Regions
	Domain	69 – 99	31	4Fe-4S ferredoxin-type 1
	Domain	932 – 964	33	4Fe-4S ferredoxin-type 2
	Domain	965 – 995	31	4Fe-4S ferredoxin-type 3
	Nucleotide binding	334 – 350	17	NADP Potential
	Nucleotide binding	468 – 479	12	FAD Potential
	Region	659 – 676	18	Uracil binding Potential
Sites
	Metal binding	941	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	944	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	947	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	951	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	974	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	977	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	980	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	984	1	Iron-sulfur 2 (4Fe-4S) Potential
Experimental info
	Sequence conflict	68	1	E → G in AAQ11981. Ref.1
	Sequence conflict	234	1	R → H in AAQ11981. Ref.1
	Sequence conflict	532	1	S → C in AAQ11981. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q55FT1-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: CBC49049106B86B7	FASTA	1,009	110,444
	10 20 30 40 50 60 MTGHTGDVSQ VHDIEILALN PTVNKHATFK PTIVSKKDKE NWARLDHCKK GCELKNDFED 70 80 90 100 110 120 VKPTTLTERG ALFESARCLK CADAPCQKGC PTQLDIKSFI SSISTKNYYG AAKTIFSDNP 130 140 150 160 170 180 LGLTCGMVCP VSSLCQYGCN LAATEEGPIN IGGLQQFATE VFKKMNIPQI RDPSLTPLSQ 190 200 210 220 230 240 LPESYKAKIA LIGCGPTSIS CATFLGRLGY TDVTIFEKEQ YLGGLSSSEI PNYRLNYEVV 250 260 270 280 290 300 EFEIKLMKDL GVKVEYGKRL GENGFTVESL QKQGYEAIYL GIGMPEPKID PVFNELTSDQ 310 320 330 340 350 360 GFFSSKEFLP KVSKASKAGM CGCKSQLPQL NGRVIVLGAG DTAFDCATSA FRCGASRVTV 370 380 390 400 410 420 CFRRGFSDMR AVPEEVDIAK DERCEFLPYV LPKQVIKRDG KVVAMEFYKT EKGDDGNYSV 430 440 450 460 470 480 DEDQFFRVKC DYIISAFGSQ IGSVAESCSP LQFNKWGTAD IDPMTMTSKH AEWLFCGGDL 490 500 510 520 530 540 VGNGTTVEAV NDGKTASWNI HKYLQSLHGI PIPDGPPQLP NFFTPIDLVD ISVEMCGMKF 550 560 570 580 590 600 PNPFGLASAT PATSAAMIRR SFEQGWGFAV TKTFSLDKDL VTNVSPRIVR GTTSGHHFGP 610 620 630 640 650 660 GQGAFLNIEL ISEKTCHYWC KAIGELKRDF PDRIVIASIM CGFNKEDWTQ LAKMAEASGA 670 680 690 700 710 720 DGIELNLSCP HGMGEKGMGL ACGQDTELVF HICQWVRAAT RLPFFAKLTP NVTEIKEIAK 730 740 750 760 770 780 AAHDGGADGV TAINTVSGLM GLKGDSNAWP AIGDEKRTTY GGVSGNATRP IALRAVSSIR 790 800 810 820 830 840 KSLPDYPIMA TGGADSADAT IQFLHCGASV VQICSSVQNQ DFTVVQDYIT GLKTYLYMQS 850 860 870 880 890 900 REDLLQWDGQ SPPNEIINKN PKLKGLPKFG KYLLERNRID TEEKQNIDLQ KVKNPLVPSP 910 920 930 940 950 960 NPTHPVPSLK DQINRAIPRI GRHDDLKRDQ QVVALIDEDK CINCGKCYMT CNDSGYQAIK 970 980 990 1000 FDGKTHIPLV TDLCTGCDLC LSVCPVPDCI TMVPRETIYV PDRGLTVQN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Dihydropyrimidine dehydrogenases and the evolution of the pyrimidine degradation pathway." Gojkovic Z., Sandrini M.P.B., Piskur J. Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF545064 mRNA. Translation: AAQ11981.1. AAFI02000003 Genomic DNA. Translation: EAL73436.1.
RefSeq	XP_647452.1.
3D structure databases
HSSP	HSSP built from PDB template 1GTE based on UniProtKB Q28943.
SMR	Q55FT1. Positions 11-1005.
ModBase	Search...
Protein-protein interaction databases
STRING	Q55FT1.
Genome annotation databases
GeneID	8616259.
KEGG	ddi:DDB_0231100.
Organism-specific databases
dictyBase	DDB_G0267966. pyd1.
Phylogenomic databases
eggNOG	KOG1799.
HOGENOM	HBG314257.
OMA	IGIGLPE.
PhylomeDB	Q55FT1.
Enzyme and pathway databases
BRENDA	1.3.1.2. 424.
Family and domain databases
InterPro	IPR017896. 4Fe4S_Fe-S-bd. 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. 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. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PRINTS	PR00419. ADXRDTASE.
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_DICDI

Accession

Primary (citable) accession number: Q55FT1
Secondary accession number(s): Q5ZQQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	February 9, 2010
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)