P32747 (PYRD_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydroorotate dehydrogenase (quinone), mitochondrial
Short name=DHOD
Short name=DHODase
Short name=DHOdehase
EC=1.3.5.2

Alternative name(s):
Dihydroorotate oxidase

Gene names

Name:	ura3
ORF Names:	SPAC57A10.12c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	443 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	In the de novo pyrimidine biosynthesic pathway, catalyzes the stereospecific oxidation of (S)-dihydroorotate to orotate with reduction of flavin and the transfer of electrons to ubiquinone, which is part of the repiratory chain. Does not use fumarate and NAD as electron acceptors. Ref.1 Ref.3 Ref.4
Catalytic activity	(S)-dihydroorotate + a quinone = orotate + a quinol.
Cofactor	Binds 1 FMN per subunit.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular location	Mitochondrion inner membrane; Single-pass membrane protein Potential Ref.1.
Sequence similarities	Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
Biophysicochemical properties	Kinetic parameters: KM=257 µM for (S)-dihydroorotate Ref.3 KM=109 µM for decylubiquinone Vmax=2 µmol/min/mg enzyme

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide Transmembrane Transmembrane helix
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	'de novo' pyrimidine base biosynthetic process Inferred from direct assay. Source: GeneDB_Spombe UMP biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dihydroorotate oxidase activity Inferred from direct assay. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 21	21	Mitochondrion Potential
	Chain	22 – 443	422	Dihydroorotate dehydrogenase (quinone), mitochondrial		PRO_0000029896
Regions
	Transmembrane	38 – 54	17	Helical; Potential
	Nucleotide binding	122 – 126	5	FMN By similarity
	Nucleotide binding	408 – 409	2	FMN By similarity
	Region	171 – 175	5	Substrate binding By similarity
	Region	264 – 269	6	Substrate binding By similarity
	Region	335 – 336	2	Substrate binding By similarity
Sites
	Active site	267	1	Nucleophile By similarity
	Binding site	126	1	Substrate By similarity
	Binding site	146	1	FMN By similarity
	Binding site	234	1	FMN By similarity
	Binding site	264	1	FMN By similarity
	Binding site	306	1	FMN By similarity
	Binding site	358	1	FMN; via amide nitrogen By similarity
	Binding site	387	1	FMN; via amide nitrogen By similarity
Amino acid modifications
	Modified residue	168	1	Phosphoserine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P32747 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: F58AB452E3A2F0D5	FASTA	443	48,296
	10 20 30 40 50 60 MYQRSLFRGV AQGLKRSSVR FQSTSSGSSN GNFFLRHWKL LSVIGSFTAG VAIYDMSDVR 70 80 90 100 110 120 SFIHGRIEMP LFHAFTTPEF SHRVAILAAS WGITPKDRVA DDPSLAVEVW GKKFCNPIGL 130 140 150 160 170 180 AAGFDKQADA ISGLLNFGFS YLEIGSVTPK PQPGNPKPRY FRLKPDLSVI NRYGFNSIGH 190 200 210 220 230 240 DAILAKIQKR VRKYIAKTSP QLLKQFDANP ASCTDPAVLG VPRSLIPNKF LGINLGKNKN 250 260 270 280 290 300 GNEIEDYVEG VRTFGNFADI LVINVSSPNT PGLRNLQKKS ALSTLLTAVV SERNKLNSPH 310 320 330 340 350 360 PPVLVKIAPD LNEEELTDIA DVLKKCKIDG VIVGNTTVQR PKTLKSTSHV EETGGLSGPP 370 380 390 400 410 420 LKPIALNTLR TLRKHLSSDI PIIGCGGISS GKDAIEYARA GATMVQVYTA LGYDGPVIAH 430 440 KIKQEILAEL KGKRWVDIIG KEE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts." Nagy M., Lacroute F., Thomas D. Proc. Natl. Acad. Sci. U.S.A. 89:8966-8970(1992) [PubMed: 1409592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[3]	"Two different dihydroorotate dehydrogenases from yeast Saccharomyces kluyveri." Zameitat E., Knecht W., Piskur J., Loeffler M. FEBS Lett. 568:129-134(2004) [PubMed: 15196933] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[4]	"Horizontal gene transfer promoted evolution of the ability to propagate under anaerobic conditions in yeasts." Gojkovic Z., Knecht W., Zameitat E., Warneboldt J., Coutelis J.-B., Pynyaha Y., Neuveglise C., Moeller K., Loeffler M., Piskur J. Mol. Genet. Genomics 271:387-393(2004) [PubMed: 15014982] [Abstract] Cited for: FUNCTION.
[5]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X65114 mRNA. Translation: CAA46230.1. CU329670 Genomic DNA. Translation: CAB08175.1.
PIR	A46248.
RefSeq	NP_593317.1. NM_001018748.1.
3D structure databases
ProteinModelPortal	P32747.
ModBase	Search...
Protein-protein interaction databases
STRING	P32747.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC57A10.12c.1; SPAC57A10.12c.1:pep; SPAC57A10.12c.
GeneID	2542781.
GenomeReviews	Gene locus ura3 in contig CU329670_GR.
KEGG	spo:SPAC57A10.12c.
NMPDR	fig|4896.1.peg.3287.
Organism-specific databases
GeneDB_Spombe	SPAC57A10.12c.
Phylogenomic databases
eggNOG	fuNOG05791.
GeneTree	EFGT00050000005424.
HOGENOM	HBG351027.
OMA	AALNRMG.
OrthoDB	EOG4NS6M1.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001015-MONOMER.
Gene expression databases
ArrayExpress	P32747.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR012135. Dihydroorotate_DH_1_2. IPR005719. Dihydroorotate_DH_2. IPR001295. Dihydroorotate_DH_CS. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K00226.
Pfam	PF01180. DHO_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR01036. PyrD_sub2. 1 hit.
PROSITE	PS00911. DHODEHASE_1. 1 hit. PS00912. DHODEHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRD_SCHPO

Accession

Primary (citable) accession number: P32747

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	December 14, 2011
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program