Q75CE1 (PYRD_ASHGO) 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:	URA9
Ordered Locus Names:	ACL035C

Organism

Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Complete proteome]

Taxonomic identifier

284811 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor By similarity.
Catalytic activity	(S)-dihydroorotate + a quinone = orotate + a quinol.
Cofactor	Binds 1 FMN per subunit By similarity.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular location	Mitochondrion inner membrane By similarity; Single-pass membrane protein Potential.
Sequence similarities	Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

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
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
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 electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 444		Dihydroorotate dehydrogenase (quinone), mitochondrial		PRO_0000029890
Regions
	Transmembrane	34 – 56	23	Helical; Potential
	Nucleotide binding	124 – 128	5	FMN By similarity
	Nucleotide binding	406 – 407	2	FMN By similarity
	Region	173 – 177	5	Substrate binding By similarity
	Region	250 – 255	6	Substrate binding By similarity
	Region	330 – 331	2	Substrate binding By similarity
Sites
	Active site	253	1	Nucleophile By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	148	1	FMN By similarity
	Binding site	220	1	FMN By similarity
	Binding site	250	1	FMN By similarity
	Binding site	301	1	FMN By similarity
	Binding site	329	1	FMN; via carbonyl oxygen By similarity
	Binding site	355	1	FMN; via amide nitrogen By similarity
	Binding site	385	1	FMN; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q75CE1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 27E890B278E04733	FASTA	444	48,288
	10 20 30 40 50 60 MSYKMFGRCR TACFRSPNLF AANKGMPLQA SVAGGASRYI IGTASVLVGA MAGFYIMNSR 70 80 90 100 110 120 SAIHEYVSCP LVRLVTPDAE DGHKLGIWFL KYGLAPKLMF DKDDPVLKVE VFGKTMSNPI 130 140 150 160 170 180 GCAAGLDKDG EAIDGIAQSG FGYVEIGTVT PLAQPGNPKP RFFRLPMDEA VINRYGFNSS 190 200 210 220 230 240 GHKKVYDNVL SRVRQFLGAY FRDDTVNSLA LYKDKLLGIN LGKNKNGDEV EDYLRGVEKF 250 260 270 280 290 300 QSLADVLVIN VSSPNTPGLR DLQQEGRLTE LLSMIVAKRN SLINEGNVLG ASTHKPPVLV 310 320 330 340 350 360 KIAPDLTEPE LQSIAEAAKK SSIDGIIVSN TTIQRPDSLY TVDEELKNQA GGLSGKPVKP 370 380 390 400 410 420 FALKALRTIH QYTKDTNLVL VGCGGISSGQ DAIEFAKAGA HFVQLYTAYA YRGPGLIARI 430 440 KDEVTEELRN EGKTWMEIIG QDAK

References

[1]

"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome." Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P. Science 304:304-307(2004) [PubMed: 15001715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016816 Genomic DNA. Translation: AAS51193.1.
RefSeq	NP_983369.1. NM_208722.1.
3D structure databases
ProteinModelPortal	Q75CE1.
ModBase	Search...
Protein-protein interaction databases
STRING	Q75CE1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4619494.
GenomeReviews	Gene locus ACL035C in contig AE016816_GR.
KEGG	ago:AGOS_ACL035C.
NMPDR	fig|33169.1.peg.1014.
Organism-specific databases
AGD	ACL035C.
Phylogenomic databases
eggNOG	fuNOG05791.
HOGENOM	HBG351027.
OMA	AALNRMG.
OrthoDB	EOG4NS6M1.
PhylomeDB	Q75CE1.
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_ASHGO

Accession

Primary (citable) accession number: Q75CE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	July 5, 2004
Last modified:	December 14, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program