Dihydroorotate dehydrogenase (quinone), mitochondrial precursor - Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast)

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Q6SZS5 (PYRD_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 67. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	CAGL0M12881g

Organism

Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

284593 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	439 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 – 22

Mitochondrion Potential

Chain

23 – 439

417

Dihydroorotate dehydrogenase (quinone), mitochondrial

PRO_0000029892

Regions

Transmembrane

37 – 53

Helical; Potential

Nucleotide binding

119 – 123

FMN By similarity

Nucleotide binding

401 – 402

FMN By similarity

Region

168 – 172

Substrate binding By similarity

Region

245 – 250

Substrate binding By similarity

Region

325 – 326

Substrate binding By similarity

Sites

Active site

248

Nucleophile By similarity

Binding site

123

Substrate By similarity

Binding site

143

FMN By similarity

Binding site

215

FMN By similarity

Binding site

245

FMN By similarity

Binding site

296

FMN By similarity

Binding site

324

FMN; via carbonyl oxygen By similarity

Binding site

350

FMN; via amide nitrogen By similarity

Binding site

380

FMN; via amide nitrogen By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q6SZS5 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: E116514C9B8CCBB4
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FASTA

439

48,217

        10         20         30         40         50         60 
MMHRVGFNVI GRRSFFTVNA RRQVLKSSFM GLKPLQLTAL LLAGSAGYLY FMNARSAIHE 

        70         80         90        100        110        120 
YVVCPVVRLI TPDPENGHKL GIWCFKWGLS PKLYFDKDPE SLHVNVFGTT MTNPIGCAAG 

       130        140        150        160        170        180 
LDKDAEAIDG IMPTGFGYME VGSVTPVAQP GNPRPRFFRL PADDAVINRY GFNSSGHDVV 

       190        200        210        220        230        240 
YNNLMKRVNK FLNSYFGDKS IDKLSLYKDK LLAVNLGKNK NGDEVKDYLK GVEKFQSLAD 

       250        260        270        280        290        300 
VLVINVSSPN TPGLRDLQNE AKLTNLLSEI ITKRDSQSNK PNALGKQNHK PPVLVKIAPD 

       310        320        330        340        350        360 
LTEPELQSIV EAAKKSKVDG IIVSNTTIQR PNTLKTQDET LRNQVGGLSG KPLKPFALKA 

       370        380        390        400        410        420 
MKAVSKYAKD SDLVLVGCGG ISSGKDAIEF AKAGATFVQL YTSYAYVGPA LIARIKDEVA 

       430 
EELKKEGKTW MEIIGEDNK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Contribution of horizontal gene transfer to the evolution of Saccharomyces cerevisiae." Hall C.R., Brachat S., Dietrich F.S. Eukaryot. Cell 4:1102-1115(2005) [PubMed: 15947202] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY444340 Genomic DNA. Translation: AAR17523.1. CR380959 Genomic DNA. Translation: CAG62883.1.
RefSeq	XP_449903.1. XM_449903.1.
3D structure databases
ProteinModelPortal	Q6SZS5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2891454.
GenomeReviews	Gene locus CAGL0M12881g in contig CR380959_GR.
KEGG	cgr:CAGL0M12881g.
Phylogenomic databases
eggNOG	fuNOG05791.
HOGENOM	HBG351027.
OMA	AALNRMG.
OrthoDB	EOG4NS6M1.
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]
PIRSF	PIRSF000164. DHO_oxidase. 1 hit.
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_CANGA

Accession

Primary (citable) accession number: Q6SZS5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	July 5, 2004
Last modified:	December 14, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents