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O35435 (PYRD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydroorotate dehydrogenase (quinone), mitochondrial
Short name=DHOdehase
EC=1.3.5.2
Alternative name(s):
Dihydroorotate oxidase
Gene names
Name:Dhodh
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.

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.

Subunit structure

Monomer By similarity.

Subcellular location

Mitochondrion inner membrane; Single-pass membrane protein By similarity.

Post-translational modification

The uncleaved transit peptide is required for mitochondrial targeting and proper membrane integration By similarity.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 395395Dihydroorotate dehydrogenase (quinone), mitochondrial
PRO_0000029885
Transit peptide1 – 1010Mitochondrion; not cleaved By similarity

Regions

Topological domain1 – 1010Mitochondrial matrix Potential
Transmembrane11 – 3020Helical; Potential
Topological domain31 – 395365Mitochondrial intermembrane Potential
Nucleotide binding95 – 995FMN By similarity
Nucleotide binding355 – 3562FMN By similarity
Region144 – 1485Substrate binding By similarity
Region211 – 2166Substrate binding By similarity
Region283 – 2842Substrate binding By similarity

Sites

Active site2141Nucleophile By similarity
Binding site991Substrate By similarity
Binding site1191FMN By similarity
Binding site1801FMN By similarity
Binding site2111FMN By similarity
Binding site2541FMN By similarity
Binding site2821FMN; via carbonyl oxygen By similarity
Binding site3051FMN; via amide nitrogen By similarity
Binding site3341FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
O35435 [UniParc].

Last modified October 1, 2000. Version 2.
Checksum: 84F2D93D0646E39D

FASTA39542,700
        10         20         30         40         50         60 
MAWRQLRKRA LDAAIILGGG GLLFTSYLTA TGDDHFYAEY LMPALQRLLD PESAHRLAVR 

        70         80         90        100        110        120 
VISLGLLPRA TFQDSNMLEV RVLGHKFRNP VGIAAGFDKH GEAVDGLYKL GFGFVEVGSV 

       130        140        150        160        170        180 
TPQPQEGNPR PRVFRLPEDQ AVINRYGFNS HGLSAVEHRL RARQQKQTQL TTDGLPLGIN 

       190        200        210        220        230        240 
LGKNKTSVDA AADYVEGVRI LGPLADYLVV NVSSPNTAGL RSLQGKTELR RLLSKVLQER 

       250        260        270        280        290        300 
DALKGPQKPA VLVKIAPDLT AQDKEDIASV ARELGIDGLI ITNTTVSRPV GLQGALRSET 

       310        320        330        340        350        360 
GGLSGKPLRD LSTQTIREMY ALTQGTIPII GVGGVSSGQD ALEKIQAGAS LVQLYTALTF 

       370        380        390 
LGPPVVARVK RELEALLKER GFNTVTDAIG VDHRR

« Hide

References

« Hide 'large scale' references
[1]"Cloning of murine dihydroorotate dehydrogenase."
Knecht W., Ullrich A., Loeffler M.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF029667 mRNA. Translation: AAB82948.2.
BC019542 mRNA. Translation: AAH19542.1.
BC027829 mRNA. Translation: AAH27829.1.
BC045206 mRNA. Translation: AAH45206.1.
IPIIPI00130733.
RefSeqNP_064430.1. NM_020046.3.
UniGeneMm.23894.

3D structure databases

ProteinModelPortalO35435.
SMRO35435. Positions 37-395.
ModBaseSearch...

Protein-protein interaction databases

IntActO35435. 1 interaction.
STRINGO35435.

PTM databases

PhosphoSiteO35435.

Proteomic databases

PRIDEO35435.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000069058; ENSMUSP00000070303; ENSMUSG00000031730.
ENSMUST00000123605; ENSMUSP00000115934; ENSMUSG00000031730.
GeneID56749.
KEGGmmu:56749.
UCSCuc009nip.1. mouse.

Organism-specific databases

CTD1723.
MGIMGI:1928378. Dhodh.

Phylogenomic databases

eggNOGroNOG14604.
HOGENOMHBG351027.
HOVERGENHBG006898.
InParanoidO35435.
OMAAALNRMG.
PhylomeDBO35435.

Gene expression databases

ArrayExpressO35435.
BgeeO35435.
CleanExMM_DHODH.
GenevestigatorO35435.
GermOnlineENSMUSG00000031730. Mus musculus.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK00254.
PfamPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsTIGR01036. PyrD_sub2. 1 hit.
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio313274.
SOURCESearch...

Entry information

Entry namePYRD_MOUSE
AccessionPrimary (citable) accession number: O35435
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: October 1, 2000
Last modified: November 16, 2011
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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