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Q472J6 (PYRD_CUPPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydroorotate dehydrogenase (quinone)
EC=1.3.5.2
Alternative name(s):
DHOdehase
Short name=DHOD
Short name=DHODase
Dihydroorotate oxidase
Gene names
Name:pyrD
Ordered Locus Names:Reut_A1317
OrganismCupriavidus pinatubonensis (strain JMP134 / LMG 1197) (Alcaligenes eutrophus) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier264198 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor By similarity. HAMAP MF_00225

Catalytic activity

(S)-dihydroorotate + a quinone = orotate + a quinol. HAMAP MF_00225

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP MF_00225

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. HAMAP MF_00225

Subunit structure

Monomer By similarity. HAMAP MF_00225

Subcellular location

Cell membrane; Peripheral membrane protein By similarity HAMAP MF_00225.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCell membrane
Membrane
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete 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 componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondihydroorotate oxidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_1000024211

Regions

Nucleotide binding65 – 695FMN By similarity
Nucleotide binding324 – 3252FMN By similarity
Region114 – 1185Substrate binding By similarity
Region252 – 2532Substrate binding By similarity

Sites

Active site1811Nucleophile By similarity
Binding site691Substrate By similarity
Binding site891FMN; via amide nitrogen By similarity
Binding site1451FMN By similarity
Binding site1781FMN By similarity
Binding site1781Substrate By similarity
Binding site1831Substrate By similarity
Binding site2231FMN By similarity
Binding site2511FMN; via carbonyl oxygen By similarity
Binding site2741FMN; via amide nitrogen By similarity
Binding site3031FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q472J6 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 9B317973F51EECC9

FASTA34436,740
        10         20         30         40         50         60 
MLNALYPLFR PALFSMDAED AHHFTLNNLL RAQRLGLGGC IGNRIAEDPR TVMGVRFPNP 

        70         80         90        100        110        120 
VGLAAGLDKD GAYIDGLASF GFGFIEVGTV TPRAQPGNPR PRMFRLPQAD ALINRMGFNN 

       130        140        150        160        170        180 
GGVDAFIANV KASRWKAEGG VLGLNIGKNA DTPIERAADD YLYCLERVYP HASYVTVNIS 

       190        200        210        220        230        240 
SPNTKNLRQL QGASELDSLL STLKAAQQRL ADQHKRYVPV ALKIAPDLDA DQIGNIGDAL 

       250        260        270        280        290        300 
VRHKIDGVIA TNTTISRDAV KGLPHAEEAG GLSGRPVFEQ STHVVRALRQ VVGDAVPIIG 

       310        320        330        340 
VGGIFSGADA RAKIDAGAKL VQVYSGLIYR GPTLVRDCAA ALRA

« Hide

References

[1]"Complete sequence of chromosome 1 of Ralstonia eutropha JMP134."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JMP134 / LMG 1197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000090 Genomic DNA. Translation: AAZ60687.1.
RefSeqYP_295531.1. NC_007347.1.

3D structure databases

ProteinModelPortalQ472J6.
SMRQ472J6. Positions 5-341.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ472J6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3610700.
GenomeReviewsGene locus Reut_A1317 in contig CP000090_GR.
KEGGreu:Reut_A1317.
NMPDRfig|264198.3.peg.1978.
PATRIC20228137. VBIRalEut24049_1935.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG351027.
OMASYVTVNI.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycREUT264198:REUT_A1317-MONOMER.

Family and domain databases

HAMAPMF_00225. DHO_dh_type2.
[Tree]
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.
KOK00226.
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...

Entry information

Entry namePYRD_CUPPJ
AccessionPrimary (citable) accession number: Q472J6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 13, 2005
Last modified: January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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