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B3PNN8 (PYRD_RHIE6) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. 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:RHECIAT_CH0000610
OrganismRhizobium etli (strain CIAT 652) [Complete proteome] [HAMAP]
Taxonomic identifier491916 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Rhizobium

Protein attributes

Sequence length362 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 – 362362Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_1000100277

Regions

Nucleotide binding62 – 665FMN By similarity
Nucleotide binding316 – 3172FMN By similarity
Region111 – 1155Substrate binding By similarity
Region244 – 2452Substrate binding By similarity

Sites

Active site1731Nucleophile By similarity
Binding site661Substrate By similarity
Binding site861FMN; via amide nitrogen By similarity
Binding site1391FMN By similarity
Binding site1701FMN By similarity
Binding site1701Substrate By similarity
Binding site1751Substrate By similarity
Binding site2151FMN By similarity
Binding site2431FMN; via carbonyl oxygen By similarity
Binding site2661FMN; via amide nitrogen By similarity
Binding site2951FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
B3PNN8 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 53D47EBBBBF10DA9

FASTA36238,943
        10         20         30         40         50         60 
MIDPFKRLAR KGLFLFDPET AHGMSIAALK SGLVPACQIT PDPRLRQTVA GLTFENPLGM 

        70         80         90        100        110        120 
AAGYDKNAEV PEALLRLGFG FTEIGTVTPR PQSGNPRPRI FRLVEDEAVI NRLGFNNEGH 

       130        140        150        160        170        180 
EAAFERLSAL TGKGVVGVNI GANKDSEDRI TDYVAGIRCF YSVARYFTAN ISSPNTPGLR 

       190        200        210        220        230        240 
DLQARESLAA LLSAVLAARD EMAERSGRKI PVFLKIAPDL TEEGMDDIAA EALAHPLDGL 

       250        260        270        280        290        300 
IVSNTTLSRE GLKDQRQAKE TGGLSGVPLF EKSTAVLARM RKRVGAALPI IGVGGVSSAE 

       310        320        330        340        350        360 
TALEKIRAGA DLVQLYSCMV YEGPGLPGNI VRGLSGLLDR EKAGSIRELR DSRLDYWAAR 


KV

« Hide

References

[1]"Genome diversity and DNA divergence of Rhizobium etli."
Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J., Palacios R., Davila G.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CIAT 652.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001074 Genomic DNA. Translation: ACE89601.1.
RefSeqYP_001976779.1. NC_010994.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB3PNN8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6398698.
GenomeReviewsGene locus pyrD in contig CP001074_GR.
KEGGrec:RHECIAT_CH0000610.
PATRIC23094672. VBIRhiEtl120572_0600.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG351027.
OMASYVTVNI.
ProtClustDBPRK05286.

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_RHIE6
AccessionPrimary (citable) accession number: B3PNN8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 2, 2008
Last modified: January 25, 2012
This is version 29 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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