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A4Z2G7 (PYRD_BRASO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 49. 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:BRADO6742
OrganismBradyrhizobium sp. (strain ORS278) [Complete proteome] [HAMAP]
Taxonomic identifier114615 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium

Protein attributes

Sequence length364 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-Rule MF_00225

Catalytic activity

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

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP-Rule MF_00225

Pathway

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

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00225

Subcellular location

Cell membrane; Peripheral membrane protein By similarity HAMAP-Rule 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' UMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

'de novo' pyrimidine nucleobase 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 – 364364Dihydroorotate dehydrogenase (quinone) HAMAP-Rule MF_00225
PRO_1000024156

Regions

Nucleotide binding61 – 655FMN By similarity
Nucleotide binding316 – 3172FMN By similarity
Region110 – 1145Substrate binding By similarity
Region243 – 2442Substrate binding By similarity

Sites

Active site1731Nucleophile By similarity
Binding site651Substrate By similarity
Binding site851FMN; via amide nitrogen By similarity
Binding site1391FMN By similarity
Binding site1701FMN By similarity
Binding site1701Substrate By similarity
Binding site1751Substrate By similarity
Binding site2141FMN By similarity
Binding site2421FMN; via carbonyl oxygen By similarity
Binding site2661FMN; via amide nitrogen By similarity
Binding site2951FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A4Z2G7 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: AA9B41BB22A0DF17

FASTA36439,208
        10         20         30         40         50         60 
MIRAFDQLSL PLLRWLDAED AHRLAIQGLK LLPAVKPRAD DAKLAVRAFG LNFPNPVGMA 

        70         80         90        100        110        120 
AGFDKNAEVP DALLRLGFGF VEIGSVTPRP QSGNPRPRLF RLERDEAVIN RMGFNNDGAE 

       130        140        150        160        170        180 
IVLRRLAGRA NQGGIVGVNV GANKDSADRV ADYVRLIETF APVASYFTVN ISSPNTPGLR 

       190        200        210        220        230        240 
NLQQASQLDD LLTKVLEARD RVRRKAGDTP VLLKIAPDLS LAELDDVVHV ARSRGVDGMI 

       250        260        270        280        290        300 
VSNTTLARPN SLREQMRAKE QGGLSGRPLF RLSTRMVAET FVRVEGAFPL IGVGGIDTGG 

       310        320        330        340        350        360 
AALTKIRAGA SLIQLYSSLV YKGLGLVESI KADLTSTLLR TGRESLSEIV GADAATITAE 


DWPV

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU234118 Genomic DNA. Translation: CAL80343.1.
RefSeqYP_001208558.1. NC_009445.1.

3D structure databases

ProteinModelPortalA4Z2G7.
ModBaseSearch...

Protein-protein interaction databases

STRING114615.BRADO6742.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL80343; CAL80343; BRADO6742.
GeneID5119338.
KEGGbra:BRADO6742.
PATRIC21229335. VBIBraSp122330_6453.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHOG000225103.
KOK00226.
OMAALNRMGF.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycBSP114615:GJN5-6433-MONOMER.
UniPathwayUPA00070; UER00946.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00225. DHO_dh_type2.
InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
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_BRASO
AccessionPrimary (citable) accession number: A4Z2G7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: May 1, 2013
This is version 49 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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