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B9MIU2 (PYRD_ACIET) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 25. 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:Dtpsy_1650
OrganismAcidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)) [Complete proteome] [HAMAP]
Taxonomic identifier535289 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax

Protein attributes

Sequence length351 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 – 351351Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_1000195068

Regions

Nucleotide binding65 – 695FMN By similarity
Nucleotide binding329 – 3302FMN By similarity
Region114 – 1185Substrate binding By similarity
Region257 – 2582Substrate binding By similarity

Sites

Active site1861Nucleophile By similarity
Binding site691Substrate By similarity
Binding site891FMN; via amide nitrogen By similarity
Binding site1501FMN By similarity
Binding site1831FMN By similarity
Binding site1831Substrate By similarity
Binding site1881Substrate By similarity
Binding site2281FMN By similarity
Binding site2561FMN; via carbonyl oxygen By similarity
Binding site2791FMN; via amide nitrogen By similarity
Binding site3081FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
B9MIU2 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 9215B7FB03783140

FASTA35137,375
        10         20         30         40         50         60 
MSLLPYALAR SFLFGMDAEA AHELTMDMLA RGQRTPLQWA WCNETVSDPI ELAGLRFPNR 

        70         80         90        100        110        120 
VGLAAGLDKN ARCIDALAAM GFGFVEVGTV TPRAQPGNPK PRMFRLPEAR ALINRLGFNN 

       130        140        150        160        170        180 
EGLDAFVANV QRSQVRTQGR GQSKLLLGLN IGKNATTPIE DATRDYLTCL EGVYPHADYV 

       190        200        210        220        230        240 
TVNISSPNTQ NLRALQSDAA LDCLLGAIAE HRGQLAAAQG RRVPIFVKIA PDLDEAQVAV 

       250        260        270        280        290        300 
IATTLQRHGM DGVVATNTTI RRDAVQGLRH AGETGGLSGA PVLEASNAVI RQLRAALGPA 

       310        320        330        340        350 
FPIIGVGGIL SAEDAVSKIR AGADVVQIYT GLIYEGPALV GRAAKAIRDL R

« Hide

References

[1]"Complete sequence of Diaphorobacter sp. TPSY."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TPSY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001392 Genomic DNA. Translation: ACM33108.1.
RefSeqYP_002553108.1. NC_011992.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB9MIU2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7384724.
GenomeReviewsGene locus Dtpsy_1650 in contig CP001392_GR.
KEGGdia:Dtpsy_1650.
PATRIC21780397. VBIDiaSp55748_1686.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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_ACIET
AccessionPrimary (citable) accession number: B9MIU2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: January 25, 2012
This is version 25 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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