Skip Header

Contribute Send feedback
Read comments (?) or add your own

A4SWU5 (PYRD_POLSQ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Pnuc_0741
OrganismPolynucleobacter sp. (strain QLW-P1DMWA-1) [Complete proteome] [HAMAP]
Taxonomic identifier312153 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Polynucleobacter

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_0000336481

Regions

Nucleotide binding64 – 685FMN By similarity
Nucleotide binding323 – 3242FMN By similarity
Region113 – 1175Substrate binding By similarity
Region251 – 2522Substrate binding By similarity

Sites

Active site1801Nucleophile By similarity
Binding site681Substrate By similarity
Binding site881FMN; via amide nitrogen By similarity
Binding site1441FMN By similarity
Binding site1771FMN By similarity
Binding site1771Substrate By similarity
Binding site1821Substrate By similarity
Binding site2221FMN By similarity
Binding site2501FMN; via carbonyl oxygen By similarity
Binding site2731FMN; via amide nitrogen By similarity
Binding site3021FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A4SWU5 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 9F55F3A130DFE4D5

FASTA34437,461
        10         20         30         40         50         60 
MIDRYSLLRP WLFCLDPEQA HNLTLKNLDR AQRFGLLQRL VSKPIADPQN LCGIEFPNPV 

        70         80         90        100        110        120 
GLAAGLDKDG KHIDSLAALG FGFLEIGTVT PRPQAGNPKP RMFRLPQAEA IINRMGFNND 

       130        140        150        160        170        180 
GVEACVSRVR QSIFWQRGGV LGLNIGKNAI TPIEDAASDY IAAMEAVYEI ATYITVNISS 

       190        200        210        220        230        240 
PNTQNLRALQ GEDMLRSLLR SLDDARKRLS DRYGVRKPLF LKIAPDLDQN DIHLIADLLM 

       250        260        270        280        290        300 
EFNIDAVIAT NTTISREAVT GMQYGEETGG LSGAPVRIAS NIVIRALKAR LGVQLPIIGV 

       310        320        330        340 
GGILSGADAR EKIMAGASLV QLYSGLIYKG PDLVSECAKA LRQS

« Hide

References

[1]"Complete sequence of Polynucleobacter sp. QLW-P1DMWA-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Poeckl M., Wu Q.L., Hahn M., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: QLW-P1DMWA-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000655 Genomic DNA. Translation: ABP33959.1.
RefSeqYP_001155523.1. NC_009379.1.

3D structure databases

ProteinModelPortalA4SWU5.
SMRA4SWU5. Positions 5-341.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4SWU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5053643.
GenomeReviewsGene locus Pnuc_0741 in contig CP000655_GR.
KEGGpnu:Pnuc_0741.
PATRIC22965889. VBIPolNec12025_0771.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHBG351027.
OMASYVTVNI.
PhylomeDBA4SWU5.
ProtClustDBCLSK2323695.

Enzyme and pathway databases

BioCycPSP312153:PNUC_0741-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_POLSQ
AccessionPrimary (citable) accession number: A4SWU5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 15, 2007
Last modified: January 25, 2012
This is version 42 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents