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Q5WVN0 (PYRD_LEGPL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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

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:lpl1785
OrganismLegionella pneumophila (strain Lens) [Complete proteome] [HAMAP]
Taxonomic identifier297245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length333 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
   LigandFlavoprotein
FMN
   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 – 333333Dihydroorotate dehydrogenase (quinone) HAMAP-Rule MF_00225
PRO_0000148450

Regions

Nucleotide binding56 – 605FMN By similarity
Nucleotide binding312 – 3132FMN By similarity
Region105 – 1095Substrate binding By similarity
Region240 – 2412Substrate binding By similarity

Sites

Active site1691Nucleophile By similarity
Binding site601Substrate By similarity
Binding site801FMN; via amide nitrogen By similarity
Binding site1331FMN By similarity
Binding site1661FMN By similarity
Binding site1661Substrate By similarity
Binding site1711Substrate By similarity
Binding site2111FMN By similarity
Binding site2391FMN; via carbonyl oxygen By similarity
Binding site2621FMN; via amide nitrogen By similarity
Binding site2911FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WVN0 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 9110AA902B8BBD1E

FASTA33336,579
        10         20         30         40         50         60 
MYSLLRPLLF RLDAEKAHSL TLSLLHYLPG FYFRKMAGQP VHAMGLVFPH QVGLAAGLDK 

        70         80         90        100        110        120 
NGEHLDALAK LGFSFIELGT VTPKGQTGNP KPRLFRIAEA NAIINRMGFN NSGVDVLVEN 

       130        140        150        160        170        180 
VKSANYKGIL GINIGKNKET NLNQAADDYL YCFRKVYDHA SYVTINISSP NTPDLRQLQQ 

       190        200        210        220        230        240 
GDYFAELLAQ LQKEQIKLAD QYGRHVPLVV KVSPDETDET LKQMTDIILQ YGIEGIIATN 

       250        260        270        280        290        300 
TTCSREMVKN LPCSEEQGGL SGRPLMELST RCLRLLKQYV GNDVTLIGVG GIDSLESAKD 

       310        320        330 
KINAGASLLQ VYSGLVYKGP ELIHDIVSGL NAV 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Lens.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628337 Genomic DNA. Translation: CAH16024.1.
RefSeqYP_127123.1. NC_006369.1.

3D structure databases

ProteinModelPortalQ5WVN0.
SMRQ5WVN0. Positions 2-330.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING297245.lpl1785.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH16024; CAH16024; lpl1785.
GeneID3115233.
KEGGlpf:lpl1785.
PATRIC22317287. VBILegPne33733_1970.

Organism-specific databases

LegioListlpl1785.
CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHOG000225103.
KOK00254.
OMAWEAIADI.
OrthoDBEOG65BDN8.

Enzyme and pathway databases

BioCycLPNE297245:GJD4-1915-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_LEGPL
AccessionPrimary (citable) accession number: Q5WVN0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways