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Protein

Dihydroorotate dehydrogenase (quinone)

Gene

pyrD

Organism
Legionella pneumophila (strain Lens)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.UniRule annotation

Catalytic activityi

(S)-dihydroorotate + a quinone = orotate + a quinol.UniRule annotation

Cofactori

FMNUniRule annotationNote: Binds 1 FMN per subunit.UniRule annotation

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes orotate from (S)-dihydroorotate (quinone route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Dihydroorotate dehydrogenase (quinone) (pyrD)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes orotate from (S)-dihydroorotate (quinone route), the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei60SubstrateUniRule annotation1
Binding sitei80FMN; via amide nitrogenUniRule annotation1
Binding sitei133FMNUniRule annotation1
Binding sitei166FMNUniRule annotation1
Binding sitei166SubstrateUniRule annotation1
Active sitei169NucleophileUniRule annotation1
Binding sitei171SubstrateUniRule annotation1
Binding sitei211FMNUniRule annotation1
Binding sitei239FMN; via carbonyl oxygenUniRule annotation1
Binding sitei262FMN; via amide nitrogenUniRule annotation1
Binding sitei291FMN; via amide nitrogenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi56 – 60FMNUniRule annotation5
Nucleotide bindingi312 – 313FMNUniRule annotation2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

UniPathwayiUPA00070; UER00946.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroorotate dehydrogenase (quinone)UniRule annotation (EC:1.3.5.2UniRule annotation)
Alternative name(s):
DHOdehaseUniRule annotation
Short name:
DHODUniRule annotation
Short name:
DHODaseUniRule annotation
Dihydroorotate oxidaseUniRule annotation
Gene namesi
Name:pyrDUniRule annotation
Ordered Locus Names:lpl1785
OrganismiLegionella pneumophila (strain Lens)
Taxonomic identifieri297245 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
Proteomesi
  • UP000002517 Componenti: Chromosome

Organism-specific databases

LegioListilpl1785.

Subcellular locationi

  • Cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001484501 – 333Dihydroorotate dehydrogenase (quinone)Add BLAST333

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ5WVN0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni105 – 109Substrate bindingUniRule annotation5
Regioni240 – 241Substrate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000225103.
KOiK00254.
OMAiERIKMGA.

Family and domain databases

CDDicd04738. DHOD_2_like. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00225. DHO_dh_type2. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR005720. Dihydroorotate_DH.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsiTIGR01036. pyrD_sub2. 1 hit.
PROSITEiPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5WVN0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYSLLRPLLF RLDAEKAHSL TLSLLHYLPG FYFRKMAGQP VHAMGLVFPH
60 70 80 90 100
QVGLAAGLDK NGEHLDALAK LGFSFIELGT VTPKGQTGNP KPRLFRIAEA
110 120 130 140 150
NAIINRMGFN NSGVDVLVEN VKSANYKGIL GINIGKNKET NLNQAADDYL
160 170 180 190 200
YCFRKVYDHA SYVTINISSP NTPDLRQLQQ GDYFAELLAQ LQKEQIKLAD
210 220 230 240 250
QYGRHVPLVV KVSPDETDET LKQMTDIILQ YGIEGIIATN TTCSREMVKN
260 270 280 290 300
LPCSEEQGGL SGRPLMELST RCLRLLKQYV GNDVTLIGVG GIDSLESAKD
310 320 330
KINAGASLLQ VYSGLVYKGP ELIHDIVSGL NAV
Length:333
Mass (Da):36,579
Last modified:November 23, 2004 - v1
Checksum:i9110AA902B8BBD1E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR628337 Genomic DNA. Translation: CAH16024.1.
RefSeqiWP_011215792.1. NC_006369.1.

Genome annotation databases

EnsemblBacteriaiCAH16024; CAH16024; lpl1785.
KEGGilpf:lpl1785.
PATRICi22317287. VBILegPne33733_1970.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR628337 Genomic DNA. Translation: CAH16024.1.
RefSeqiWP_011215792.1. NC_006369.1.

3D structure databases

ProteinModelPortaliQ5WVN0.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH16024; CAH16024; lpl1785.
KEGGilpf:lpl1785.
PATRICi22317287. VBILegPne33733_1970.

Organism-specific databases

LegioListilpl1785.

Phylogenomic databases

HOGENOMiHOG000225103.
KOiK00254.
OMAiERIKMGA.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00946.

Family and domain databases

CDDicd04738. DHOD_2_like. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00225. DHO_dh_type2. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR005720. Dihydroorotate_DH.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsiTIGR01036. pyrD_sub2. 1 hit.
PROSITEiPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPYRD_LEGPL
AccessioniPrimary (citable) accession number: Q5WVN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: November 23, 2004
Last modified: November 2, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.