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Q5WVN0

- PYRD_LEGPL

UniProt

Q5WVN0 - PYRD_LEGPL

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Protein

Dihydroorotate dehydrogenase (quinone)

Gene

pyrD

Organism
Legionella pneumophila (strain Lens)
Status
Reviewed - 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

Binds 1 FMN per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601SubstrateUniRule annotation
Binding sitei80 – 801FMN; via amide nitrogenUniRule annotation
Binding sitei133 – 1331FMNUniRule annotation
Binding sitei166 – 1661FMNUniRule annotation
Binding sitei166 – 1661SubstrateUniRule annotation
Active sitei169 – 1691NucleophileUniRule annotation
Binding sitei171 – 1711SubstrateUniRule annotation
Binding sitei211 – 2111FMNUniRule annotation
Binding sitei239 – 2391FMN; via carbonyl oxygenUniRule annotation
Binding sitei262 – 2621FMN; via amide nitrogenUniRule annotation
Binding sitei291 – 2911FMN; via amide nitrogenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi56 – 605FMNUniRule annotation
Nucleotide bindingi312 – 3132FMNUniRule annotation

GO - Molecular functioni

  1. dihydroorotate dehydrogenase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' pyrimidine nucleobase biosynthetic process Source: InterPro
  2. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciLPNE297245:GJD4-1915-MONOMER.
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
ProteomesiUP000002517: Chromosome

Organism-specific databases

LegioListilpl1785.

Subcellular locationi

Cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333Dihydroorotate dehydrogenase (quinone)PRO_0000148450Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi297245.lpl1785.

Structurei

3D structure databases

ProteinModelPortaliQ5WVN0.
SMRiQ5WVN0. Positions 2-330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni105 – 1095Substrate bindingUniRule annotation
Regioni240 – 2412Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0167.
HOGENOMiHOG000225103.
KOiK00254.
OMAiWEAIADI.
OrthoDBiEOG65BDN8.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00225. DHO_dh_type2.
InterProiIPR013785. Aldolase_TIM.
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:
EMBL
GenBank
DDBJ
Links Updated
CR628337 Genomic DNA. Translation: CAH16024.1.
RefSeqiWP_011215792.1. NC_006369.1.
YP_127123.1. NC_006369.1.

Genome annotation databases

EnsemblBacteriaiCAH16024; CAH16024; lpl1785.
GeneIDi3115233.
KEGGilpf:lpl1785.
PATRICi22317287. VBILegPne33733_1970.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR628337 Genomic DNA. Translation: CAH16024.1 .
RefSeqi WP_011215792.1. NC_006369.1.
YP_127123.1. NC_006369.1.

3D structure databases

ProteinModelPortali Q5WVN0.
SMRi Q5WVN0. Positions 2-330.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 297245.lpl1785.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAH16024 ; CAH16024 ; lpl1785 .
GeneIDi 3115233.
KEGGi lpf:lpl1785.
PATRICi 22317287. VBILegPne33733_1970.

Organism-specific databases

LegioListi lpl1785.

Phylogenomic databases

eggNOGi COG0167.
HOGENOMi HOG000225103.
KOi K00254.
OMAi WEAIADI.
OrthoDBi EOG65BDN8.

Enzyme and pathway databases

UniPathwayi UPA00070 ; UER00946 .
BioCyci LPNE297245:GJD4-1915-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00225. DHO_dh_type2.
InterProi IPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view ]
Pfami PF01180. DHO_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsi TIGR01036. pyrD_sub2. 1 hit.
PROSITEi PS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

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: October 29, 2014
This is version 72 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

External Data

Dasty 3