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Q5WVN0

- PYRD_LEGPL

UniProt

Q5WVN0 - PYRD_LEGPL

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Protein
Dihydroorotate dehydrogenase (quinone)
Gene
pyrD, lpl1785
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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 FMN per subunit By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601Substrate By similarity
Binding sitei80 – 801FMN; via amide nitrogen By similarity
Binding sitei133 – 1331FMN By similarity
Binding sitei166 – 1661FMN By similarity
Binding sitei166 – 1661Substrate By similarity
Active sitei169 – 1691Nucleophile By similarity
Binding sitei171 – 1711Substrate By similarity
Binding sitei211 – 2111FMN By similarity
Binding sitei239 – 2391FMN; via carbonyl oxygen By similarity
Binding sitei262 – 2621FMN; via amide nitrogen By similarity
Binding sitei291 – 2911FMN; via amide nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi56 – 605FMN By similarity
Nucleotide bindingi312 – 3132FMN By similarity

GO - Molecular functioni

  1. dihydroorotate oxidase activity Source: InterPro

GO - Biological processi

  1. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  2. 'de novo' pyrimidine nucleobase biosynthetic process Source: InterPro
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) (EC:1.3.5.2)
Alternative name(s):
DHOdehase
Short name:
DHOD
Short name:
DHODase
Dihydroorotate oxidase
Gene namesi
Name:pyrD
Ordered Locus Names:lpl1785
OrganismiLegionella pneumophila (strain Lens)
Taxonomic identifieri297245 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
ProteomesiUP000002517: Chromosome

Organism-specific databases

LegioListilpl1785.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

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

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi297245.lpl1785.

Structurei

3D structure databases

ProteinModelPortaliQ5WVN0.
SMRiQ5WVN0. Positions 2-330.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni105 – 1095Substrate binding By similarity
Regioni240 – 2412Substrate binding By similarity

Sequence similaritiesi

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

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MYSLLRPLLF RLDAEKAHSL TLSLLHYLPG FYFRKMAGQP VHAMGLVFPH    50
QVGLAAGLDK NGEHLDALAK LGFSFIELGT VTPKGQTGNP KPRLFRIAEA 100
NAIINRMGFN NSGVDVLVEN VKSANYKGIL GINIGKNKET NLNQAADDYL 150
YCFRKVYDHA SYVTINISSP NTPDLRQLQQ GDYFAELLAQ LQKEQIKLAD 200
QYGRHVPLVV KVSPDETDET LKQMTDIILQ YGIEGIIATN TTCSREMVKN 250
LPCSEEQGGL SGRPLMELST RCLRLLKQYV GNDVTLIGVG GIDSLESAKD 300
KINAGASLLQ VYSGLVYKGP ELIHDIVSGL NAV 333
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: September 3, 2014
This is version 70 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

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