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A3N0D6 (PYRD_ACTP2) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:APL_0774
OrganismActinobacillus pleuropneumoniae serotype 5b (strain L20) [Complete proteome] [HAMAP]
Taxonomic identifier416269 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length335 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 – 335335Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_1000024146

Regions

Nucleotide binding58 – 625FMN By similarity
Nucleotide binding314 – 3152FMN By similarity
Region107 – 1115Substrate binding By similarity
Region242 – 2432Substrate binding By similarity

Sites

Active site1711Nucleophile By similarity
Binding site621Substrate By similarity
Binding site821FMN; via amide nitrogen By similarity
Binding site1351FMN By similarity
Binding site1681FMN By similarity
Binding site1681Substrate By similarity
Binding site1731Substrate By similarity
Binding site2131FMN By similarity
Binding site2411FMN; via carbonyl oxygen By similarity
Binding site2641FMN; via amide nitrogen By similarity
Binding site2931FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A3N0D6 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 092E27DA1B4AFE3E

FASTA33536,192
        10         20         30         40         50         60 
MYSLIRKCLF SMDAETAHNF SIQALKLAGK LPINVLPMPL NPVEVMGLQF KNPIGLAAGA 

        70         80         90        100        110        120 
DKNGEAIDGF GKLGFGFIEV GTVTPVAQDG NPKPRQFRIL EAEGIINRNG FNNLGVDVLV 

       130        140        150        160        170        180 
ENVKKAKYDG IIGINIGKNA VTPIERALDD YQICLRKVYE HADYITVNIS SPNTKNLRTL 

       190        200        210        220        230        240 
QYGEALDDLL RSLKSEQESL SQKFNRYKPL VLKIAPDLTD EEIASVADSL VRYKIDGVIA 

       250        260        270        280        290        300 
GNTTLSRDPV VGLKNAEQQG GLSGKPLNTL STRLISTLAK ELNGALPIIG SGGIHSVASG 

       310        320        330 
QEKIDAGASL LQVYSAMIYQ GPALIQNLAK HIQVR

« Hide

References

[1]"The complete genome sequence of Actinobacillus pleuropneumoniae L20 (serotype 5b)."
Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., Nash J.H.E.
J. Bacteriol. 190:1495-1496(2008) [PubMed: 18065534] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: L20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000569 Genomic DNA. Translation: ABN73872.1.
RefSeqYP_001053477.1. NC_009053.1.

3D structure databases

ProteinModelPortalA3N0D6.
SMRA3N0D6. Positions 2-331.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3N0D6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4849059.
GenomeReviewsGene locus APL_0774 in contig CP000569_GR.
KEGGapl:APL_0774.
PATRIC20746424. VBIActPle94089_0809.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHBG351027.
OMASYVTVNI.
PhylomeDBA3N0D6.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycAPLE416269:APL_0774-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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_ACTP2
AccessionPrimary (citable) accession number: A3N0D6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: December 14, 2011
This is version 40 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

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