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B0V824 (PYRD_ACIBY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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:ABAYE1278
OrganismAcinetobacter baumannii (strain AYE) [Complete proteome] [HAMAP]
Taxonomic identifier509173 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length334 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 – 334334Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_1000100243

Regions

Nucleotide binding59 – 635FMN By similarity
Nucleotide binding315 – 3162FMN By similarity
Region108 – 1125Substrate binding By similarity
Region243 – 2442Substrate binding By similarity

Sites

Active site1721Nucleophile By similarity
Binding site631Substrate By similarity
Binding site831FMN; via amide nitrogen By similarity
Binding site1361FMN By similarity
Binding site1691FMN By similarity
Binding site1691Substrate By similarity
Binding site1741Substrate By similarity
Binding site2141FMN By similarity
Binding site2421FMN; via carbonyl oxygen By similarity
Binding site2651FMN; via amide nitrogen By similarity
Binding site2941FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
B0V824 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 9D610BBC7CA7ECE1

FASTA33436,093
        10         20         30         40         50         60 
MLYSLARPML FSLAPERAHE LTLSMLDKAH KLGMMRQTVE AKPTTCMGIE FPNPVGLAAG 

        70         80         90        100        110        120 
LDKNGAHIDA LAGLGFGFIE IGTITPRPQS GNPKPRLFRI PEAKAIINRM GFNNDGVDKL 

       130        140        150        160        170        180 
IENVKASKFR GILGINIGKN ADTPVEKAVD DYLICLEKVY NYASYITVNI SSPNTKNLRS 

       190        200        210        220        230        240 
LQSGDALTEL LQTLKARQLE LAEQYNHYVP LVLKVAPDLT AEDVEFISAQ LLDFKIDGLI 

       250        260        270        280        290        300 
VTNTTLSREG VENLPYGNES GGLSGAPVFE KSTECLRLFA QTLKGQIPLI GVGGILSGEQ 

       310        320        330 
AAAKQQAGAT LVQIYSGLIY TGPTLVKQCV EAMT

« Hide

References

[1]"Comparative analysis of Acinetobacters: three genomes for three lifestyles."
Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S.
PLoS ONE 3:E1805-E1805(2008) [PubMed: 18350144] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AYE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU459141 Genomic DNA. Translation: CAM86199.1.
RefSeqYP_001713200.1. NC_010410.1.

3D structure databases

ProteinModelPortalB0V824.
SMRB0V824. Positions 1-332.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0V824.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6001108.
GenomeReviewsGene locus ABAYE1278 in contig CU459141_GR.
PATRIC20725955. VBIAciBau69881_1300.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG351027.
OMASYVTVNI.
ProtClustDBPRK05286.

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.
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_ACIBY
AccessionPrimary (citable) accession number: B0V824
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: January 25, 2012
This is version 31 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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