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A9IQ81 (PYRD_BART1) 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:BT_0576
OrganismBartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP]
Taxonomic identifier382640 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length360 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 – 360360Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_0000336456

Regions

Nucleotide binding60 – 645FMN By similarity
Nucleotide binding314 – 3152FMN By similarity
Region109 – 1135Substrate binding By similarity
Region242 – 2432Substrate binding By similarity

Sites

Active site1711Nucleophile By similarity
Binding site641Substrate By similarity
Binding site841FMN; via amide nitrogen By similarity
Binding site1371FMN 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
A9IQ81 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 8A403EC0D4EF371F

FASTA36039,905
        10         20         30         40         50         60 
MSFFRCIGRS ALFMLDPEHA HRLAIVGLKS GLNGCQKVVD KRLSVTIAGL KFKNFIGLAA 

        70         80         90        100        110        120 
GFDKNAEVVD EIFRLGFGFT EIGTVTPKPQ IGNPKPRLFR LKEDEAIINR MGFNNDGHQV 

       130        140        150        160        170        180 
VDDRLRICKK AGVVGVNIGA NKDTVDKIDD YTVGIAHFYD VADYFTVNIS SPNTPGLRDL 

       190        200        210        220        230        240 
QARDSLHLLL NAISKARKEQ EKKHGFSIPI FLKIAPDLSE KELDDIAEEI KLSDFDGLIV 

       250        260        270        280        290        300 
SNTTLSRQGL NNSHFSNEEG GLSGRPLFER STIVLAKMRQ KLGKEIAIIG VGGVKDAQTA 

       310        320        330        340        350        360 
LEKVKAGADL IQLYSGMVYE GPNLVITILK EILQMMQQDG VDNIKDYRDH NLEHWAKFPL

« Hide

References

[1]"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors."
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.
Nat. Genet. 39:1469-1476(2007) [PubMed: 18037886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CIP 105476 / IBS 506.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM260525 Genomic DNA. Translation: CAK01023.1.
RefSeqYP_001609018.1. NC_010161.1.

3D structure databases

ProteinModelPortalA9IQ81.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9IQ81.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5829298.
GenomeReviewsGene locus BT_0576 in contig AM260525_GR.
PATRIC20548910. VBIBarTri113218_0615.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG351027.
OMAAALNRMG.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycBTRI382640:BT_0576-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.
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_BART1
AccessionPrimary (citable) accession number: A9IQ81
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 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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