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Q129L9 (PYRD_POLSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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:Bpro_2858
OrganismPolaromonas sp. (strain JS666 / ATCC BAA-500) [Complete proteome] [HAMAP]
Taxonomic identifier296591 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Polaromonas

Protein attributes

Sequence length350 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 – 350350Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_1000024196

Regions

Nucleotide binding65 – 695FMN By similarity
Nucleotide binding328 – 3292FMN By similarity
Region114 – 1185Substrate binding By similarity
Region256 – 2572Substrate binding By similarity

Sites

Active site1851Nucleophile By similarity
Binding site691Substrate By similarity
Binding site891FMN; via amide nitrogen By similarity
Binding site1491FMN By similarity
Binding site1821FMN By similarity
Binding site1821Substrate By similarity
Binding site1871Substrate By similarity
Binding site2271FMN By similarity
Binding site2551FMN; via carbonyl oxygen By similarity
Binding site2781FMN; via amide nitrogen By similarity
Binding site3071FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q129L9 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 4E887614D10C09F4

FASTA35037,251
        10         20         30         40         50         60 
MSLLPYALAR PFLFGLDPET AHELTMASLA RTQGTPLSLA WCSSRVNDPI ALAGLKFANR 

        70         80         90        100        110        120 
VGLAAGLDKN ARCIDGLAAM GFGFVEVGTV TPKGQPGNPK PRMFRLPEAN ALINRLGFNN 

       130        140        150        160        170        180 
DGLDAFLANV QQSRVRRQNT PNPLILGLNI GKNAVTPIEN AVDDYLTCLD GVYPHADYVT 

       190        200        210        220        230        240 
VNISSPNTKN LRALQSDEAL DALLGRIAER RESLARQHGK RVPIFVKIAP DLDEAQVDVI 

       250        260        270        280        290        300 
AATLKRHAMD GVVATNTTLS RDAVKGLRHA EEAGGLSGAP VLEASNRVIR QLRAALGAGF 

       310        320        330        340        350 
PIIGVGGVMS GQDAVSKIRA GADVVQIYTG LIYKGPELVN EAALAIKKNR

« Hide

References

[1]"Complete sequence of chromosome of Polaromonas sp. JS666."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JS666 / ATCC BAA-500.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000316 Genomic DNA. Translation: ABE44773.1.
RefSeqYP_549671.1. NC_007948.1.

3D structure databases

ProteinModelPortalQ129L9.
SMRQ129L9. Positions 4-342.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ129L9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4014470.
GenomeReviewsGene locus Bpro_2858 in contig CP000316_GR.
KEGGpol:Bpro_2858.
NMPDRfig|296591.1.peg.5449.
PATRIC22958886. VBIPolSp102244_2903.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHBG351027.
OMASYVTVNI.
PhylomeDBQ129L9.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycPSP296591:BPRO_2858-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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_POLSJ
AccessionPrimary (citable) accession number: Q129L9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: January 25, 2012
This is version 45 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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