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Q0KBT4 (PYRD_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:H16_A1401
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length344 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 – 344344Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_1000024210

Regions

Nucleotide binding65 – 695FMN By similarity
Nucleotide binding324 – 3252FMN By similarity
Region114 – 1185Substrate binding By similarity
Region252 – 2532Substrate binding By similarity

Sites

Active site1811Nucleophile By similarity
Binding site691Substrate By similarity
Binding site891FMN; via amide nitrogen By similarity
Binding site1451FMN By similarity
Binding site1781FMN By similarity
Binding site1781Substrate By similarity
Binding site1831Substrate By similarity
Binding site2231FMN By similarity
Binding site2511FMN; via carbonyl oxygen By similarity
Binding site2741FMN; via amide nitrogen By similarity
Binding site3031FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0KBT4 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: DDEF1436EFDB71AB

FASTA34436,644
        10         20         30         40         50         60 
MLNALYPLVR PALFSMDAED AHHFTLNNLL RAHRMGLAGC IGNRIADDPR TVMGVRFPNP 

        70         80         90        100        110        120 
VGLAAGLDKD GAYIDGLAAF GFGFIEVGTV TPRAQPGNPR PRMFRLPQAD ALINRMGFNN 

       130        140        150        160        170        180 
GGVDAFVANV RASRWKAEGG VLGLNIGKNA DTPIERANDD YLYCLERVYP HASYVTVNIS 

       190        200        210        220        230        240 
SPNTKNLRQL QGASELDSLL STLKDAQQRL ADQHKRYVPL ALKIAPDLDA DQIGNIGDAL 

       250        260        270        280        290        300 
VRHKIDGVIA TNTTISREAV KGLPHAEEAG GLSGRPVFEA STRVVRALHG VVGDAVPIIG 

       310        320        330        340 
VGGIFGGADA RAKIDAGAKL VQVYSGLIYR GPALVRECAA ALRG

« Hide

References

[1]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed: 16964242] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM260479 Genomic DNA. Translation: CAJ92537.1.
RefSeqYP_725905.1. NC_008313.1.

3D structure databases

ProteinModelPortalQ0KBT4.
SMRQ0KBT4. Positions 5-341.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0KBT4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4248861.
GenomeReviewsGene locus H16_A1401 in contig AM260479_GR.
KEGGreh:H16_A1401.
PATRIC35232265. VBIRalEut6770_1790.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHBG351027.
OMASYVTVNI.
PhylomeDBQ0KBT4.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycREUT381666:H16_A1401-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_CUPNH
AccessionPrimary (citable) accession number: Q0KBT4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: January 25, 2012
This is version 44 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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