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B1K0S4 (B1K0S4_BURCC) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
EC=1.3.5.2 HAMAP MF_00225
Alternative name(s):
DHOdehase HAMAP MF_00225
Dihydroorotate oxidase HAMAP MF_00225
Gene names
Name:pyrD HAMAP MF_00225
Ordered Locus Names:Bcenmc03_1530
OrganismBurkholderia cenocepacia (strain MC0-3) [Complete proteome] [HAMAP] EMBL ACA90705.1
Taxonomic identifier406425 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length330 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 SAAS SAAS012135

Catalytic activity

(S)-dihydroorotate + a quinone = orotate + a quinol. HAMAP MF_00225 SAAS SAAS012135

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP MF_00225 SAAS SAAS012135

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. HAMAP MF_00225 SAAS SAAS012135

Subunit structure

Monomer By similarity. HAMAP MF_00225 SAAS SAAS012135

Subcellular location

Cell membrane; Peripheral membrane protein By similarity HAMAP MF_00225.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily. HAMAP MF_00225

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding50 – 545FMN By similarity HAMAP MF_00225
Nucleotide binding306 – 3072FMN By similarity HAMAP MF_00225
Region99 – 1035Substrate binding By similarity HAMAP MF_00225
Region234 – 2352Substrate binding By similarity HAMAP MF_00225

Sites

Active site1631Nucleophile By similarity PIRSR PIRSR000164-1 HAMAP MF_00225
Binding site541Substrate By similarity HAMAP MF_00225
Binding site741FMN; via amide nitrogen By similarity HAMAP MF_00225
Binding site1271FMN By similarity HAMAP MF_00225
Binding site1601FMN By similarity HAMAP MF_00225
Binding site1601Substrate By similarity HAMAP MF_00225
Binding site1651Substrate By similarity HAMAP MF_00225
Binding site2051FMN By similarity HAMAP MF_00225
Binding site2331FMN; via carbonyl oxygen By similarity HAMAP MF_00225
Binding site2561FMN; via amide nitrogen By similarity HAMAP MF_00225
Binding site2851FMN; via amide nitrogen By similarity HAMAP MF_00225

Sequences

Sequence LengthMass (Da)Tools
B1K0S4 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 3D447C93BB0C061B

FASTA33035,090
        10         20         30         40         50         60 
MDAEDAHHLT LRALGAAGRT GLACALSARV PDAPRTVMGL TFRNPVGLAA GLDKDGAAID 

        70         80         90        100        110        120 
GLAALGFGFI EVGTVTPRPQ PGNPRPRMFR LPQAEALINR MGFNNHGVDQ FVKNVQAARY 

       130        140        150        160        170        180 
RGILGLNIGK NADTPIERAA EDYLYCLERV YPFASYVTIN ISSPNTKNLR QLQGAGELDA 

       190        200        210        220        230        240 
LLAALKDKQQ RLADLHGKLV PLALKIAPDL DDEQVKEIGD TLLRHKIEAV IATNTTLSRA 

       250        260        270        280        290        300 
AVQGLPHADE AGGLSGRPVF DASNEVIRKL HAEVGNDVPI IGVGGIFSGE DARAKLAAGA 

       310        320        330 
ALVQLYTGFI YRGPALVSEC VRAIARERSA

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3."
Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Tiedje J., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000958 Genomic DNA. Translation: ACA90705.1.
RefSeqYP_001764827.1. NC_010508.1.

3D structure databases

ProteinModelPortalB1K0S4.
SMRB1K0S4. Positions 1-324.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1K0S4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6123208.
GenomeReviewsGene locus Bcenmc03_1530 in contig CP000958_GR.
KEGGbcm:Bcenmc03_1530.
PATRIC19090140. VBIBurCen61509_1583.

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.
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 nameB1K0S4_BURCC
AccessionPrimary (citable) accession number: B1K0S4
Entry history
Integrated into UniProtKB/TrEMBL: April 29, 2008
Last sequence update: April 29, 2008
Last modified: December 14, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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