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A4JE22 (A4JE22_BURVG) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 42. 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:Bcep1808_1518
OrganismBurkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia (strain R1808)) [Complete proteome] [HAMAP]
Taxonomic identifier269482 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length356 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 binding76 – 805FMN By similarity HAMAP MF_00225
Nucleotide binding332 – 3332FMN By similarity HAMAP MF_00225
Region125 – 1295Substrate binding By similarity HAMAP MF_00225
Region260 – 2612Substrate binding By similarity HAMAP MF_00225

Sites

Active site1891Nucleophile By similarity PIRSR PIRSR000164-1 HAMAP MF_00225
Binding site801Substrate By similarity HAMAP MF_00225
Binding site1001FMN; via amide nitrogen By similarity HAMAP MF_00225
Binding site1531FMN By similarity HAMAP MF_00225
Binding site1861FMN By similarity HAMAP MF_00225
Binding site1861Substrate By similarity HAMAP MF_00225
Binding site1911Substrate By similarity HAMAP MF_00225
Binding site2311FMN By similarity HAMAP MF_00225
Binding site2591FMN; via carbonyl oxygen By similarity HAMAP MF_00225
Binding site2821FMN; via amide nitrogen By similarity HAMAP MF_00225
Binding site3111FMN; via amide nitrogen By similarity HAMAP MF_00225

Sequences

Sequence LengthMass (Da)Tools
A4JE22 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 4DFDA9E3AD268939

FASTA35637,712
        10         20         30         40         50         60 
MSSISAVRPI PVFSSLYPLA RASLFKMDAE DAHHLTLRAL GAAGRTGLAC ALSARVPDAP 

        70         80         90        100        110        120 
RTVMGLTFRN PVGLAAGLDK DGAAIDGLAA LGFGFIEVGT VTPRPQPGNP RPRMFRLPQA 

       130        140        150        160        170        180 
DALINRMGFN NHGVDQFVKN VQAARYRGVL GLNIGKNADT PIERAADDYL YCLERVYPFA 

       190        200        210        220        230        240 
SYVTINISSP NTKNLRQLQG AGELDALLAA LKDKQQRLAD LHGKLVPLAL KIAPDLDDEQ 

       250        260        270        280        290        300 
VKEIADTLLR HKIEAVIATN TTLSRAAVQG LPHADEAGGL SGRPVFDASN EVIRKLHAEL 

       310        320        330        340        350 
GSAVPIIGVG GIFSGDDART KLAAGASLVQ LYTGFIYRGP ALVAECVKAI AAERAA

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Tiedje J., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G4 / LMG 22486.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000614 Genomic DNA. Translation: ABO54525.1.
RefSeqYP_001119360.1. NC_009256.1.

3D structure databases

ProteinModelPortalA4JE22.
SMRA4JE22. Positions 16-350.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4JE22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4953235.
GenomeReviewsGene locus Bcep1808_1518 in contig CP000614_GR.
KEGGbvi:Bcep1808_1518.
PATRIC19321578. VBIBurVie89221_5757.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
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 nameA4JE22_BURVG
AccessionPrimary (citable) accession number: A4JE22
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 2007
Last sequence update: May 1, 2007
Last modified: December 14, 2011
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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