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B1YPI6 (B1YPI6_BURA4) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 31. 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:BamMC406_1476
OrganismBurkholderia ambifaria (strain MC40-6) [Complete proteome] [HAMAP] EMBL ACB63963.1
Taxonomic identifier398577 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia 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
B1YPI6 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: CB36B4BFF15EA76B

FASTA35637,926
        10         20         30         40         50         60 
MSFIPAVRPI PVFSSLYPLA RASLFKMDAE DAHHLTLRAL GAAGRTGLAC ALSARVPDAP 

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

       130        140        150        160        170        180 
DALINRMGFN NHGVDQFVKN VQAARYRGIL GLNIGKNADT PIERAAEDYL YCLERVYPFA 

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

       250        260        270        280        290        300 
VKEIGDTLLR HKIEAVIATN TTLSRAAVQG LPHADEAGGL SGRPVFDASN EVIRKLHAEV 

       310        320        330        340        350 
GSAVPIIGVG GIFSGEDARV KLAAGASLVQ LYTGFIYRGP ALVAECVKAI ARERTA 

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References

[1]"Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A. expand/collapse author list , Ramette A., Konstantinidis K., Tiedje J., Richardson P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001025 Genomic DNA. Translation: ACB63963.1.
RefSeqYP_001808179.1. NC_010551.1.

3D structure databases

ProteinModelPortalB1YPI6.
SMRB1YPI6. Positions 16-350.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1YPI6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6177080.
GenomeReviewsGene locus BamMC406_1476 in contig CP001025_GR.
KEGGbac:BamMC406_1476.
PATRIC19032366. VBIBurAmb82852_1509.

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 nameB1YPI6_BURA4
AccessionPrimary (citable) accession number: B1YPI6
Entry history
Integrated into UniProtKB/TrEMBL: May 20, 2008
Last sequence update: May 20, 2008
Last modified: December 14, 2011
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)