Skip Header

Contribute Send feedback
Read comments (?) or add your own

B1Y3C1 (PYRD_LEPCP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Lcho_1055
OrganismLeptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix discophora (strain SP-6)) [Complete proteome] [HAMAP]
Taxonomic identifier395495 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Leptothrix

Protein attributes

Sequence length345 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 – 345345Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_1000100271

Regions

Nucleotide binding65 – 695FMN By similarity
Nucleotide binding325 – 3262FMN By similarity
Region114 – 1185Substrate binding By similarity
Region253 – 2542Substrate binding By similarity

Sites

Active site1821Nucleophile By similarity
Binding site691Substrate By similarity
Binding site891FMN; via amide nitrogen By similarity
Binding site1461FMN By similarity
Binding site1791FMN By similarity
Binding site1791Substrate By similarity
Binding site1841Substrate By similarity
Binding site2241FMN By similarity
Binding site2521FMN; via carbonyl oxygen By similarity
Binding site2751FMN; via amide nitrogen By similarity
Binding site3041FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
B1Y3C1 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: E5F04E9465DBF2B2

FASTA34536,152
        10         20         30         40         50         60 
MALVPYPLTR PFLFGMDPEA AHELTLGSIA RFQNTPLQCL WSQSRIADPV TVAGLRFPNR 

        70         80         90        100        110        120 
IGLAAGLDKN GRCIDGLGAM GFGFIEVGTV TPLGQPGNPK PRMFRLPEKN ALINRLGFNN 

       130        140        150        160        170        180 
EGLASFLANV QRATSFRRNG GLLGLNIGKN AVTPIENAAD DYLIALAGVY PHADYVTVNI 

       190        200        210        220        230        240 
SSPNTKNLRA LQSDAALDAL LGALQTRRLA LATEHGRSVP MFVKIAPDLD EAQVRVIAAT 

       250        260        270        280        290        300 
LRHNGIDGVI ATNTTLARDA VAGLAHADEA GGLSGAPVLA ASNRVIAQLR AELGGAYPII 

       310        320        330        340 
GVGGVLSGAD ARSKRAAGAD LVQVYTGLIY RGPALVPECA RALRG

« Hide

References

[1]"Complete sequence of Leptothrix cholodnii SP-6."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Emerson D., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51168 / LMG 8142 / SP-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001013 Genomic DNA. Translation: ACB33324.1.
RefSeqYP_001790089.1. NC_010524.1.

3D structure databases

ProteinModelPortalB1Y3C1.
SMRB1Y3C1. Positions 5-343.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1Y3C1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6163133.
GenomeReviewsGene locus Lcho_1055 in contig CP001013_GR.
KEGGlch:Lcho_1055.
PATRIC22392401. VBILepCho83238_1054.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG351027.
OMASYVTVNI.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycLCHO395495:LCHO_1055-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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_LEPCP
AccessionPrimary (citable) accession number: B1Y3C1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 33 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents