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Q1H411 (PYRD_METFK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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:Mfla_0506
OrganismMethylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875) [Complete proteome] [HAMAP]
Taxonomic identifier265072 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Methylophilales › Methylophilaceae › Methylobacillus

Protein attributes

Sequence length337 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 – 337337Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_1000024183

Regions

Nucleotide binding62 – 665FMN By similarity
Nucleotide binding318 – 3192FMN By similarity
Region111 – 1155Substrate binding By similarity
Region246 – 2472Substrate binding By similarity

Sites

Active site1751Nucleophile By similarity
Binding site661Substrate By similarity
Binding site861FMN; via amide nitrogen By similarity
Binding site1391FMN By similarity
Binding site1721FMN By similarity
Binding site1721Substrate By similarity
Binding site1771Substrate By similarity
Binding site2171FMN By similarity
Binding site2451FMN; via carbonyl oxygen By similarity
Binding site2681FMN; via amide nitrogen By similarity
Binding site2971FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1H411 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 8A8DD550CC0F15DA

FASTA33736,673
        10         20         30         40         50         60 
MLYSIVKPWL FRLDAERAHD FTLKNLKRLE RSGLLNLYPR PPKCKQRQVM GINFPNPVGL 

        70         80         90        100        110        120 
AAGLDKNGAY IDALAGLGFG FIEIGTITPR PQPGNPKPRM FRLPEAQGVI NRFGFNNLGV 

       130        140        150        160        170        180 
DVLLRNVAAT KYKGVLGINI GKNFDTPNER AVDDYLHCLR KVYPYAHYVT VNISSPNTKN 

       190        200        210        220        230        240 
LRALQEKEAL GQLLHALKQE QQVLADQHGR YVPIALKIAP DLDEGQVADI AALLMKHQFD 

       250        260        270        280        290        300 
GVIATNTTLA RDMVQALPCA QEAGGLSGAP LRDRSTAVIQ SLSNHLAGAL PIIGVGGILS 

       310        320        330 
GEDAEQKIKA GASLVQVYSG LVYRGPVLVD DICRTLG

« Hide

References

[1]"Complete sequence of Methylobacillus flagellatus KT."
US DOE Joint Genome Institute
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., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT / ATCC 51484 / DSM 6875.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000284 Genomic DNA. Translation: ABE48776.1.
RefSeqYP_544617.1. NC_007947.1.

3D structure databases

ProteinModelPortalQ1H411.
SMRQ1H411. Positions 1-336.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1H411.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3999565.
GenomeReviewsGene locus Mfla_0506 in contig CP000284_GR.
KEGGmfa:Mfla_0506.
NMPDRfig|265072.7.peg.501.
PATRIC32266547. VBIMetFla97085_0516.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHBG351027.
OMASYVTVNI.
PhylomeDBQ1H411.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycMFLA265072:MFLA_0506-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_METFK
AccessionPrimary (citable) accession number: Q1H411
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 27, 2006
Last modified: January 25, 2012
This is version 45 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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