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A9WDI1 (PYRD_CHLAA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. 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:Caur_3923
OrganismChloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
Taxonomic identifier324602 [NCBI]
Taxonomic lineageBacteria › Chloroflexi › Chloroflexales › Chloroflexaceae › Chloroflexus

Protein attributes

Sequence length363 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
Reference 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 – 363363Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_0000336462

Regions

Nucleotide binding77 – 815FMN By similarity
Nucleotide binding337 – 3382FMN By similarity
Region126 – 1305Substrate binding By similarity
Region263 – 2642Substrate binding By similarity

Sites

Active site1911Nucleophile By similarity
Binding site811Substrate By similarity
Binding site1011FMN; via amide nitrogen By similarity
Binding site1551FMN By similarity
Binding site1881FMN By similarity
Binding site1881Substrate By similarity
Binding site1931Substrate By similarity
Binding site2341FMN By similarity
Binding site2621FMN; via carbonyl oxygen By similarity
Binding site2871FMN; via amide nitrogen By similarity
Binding site3161FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A9WDI1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 8EA52C0ABAC594F0

FASTA36339,418
        10         20         30         40         50         60 
MNRSEALFYR YGIRPILFRL GRGDAETAHE RTLHILALIS RSRLLCKTIG YLTTIRDQRL 

        70         80         90        100        110        120 
QRTVCGIPFP NPVGLAAGMD KDGVAIPAWA ALGFGFVEVG TVTHHPQPGN PRPRLFRLPE 

       130        140        150        160        170        180 
QEALINRMGF NNQGAASLAR RLARLQPAPI PVGVSIGKSK ITPLEQAIDD YRASFRQLFP 

       190        200        210        220        230        240 
YAAYIAINVS SPNTPGLRQL QDADQLRALL AALQHDNAEL GRTDQRGPRP LLVKIAPDLS 

       250        260        270        280        290        300 
DTAIEEVLTV CADHGVAGII ATNTTISREG LTGVDPRLAA EAGGLSGRPL IARALHVVRL 

       310        320        330        340        350        360 
IARLTGNRLP IIGVGGIHTP DDGLRMLEAG ASLIQIYTGL VYYGPLLPRR INRAILTHSK 


VQQ

« Hide

References

[1]"Complete sequence of Chloroflexus aurantiacus J-10-fl."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Pierson B.K., Blankenship R.E., Richardson P.
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29366 / DSM 635 / J-10-fl.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000909 Genomic DNA. Translation: ABY37100.1.
RefSeqYP_001637489.1. NC_010175.1.

3D structure databases

ProteinModelPortalA9WDI1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9WDI1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5825733.
GenomeReviewsGene locus Caur_3923 in contig CP000909_GR.
KEGGcau:Caur_3923.
PATRIC21419334. VBIChlAur28763_4398.

Phylogenomic databases

HOGENOMHBG351027.
OMAAKEYERY.
PhylomeDBA9WDI1.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_CHLAA
AccessionPrimary (citable) accession number: A9WDI1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 35 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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