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A8LY18 (PYRD_SALAI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. 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:Sare_1850
OrganismSalinispora arenicola (strain CNS-205) [Complete proteome] [HAMAP]
Taxonomic identifier391037 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micromonosporineae › Micromonosporaceae › Salinispora

Protein attributes

Sequence length338 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 – 338338Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_0000336490

Regions

Nucleotide binding68 – 725FMN By similarity
Nucleotide binding317 – 3182FMN By similarity
Region117 – 1215Substrate binding By similarity
Region243 – 2442Substrate binding By similarity

Sites

Active site1831Nucleophile By similarity
Binding site721Substrate By similarity
Binding site921FMN; via amide nitrogen By similarity
Binding site1471FMN By similarity
Binding site1801FMN By similarity
Binding site1801Substrate By similarity
Binding site1851Substrate By similarity
Binding site2141FMN By similarity
Binding site2421FMN; via carbonyl oxygen By similarity
Binding site2671FMN; via amide nitrogen By similarity
Binding site2961FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A8LY18 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 090DBC9A768B0985

FASTA33835,324
        10         20         30         40         50         60 
MLFERVVRPT LFRLKGGDAE AAHEFAVRRL AGLARMPAAL AVLRARYGVS APRTVFGLRF 

        70         80         90        100        110        120 
PNPVGLAAGM DKDGLALPAW PALGFGFVEV GTVTAHPQPG NPRPRLFRLP DSGAVVNRMG 

       130        140        150        160        170        180 
FNNAGAGALA ARLAALPRPL GVPLGISLGK SRITPLEEAV EDYQTSYRAL REYGDYFAVN 

       190        200        210        220        230        240 
VSSPNTPGLR ELQDRAHLDA LLAALVGEKP ILVKIAPDLP EPAIAELLEV CLARGVAGVI 

       250        260        270        280        290        300 
ATNTTLARDG LAPADQAGGA EAGGLSGRPL ADRAREVVAF VHRETDGRLP IVGVGGIVTP 

       310        320        330 
DDAGRMFDAG ASLVQLYTGF VYRGPALVRA AAAAARTP

« Hide

References

[1]"Complete sequence of Salinispora arenicola CNS-205."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K. expand/collapse author list , Jenkins C., Udwary D., Xiang L., Gontang E., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CNS-205.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000850 Genomic DNA. Translation: ABV97735.1.
RefSeqYP_001536726.1. NC_009953.1.

3D structure databases

ProteinModelPortalA8LY18.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8LY18.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5704785.
GenomeReviewsGene locus Sare_1850 in contig CP000850_GR.
KEGGsaq:Sare_1850.
PATRIC23432216. VBISalAre38676_1878.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG351027.
OMASYVTVNI.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycSARE391037:SARE_1850-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_SALAI
AccessionPrimary (citable) accession number: A8LY18
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 4, 2007
Last modified: January 25, 2012
This is version 34 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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