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Q6FCL9 (PYRD_ACIAD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 58. 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:ACIAD1321
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length334 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 – 334334Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_0000148420

Regions

Nucleotide binding59 – 635FMN By similarity
Nucleotide binding315 – 3162FMN By similarity
Region108 – 1125Substrate binding By similarity
Region243 – 2442Substrate binding By similarity

Sites

Active site1721Nucleophile By similarity
Binding site631Substrate By similarity
Binding site831FMN; via amide nitrogen By similarity
Binding site1361FMN By similarity
Binding site1691FMN By similarity
Binding site1691Substrate By similarity
Binding site1741Substrate By similarity
Binding site2141FMN By similarity
Binding site2421FMN; via carbonyl oxygen By similarity
Binding site2651FMN; via amide nitrogen By similarity
Binding site2941FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6FCL9 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 34E542D27E5FAE47

FASTA33436,308
        10         20         30         40         50         60 
MLYSLARPML FSLAPERAHE LTLSMLKTAH KMGMLRQTIQ PKPVTCMGIE FPNPVGLAAG 

        70         80         90        100        110        120 
LDKNGAYIDA LAGLGFGFIE IGTITPRPQS GNPKPRLFRI PEAKAIINRM GFNNEGVDQL 

       130        140        150        160        170        180 
VENVKAAKFR GILGINIGKN ADTPVENAVD DYLICLEKVY NYASYITVNI SSPNTKNLRS 

       190        200        210        220        230        240 
LQSGDALTEL LETLKKRQLE LAEQYHHYVP LVLKVAPDLT HEDIQFISEQ LLTFKIDGLI 

       250        260        270        280        290        300 
VTNTTLSREG VENLPFGNEA GGLSGAPVFE KSTECLRSFA KVLNDQIPLI GVGGITQGEH 

       310        320        330 
AVAKKDAGAS LVQIYSGLIY TGPDLIKECV SAIT

« Hide

References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ADP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR543861 Genomic DNA. Translation: CAG68191.1.
RefSeqYP_046013.1. NC_005966.1.

3D structure databases

ProteinModelPortalQ6FCL9.
SMRQ6FCL9. Positions 1-333.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6FCL9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2879565.
GenomeReviewsGene locus ACIAD1321 in contig CR543861_GR.
KEGGaci:ACIAD1321.
NMPDRfig|62977.3.peg.495.
PATRIC20740457. VBIAciSp98416_1187.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHBG351027.
OMASYVTVNI.
PhylomeDBQ6FCL9.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycASP62977:ACIAD1321-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_ACIAD
AccessionPrimary (citable) accession number: Q6FCL9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 19, 2004
Last modified: January 25, 2012
This is version 58 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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