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A6H0L5 (PYRD_FLAPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 41. 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:FP1822
OrganismFlavobacterium psychrophilum (strain JIP02/86 / ATCC 49511)
Taxonomic identifier402612 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Flavobacterium

Protein attributes

Sequence length350 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 – 350350Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_0000336467

Regions

Nucleotide binding67 – 715FMN By similarity
Nucleotide binding327 – 3282FMN By similarity
Region116 – 1205Substrate binding By similarity
Region256 – 2572Substrate binding By similarity

Sites

Active site1791Nucleophile By similarity
Binding site711Substrate By similarity
Binding site911FMN; via amide nitrogen By similarity
Binding site1431FMN By similarity
Binding site1761FMN By similarity
Binding site1761Substrate By similarity
Binding site1811Substrate By similarity
Binding site2271FMN By similarity
Binding site2551FMN; via carbonyl oxygen By similarity
Binding site2771FMN; via amide nitrogen By similarity
Binding site3061FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A6H0L5 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 33EF90906855958E

FASTA35038,966
        10         20         30         40         50         60 
MYKLIIRPIL FCFDPEKVHY FTFSLIRTIA KIPGFTSIFK SLYEVNDKRL EREVFGLKFK 

        70         80         90        100        110        120 
NPVGLAAGFD KDAKLYKELS NFGFGFIEIG TLTPKGQEGN PKKRLFRLQE DSAIINRMGF 

       130        140        150        160        170        180 
NNGGVLEAVE RLKKNNGVLI GGNIGKNKLT PNENATSDYE ICFDALYDYV DYFVVNVSSP 

       190        200        210        220        230        240 
NTPNLRELQE KEPLTQLLNT LQNKNQNKQK QTRDGAQSSG AKPILLKIAP DLTNEQLLDI 

       250        260        270        280        290        300 
IDIVKTTKIA GIIATNTTIS REGLQSINRI EMGGLSGKPL TNRSTEVIRF LSQKSNKAFP 

       310        320        330        340        350 
IIGVGGIHCV QDAIEKLEAG ASLIQLYTGF IYEGPALVKA INKEILKKSL

« Hide

References

[1]"Complete genome sequence of the fish pathogen Flavobacterium psychrophilum."
Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B., Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F., Claverol S., Dumetz F., Le Henaff M., Benmansour A.
Nat. Biotechnol. 25:763-769(2007) [PubMed: 17592475] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JIP02/86 / ATCC 49511.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM398681 Genomic DNA. Translation: CAL43888.1.
RefSeqYP_001296693.1. NC_009613.1.

3D structure databases

ProteinModelPortalA6H0L5.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6H0L5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5300705.
GenomeReviewsGene locus FP1822 in contig AM398681_GR.
KEGGfps:FP1822.
NMPDRfig|402612.4.peg.1764.
PATRIC21908602. VBIFlaPsy4505_1847.

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHBG351027.
OMAAALNRMG.
ProtClustDBPRK05286.

Family and domain databases

HAMAPMF_00225. DHO_dh_type2.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
[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. False negative.
PS00912. DHODEHASE_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_FLAPJ
AccessionPrimary (citable) accession number: A6H0L5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 24, 2007
Last modified: December 14, 2011
This is version 41 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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