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A5FHT2 (PYRD_FLAJ1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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:Fjoh_2210
OrganismFlavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) (Cytophaga johnsonae) [Complete proteome] [HAMAP]
Taxonomic identifier376686 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Flavobacterium

Protein attributes

Sequence length344 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 – 344344Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_0000336466

Regions

Nucleotide binding67 – 715FMN By similarity
Nucleotide binding322 – 3232FMN By similarity
Region116 – 1205Substrate binding By similarity
Region251 – 2522Substrate 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 site2221FMN By similarity
Binding site2501FMN; via carbonyl oxygen By similarity
Binding site2721FMN; via amide nitrogen By similarity
Binding site3011FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A5FHT2 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: C70668EEF290082A

FASTA34438,113
        10         20         30         40         50         60 
MYKLIIRPIL FWFDPEEVHY FTFSFVKFIS KIPGVSSIIR SIYEVKDSRL EREVFGIKFK 

        70         80         90        100        110        120 
NPVGLAAGFD KDAKLYKELS DFGFGFIEIG TVTPVGQEGN PKKRLFRLKE DQAIINRMGF 

       130        140        150        160        170        180 
NNGGVLEAVE RLKKNSGVLI GGNIGKNKVT DNEDAVKDYI ICFDALYNHV DYFVVNVSSP 

       190        200        210        220        230        240 
NTPNLRALQD KEPLTALLQT LQNRNVEKQK TSTQKVKPIL LKIAPDLTDE QLLDIIDIVK 

       250        260        270        280        290        300 
TTQIAGVIAT NTTISREGLQ SSNQSETGGL SGKPLTKRST EVIRFLSEKS NKAFPIIGVG 

       310        320        330        340 
GIHSADDAIE KLNAGASLVQ LYTGFIYEGP ALIKAINKKV LGQL

« Hide

References

[1]"Complete sequence of Flavobacterium johnsoniae UW101."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E., Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Xie G., McBride M., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17061 / DSM 2064 / UW101.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000685 Genomic DNA. Translation: ABQ05238.1.
RefSeqYP_001194557.1. NC_009441.1.

3D structure databases

ProteinModelPortalA5FHT2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5FHT2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5092216.
GenomeReviewsGene locus Fjoh_2210 in contig CP000685_GR.
KEGGfjo:Fjoh_2210.
PATRIC21898851. VBIFlaJoh53613_2277.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHBG351027.
OMAAALNRMG.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycFJOH376686:FJOH_2210-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. False negative.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_FLAJ1
AccessionPrimary (citable) accession number: A5FHT2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: January 25, 2012
This is version 43 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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