Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q2IQI6 (PYRD_ANADE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Adeh_1294
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Anaeromyxobacter

Protein attributes

Sequence length364 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 – 364364Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_1000024149

Regions

Nucleotide binding62 – 665FMN By similarity
Nucleotide binding317 – 3182FMN By similarity
Region111 – 1155Substrate binding By similarity
Region245 – 2462Substrate binding By similarity

Sites

Active site1781Nucleophile By similarity
Binding site661Substrate By similarity
Binding site861FMN; via amide nitrogen By similarity
Binding site1421FMN By similarity
Binding site1751FMN By similarity
Binding site1751Substrate By similarity
Binding site1801Substrate By similarity
Binding site2161FMN By similarity
Binding site2441FMN; via carbonyl oxygen By similarity
Binding site2671FMN; via amide nitrogen By similarity
Binding site2961FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2IQI6 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: B750C3601ADADEC6

FASTA36438,378
        10         20         30         40         50         60 
MLWPALRSVL FQLDPERVHH LAHWALHRVP PALARARRPA PVPALAVRCM GLDFDGPMGL 

        70         80         90        100        110        120 
AAGFDKGDVA LPGLFGLGFS HVEIGTITPR PQPGNDRPRL FRLPEHRALL NRMGFNNEGM 

       130        140        150        160        170        180 
EACARRLAAL PAAARLGPVG INVGKNKATP NEDAASDYLA CIERLHPYAD YLVVNISSPN 

       190        200        210        220        230        240 
TPGLRQLQER EALDRLLRAC VRHLAERAPG KPLLVKLAPD LSPEALDEAV DVAIAAGAAG 

       250        260        270        280        290        300 
IVATNTTLSR AGVERHPRAA EAGGLSGAPL ERLATEVVRR CYARAAGRVP IVGVGGVMDA 

       310        320        330        340        350        360 
EGAYAKIRAG ATLVQAYTGL IYGGPGFVGR VNAGLARLLE RDGFSTLSDA VGADHRQGGG 


KAAG

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2CP-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000251 Genomic DNA. Translation: ABC81068.1.
RefSeqYP_464505.1. NC_007760.1.

3D structure databases

ProteinModelPortalQ2IQI6.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2IQI6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3888688.
GenomeReviewsGene locus Adeh_1294 in contig CP000251_GR.
KEGGade:Adeh_1294.
PATRIC20918705. VBIAnaDeh31384_1343.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHBG351027.
OMAAALNRMG.
PhylomeDBQ2IQI6.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycADEH290397:ADEH_1294-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_ANADE
AccessionPrimary (citable) accession number: Q2IQI6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 7, 2006
Last modified: January 25, 2012
This is version 46 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents