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Reviewed, UniProtKB/Swiss-Prot Q2IQI6 (PYRD_ANADE)

Last modified November 25, 2008. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dihydroorotate dehydrogenase
    EC=1.3.3.1
Alternative name(s):
    Dihydroorotate oxidase
    DHOdehase
      Short name=DHODase
      Short name=DHOD
Gene names
Name: pyrD
Ordered Locus Names: Adeh_1294
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + O(2) = orotate + H(2)O(2).

Cofactor

Binds 1 FMN per subunit By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 4/6.

Subunit structure

Homodimer By similarity.

Subcellular location

Cell membrane; Peripheral membrane proteinBy similarity.

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

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentplasma membrane

Inferred from electronic annotation. Source: HAMAP

   Molecular functiondihydroorotate oxidase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 364364Dihydroorotate dehydrogenase
PRO_1000024149

Sites

Active site1781Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2IQI6-1 [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].

Cross-references

Sequence databases

CP000251 Genomic DNA. Translation: ABC81068.1.
RefSeqYP_464505.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

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

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2IQI6.

Enzyme and pathway databases

BioCycADEH290397:ADEH_1294-MON.

Family and domain databases

HAMAPMF_00225.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR012135. DHO_DHase_1_2.
IPR005719. DHO_DHase_2.
IPR001295. Dihydroorotate_DHase_core.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
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: November 25, 2008
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents