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Reviewed, UniProtKB/Swiss-Prot A1W7S6 (PYRD_ACISJ)

Last modified June 16, 2009. Version 22. 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: Ajs_2132
OrganismAcidovorax sp. (strain JS42) [Complete proteome] [HAMAP]
Taxonomic identifier232721 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + O2 = orotate + H2O2. HAMAP MF_00225

Cofactor

Binds 1 FMN per subunit By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 4/6. HAMAP MF_00225

Subunit structure

Homodimer By similarity.

Subcellular location

Cell membrane; Peripheral membrane protein By 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: UniProtKB-SubCell

   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 – 351351Dihydroorotate dehydrogenase HAMAP MF_00225
PRO_1000024145

Sites

Active site1861Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
A1W7S6-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 25A3529D16DFA89D

FASTA35137,431
        10         20         30         40         50         60 
MSLLPYALAR SFLFGMDAEA AHELTMDMLA RGQRTPLQWA WCNETVSDPI ELAGLRFPNR 

        70         80         90        100        110        120 
VGLAAGLDKN ARCIDALAAM GFGFVEVGTV TPRAQPGNPK PRMFRLPEAR ALINRLGFNN 

       130        140        150        160        170        180 
EGLDAFVANV QRSQVRTQGR GQSKLLLGLN IGKNATTPIE DATRDYLTCL EGVYPHADYV 

       190        200        210        220        230        240 
TVNISSPNTQ NLRALQSDAA LDGLLGAIAE HREQLAAAQG RRVPIFVKIA PDLDEAQVAV 

       250        260        270        280        290        300 
IATTLQRHGM DGVVATNTTI RRDAVQGLRH AGETGGLSGA PVLEASNAVI RQLRAALGPT 

       310        320        330        340        350 
FPIIGVGGIL SAEDAVSKIR AGADVVQIYT GLIYEGPALV GRAAKAIRDL R 

« Hide

References

[1]"Complete sequence of chromosome 1 of Acidovorax sp. JS42."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000539 Genomic DNA. Translation: ABM42301.1.
RefSeqYP_986377.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4670618.
GenomeReviewsGene locus Ajs_2132 in contig CP000539_GR.
KEGGajs:Ajs_2132.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAA1W7S6. NAEQQGG.

Family and domain databases

HAMAPMF_00225.
[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.
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_ACISJ
AccessionPrimary (citable) accession number: A1W7S6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: June 16, 2009
This is version 22 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