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Reviewed, UniProtKB/Swiss-Prot O66461 (PYRD_AQUAE)

Last modified June 16, 2009. Version 70. 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: aq_046
OrganismAquifex aeolicus [Complete proteome] [HAMAP]
Taxonomic identifier63363 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length306 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_00224

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_00224

Subunit structure

Heterotetramer of 2 pyrK and 2 pyrD subunits By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCytoplasm
   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 componentcytoplasm

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 – 306306Dihydroorotate dehydrogenase HAMAP MF_00224
PRO_0000148386

Sites

Active site1291Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
O66461-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 3E1E04D8DE1FCD53

FASTA30633,523
        10         20         30         40         50         60 
MDLSVELFGI RFKNPVWVAS GTFGYGVEAA EIYDISKLGA VVTKGLSLKE RLGNETPRIV 

        70         80         90        100        110        120 
ETPCGMLNSI GLQNPGVEKF LKEIYPKIKD VDTHFIANVF GETEEEYVEV CMALEDADKI 

       130        140        150        160        170        180 
VAYELNVSCP NVKKGGILFG HDPVILGNLV DRIKAKIKKP LLVKLSPNVT DVTEFAKVCI 

       190        200        210        220        230        240 
ENGADGLVLI NTLMGMKINI WKRKPDLATK TGGLSGPAIL PIAVRMIYQV YEKFGDRIPI 

       250        260        270        280        290        300 
IGVGGITTWE DAMEHVMAGA SAVQVGTANF YEPLAPLKVI EGIENFMKSQ NIKDFKELIG 


IAHRVE 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

AE000657 Genomic DNA. Translation: AAC06426.1.
PIRB70304.
RefSeqNP_213021.1.

3D structure databases

HSSPHSSP built from PDB template 1EP3 based on UniProtKB P54322.
ModBaseSearch...

Genome annotation databases

GeneID1192658.
GenomeReviewsGene locus aq_046 in contig AE000657_GR.
KEGGaae:aq_046.
NMPDRfig|224324.1.peg.36.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO66461.
OMAO66461. NSIGLQN.

Enzyme and pathway databases

BioCycAAEO224324:AQ_046-MON.
BRENDA1.3.3.1. 189781.

Family and domain databases

HAMAPMF_00224.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005720. Dihydroorotate_DH_1_core.
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.
TIGRFAMsTIGR01037. pyrD_sub1_fam. 1 hit.
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_AQUAE
AccessionPrimary (citable) accession number: O66461
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: June 16, 2009
This is version 70 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