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Reviewed, UniProtKB/Swiss-Prot O66990 (PYRC_AQUAE)

Last modified September 2, 2008. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3
Gene names
Name: pyrC
Ordered Locus Names: aq_806
OrganismAquifex aeolicus [Complete proteome] [HAMAP]
Taxonomic identifier63363 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Pathway

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

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the DHOase family. Type 2 subfamily.

Ontologies

Keywords

   Biological processPyrimidine biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome

Gene Ontology (GO)

   Biological processpyrimidine nucleotide biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Molecular functiondihydroorotase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Dihydroorotase
PRO_0000147226

Sites

Metal binding611Zinc 1 By similarity
Metal binding631Zinc 1 By similarity
Metal binding1431Zinc 1; via carbamate group By similarity
Metal binding1431Zinc 2; via carbamate group By similarity
Metal binding1801Zinc 2 By similarity
Metal binding2321Zinc 2 By similarity
Metal binding3051Zinc 1 By similarity

Amino acid modifications

Modified residue1431N6-carboxylysine

Secondary structure

....................................................................... 422
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O66990-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 7004E6A48B0165EB

FASTA42246,380
        10         20         30         40         50         60 
MLKLIVKNGY VIDPSQNLEG EFDILVENGK IKKIDKNILV PEAEIIDAKG LIVCPGFIDI 

        70         80         90        100        110        120 
HVHLRDPGQT YKEDIESGSR CAVAGGFTTI VCMPNTNPPI DNTTVVNYIL QKSKSVGLCR 

       130        140        150        160        170        180 
VLPTGTITKG RKGKEIADFY SLKEAGCVAF TDDGSPVMDS SVMRKALELA SQLGVPIMDH 

       190        200        210        220        230        240 
CEDDKLAYGV INEGEVSALL GLSSRAPEAE EIQIARDGIL AQRTGGHVHI QHVSTKLSLE 

       250        260        270        280        290        300 
IIEFFKEKGV KITCEVNPNH LLFTEREVLN SGANARVNPP LRKKEDRLAL IEGVKRGIID 

       310        320        330        340        350        360 
CFATDHAPHQ TFEKELVEFA MPGIIGLQTA LPSALELYRK GIISLKKLIE MFTINPARII 

       370        380        390        400        410        420 
GVDLGTLKLG SPADITIFDP NKEWILNEET NLSKSRNTPL WGKVLKGKVI YTIKDGKMVY 


KD 

« 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

AE000657 Genomic DNA. Translation: AAC06948.1.
PIRC70370.
RefSeqNP_213551.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1XRFX-ray1.65A1-422[»]
1XRTX-ray1.61A/B1-422[»]
ModBaseSearch...

Genome annotation databases

GeneID1193440.
GenomeReviewsGene locus aq_806 in contig AE000657_GR.
KEGGaae:aq_806.
NMPDRfig|224324.1.peg.566.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO66990.

Enzyme and pathway databases

BioCycAAEO224324:AQ_806-MON.

Family and domain databases

HAMAPMF_00220.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004722. DHOmult.
IPR002195. Dihydroorotase_CS.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR00857. pyrC_multi. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_AQUAE
AccessionPrimary (citable) accession number: O66990
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: September 2, 2008
This is version 68 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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