Skip Header

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

O66990 (PYRC_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Dihydroorotase
Short name=DHOase
EC=3.5.2.3
Gene names
Name:pyrC
Ordered Locus Names:aq_806
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00220_B

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP MF_00220_B

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00220_B

Subunit structure

Homodimer By similarity. HAMAP MF_00220_B

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
Reference proteome
Gene Ontology (GO)
   Biological processpyrimidine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiondihydroorotase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Dihydroorotase HAMAP MF_00220_B
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 HAMAP MF_00220_B

Secondary structure

1 ....................................................................... 422
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O66990 [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

EMBL
GenBank
DDBJ		AE000657 Genomic DNA. Translation: AAC06948.1.
PIRC70370.
RefSeqNP_213551.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XRFX-ray1.65A1-422[»]
1XRTX-ray1.61A/B1-422[»]
3D6NX-ray2.30A1-422[»]
ProteinModelPortalO66990.
SMRO66990. Positions 1-422.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1193440.
GenomeReviewsGene locus aq_806 in contig AE000657_GR.
KEGGaae:aq_806.
NMPDRfig|224324.1.peg.566.
PATRIC20959012. VBIAquAeo85532_0636.

Phylogenomic databases

HOGENOMHBG724623.
OMASHHQPHE.
PhylomeDBO66990.
ProtClustDBPRK09357.

Enzyme and pathway databases

BioCycAAEO224324:AQ_806-MONOMER.

Family and domain databases

HAMAPMF_00220_B. PyrC_type2_B.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004722. DHOase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
KOK01465.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
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: January 25, 2012
This is version 88 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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