Skip Header

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

Q5L0U5 (PYRC_GEOKA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:GK1150
OrganismGeobacillus kaustophilus (strain HTA426) [Complete proteome] [HAMAP]
Taxonomic identifier235909 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 termComplete 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 – 428428Dihydroorotase HAMAP MF_00220_B
PRO_1000024083

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 binding2331Zinc 2 By similarity
Metal binding3061Zinc 1 By similarity

Amino acid modifications

Modified residue1431N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5L0U5 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 51B1DC25EE06C01A

FASTA42846,177
        10         20         30         40         50         60 
MGVWLKNGMS FNKDGELMRT HIKIEHGTIA AILYEQPLEA NEEDVIDVGG RLIVPGLIDL 

        70         80         90        100        110        120 
HVHLREPGGE AKETIETGTL AAAKGGFTTV AAMPNTNPAP DRKEQMEWLQ ARIRETARVN 

       130        140        150        160        170        180 
VLPYAAITIG QKGEELTDFA ALKEAGAFAF TDDGVGVQSA GMMFEAMKQA AALDMAIVAH 

       190        200        210        220        230        240 
CEDDTLTNGG AVHDGEFARR YGLRGIPSVC EAVHIARDVL LAEAAGCHYH VCHISTKESV 

       250        260        270        280        290        300 
RVVRDAKRAG IRVTAEVTPH HLLLCDEDIP GLDANYKMNP PLRSREDRDA LIEGLLDGTI 

       310        320        330        340        350        360 
DFIATDHAPH TAAEKAKGIE AAPFGIVGLE TAFPLLYTHF VKTGVFTLKQ LVDWLTIKPA 

       370        380        390        400        410        420 
QCFGLKAGRL AVGAPADIAV IDLETEEAID PETFASKGKN TPFAGWVCQG WPVMTFVGGT 


LVWEKGRA

« Hide

References

[1]"Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus."
Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., Matsui S., Uchiyama I.
Nucleic Acids Res. 32:6292-6303(2004) [PubMed: 15576355] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTA426.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000043 Genomic DNA. Translation: BAD75435.1.
RefSeqYP_147003.1. NC_006510.1.

3D structure databases

HSSPHSSP built from PDB template 1XRT based on UniProtKB O66990.
ProteinModelPortalQ5L0U5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3185137.
GenomeReviewsGene locus GK1150 in contig BA000043_GR.
KEGGgka:GK1150.
NMPDRfig|235909.3.peg.2213.
PATRIC21963563. VBIGeoKau81518_1251.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG724623.
OMACDVHPVG.
ProtClustDBPRK09357.

Enzyme and pathway databases

BioCycGKAU235909:GK1150-MONOMER.

Family and domain databases

HAMAPMF_00220_B. PyrC_type2_B.
[Tree]
InterProIPR004722. DHOase.
IPR024403. DHOase-like_bac.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
KOK01465.
PfamPF12890. DHOase. 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_GEOKA
AccessionPrimary (citable) accession number: Q5L0U5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 1, 2005
Last modified: January 25, 2012
This is version 47 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

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