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Q7CNB0 (PYRC_STRP8) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. 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

Names and origin

Protein namesRecommended name:
Dihydroorotase

Short name=DHOase
EC=3.5.2.3
Gene names
Name:pyrC
Ordered Locus Names:spyM18_0965
OrganismStreptococcus pyogenes serotype M18 (strain MGAS8232) [Complete proteome] [HAMAP]
Taxonomic identifier186103 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP-Rule MF_00220

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP-Rule MF_00220

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP-Rule MF_00220

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00220

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_process'de novo' UMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functiondihydroorotase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Dihydroorotase HAMAP-Rule MF_00220
PRO_0000147260

Sites

Metal binding591Zinc 1 By similarity
Metal binding611Zinc 1 By similarity
Metal binding1771Zinc 2 By similarity
Metal binding2301Zinc 2 By similarity
Metal binding3031Zinc 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7CNB0 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 53AA427590977D12

FASTA42245,248
        10         20         30         40         50         60 
MILIKNGRVM DPKSQRDQVA DVLIDGKQIV KIASAIECQE AQVIDASGLI VAPGLVDIHV 

        70         80         90        100        110        120 
HFREPGQTHK EDIHTGALAA AAGGVTTVVM MANTNPVISD VETLQEVLAS AAKEKIHIYT 

       130        140        150        160        170        180 
NASVTQAFNG KDVTDFKALL EAGAVSFSDD GIPLESSKVL KEAFDLANAN QTFISLHEED 

       190        200        210        220        230        240 
PQLNGVLGFN EGIAEEHFHF CGATGVAEYS MIARDVMIAY DRQAHVHIQH LSKAESVQVV 

       250        260        270        280        290        300 
AFAQQLGAKV TAEVSPQHFS TTEDLLLTAG TSAKMNPPLR TQRDRLAVIE GLKSGVITVI 

       310        320        330        340        350        360 
ATDHAPHHKD EKAVDDMTKA PSGMTGLETS LSLGLTHLVE PGHLTLMSLL EKMTLNPALL 

       370        380        390        400        410        420 
YGFDAGYLAE NGPADLVIFA DKQERLITEN FASKASNSPF IGNKLKGVVK YTIADGEVVY 


PN 

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References

[1]"Genome sequence and comparative microarray analysis of serotype M18 group A Streptococcus strains associated with acute rheumatic fever outbreaks."
Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S., Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A., Veasy L.G., Musser J.M.
Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MGAS8232.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009949 Genomic DNA. Translation: AAL97606.1.
RefSeqNP_607107.1. NC_003485.1.

3D structure databases

ProteinModelPortalQ7CNB0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186103.spyM18_0965.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL97606; AAL97606; spyM18_0965.
GeneID993545.
KEGGspm:spyM18_0965.
PATRIC19748531. VBIStrPyo4396_0855.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHOG000219142.
KOK01465.
OMAHHLTLTE.
OrthoDBEOG6KHFW6.
ProtClustDBPRK09357.

Enzyme and pathway databases

BioCycSPYO186103:GHJG-826-MONOMER.
UniPathwayUPA00070; UER00117.

Family and domain databases

Gene3D2.30.40.10. 1 hit.
HAMAPMF_00220_B. PyrC_type2_B.
InterProIPR004722. DHOase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMSSF51338. SSF51338. 2 hits.
TIGRFAMsTIGR00857. pyrC_multi. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_STRP8
AccessionPrimary (citable) accession number: Q7CNB0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways