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A7GRL3 (PYRC_BACCN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydroorotase
Short name=DHOase
EC=3.5.2.3
Gene names
Name:pyrC
Ordered Locus Names:Bcer98_2537
OrganismBacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]
Taxonomic identifier315749 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

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_0000325586

Sites

Metal binding591Zinc 1 By similarity
Metal binding611Zinc 1 By similarity
Metal binding1411Zinc 1; via carbamate group By similarity
Metal binding1411Zinc 2; via carbamate group By similarity
Metal binding1781Zinc 2 By similarity
Metal binding2311Zinc 2 By similarity
Metal binding3041Zinc 1 By similarity

Amino acid modifications

Modified residue1411N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7GRL3 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: CC9BA7F44AC4A21A

FASTA42846,650
        10         20         30         40         50         60 
MNYLFKNGRY LNEEGTIVAT DLLVQDGKIA KIAKNISAEN AEVIDVNGKL IAPGLVDVHV 

        70         80         90        100        110        120 
HLREPGGEHK ETIETGTLAA AKGGFTTICA MPNTRPVPDS KEHMEDLQKR IQEKAHVNVL 

       130        140        150        160        170        180 
PYGAITVRQA GSEMTDFETL KELGAFAFTD DGVGVQDASM MLAAMKRAAK LNMAVVAHCE 

       190        200        210        220        230        240 
ENTLINKGCV HEGKFSEKHG LNGIPSVCES VHIARDILLA EAADCHYHVC HVSTKGSVRV 

       250        260        270        280        290        300 
IRDAKRAGIK VTAEVTPHHL VLCEDDIPSV DPNFKMNPPL RGREDQEALI EGLLDGTIDI 

       310        320        330        340        350        360 
IATDHAPHTA EEKAQGIERA PFGITGFETA FPLLYTNLVK KGIITLEQLI QFLTEKPADT 

       370        380        390        400        410        420 
FGLETGRLKE GRAADITILD LEQEEKIDPT TFLSKGKNTP FAGWKCQGWP VMTLVGGKIV 


WQKESALV

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References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NVH 391-98.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000764 Genomic DNA. Translation: ABS22771.1.
RefSeqYP_001375766.1. NC_009674.1.

3D structure databases

ProteinModelPortalA7GRL3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7GRL3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000037983; EBBACP00000037034; EBBACG00000037974.
GeneID5344008.
GenomeReviewsGene locus Bcer98_2537 in contig CP000764_GR.
KEGGbcy:Bcer98_2537.
PATRIC18933672. VBIBacCyt128034_2680.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
GeneTreeEBGT00050000001626.
HOGENOMHBG724623.
OMACDVHPVG.
ProtClustDBPRK09357.

Enzyme and pathway databases

BioCycBCER315749:BCER98_2537-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_BACCN
AccessionPrimary (citable) accession number: A7GRL3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: September 11, 2007
Last modified: December 14, 2011
This is version 31 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

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