Q819S1 (PYRC_BACCR) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 53.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Dihydroorotase Short name=DHOase EC=3.5.2.3 | ||||
| Gene names |
| ||||
| Organism | Bacillus cereus (strain ATCC 14579 / DSM 31) | ||||
| Taxonomic identifier | 226900 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 428 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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 process | Pyrimidine biosynthesis |
| Ligand | Metal-binding Zinc |
| Molecular function | Hydrolase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | dihydroorotase activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 428 | 428 | Dihydroorotase HAMAP MF_00220_B | PRO_0000325584 | |||||
Sites | |||||||||
| Metal binding | 59 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 61 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 141 | 1 | Zinc 1; via carbamate group By similarity | ||||||
| Metal binding | 141 | 1 | Zinc 2; via carbamate group By similarity | ||||||
| Metal binding | 178 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 231 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 304 | 1 | Zinc 1 By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 141 | 1 | N6-carboxylysine By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. Kyrpides N.C.Nature 423:87-91(2003) [PubMed: 12721630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 14579 / DSM 31. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016877 Genomic DNA. Translation: AAP10809.1. |
| RefSeq | NP_833608.1. NC_004722.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1XRT based on UniProtKB O66990. |
| ProteinModelPortal | Q819S1. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q819S1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000033821; EBBACP00000033027; EBBACG00000033812. |
| GeneID | 1206233. |
| GenomeReviews | Gene locus BC_3888 in contig AE016877_GR. |
| KEGG | bce:BC3888. |
| PATRIC | 32603813. VBIBacCer54481_4010. |
Phylogenomic databases | |
| eggNOG | COG0044. |
| GeneTree | EBGT00050000001626. |
| HOGENOM | HBG724623. |
| OMA | CDVHPVG. |
| PhylomeDB | Q819S1. |
| ProtClustDB | PRK09357. |
Enzyme and pathway databases | |
| BioCyc | BCER226900:BC_3888-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00220_B. PyrC_type2_B. [Tree] |
| InterPro | IPR004722. DHOase. IPR024403. DHOase-like_bac. IPR002195. Dihydroorotase_CS. IPR011059. Metal-dep_hydrolase_composite. [Graphical view] |
| KO | K01465. |
| Pfam | PF12890. DHOase. 1 hit. [Graphical view] |
| SUPFAM | SSF51338. Metalo_hydrolase. 1 hit. |
| TIGRFAMs | TIGR00857. PyrC_multi. 1 hit. |
| PROSITE | PS00482. DIHYDROOROTASE_1. 1 hit. PS00483. DIHYDROOROTASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PYRC_BACCR | ||||||||
| Accession | Primary (citable) accession number: Q819S1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with