B7HLM2 (PYRC_BACC7) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 26.
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 AH187) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 405534 [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 |
| 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_1000193091 | |||||
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 AH187." Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B., Okstad O.A., Ravel J., Sutton G. Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AH187. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001177 Genomic DNA. Translation: ACJ78020.1. |
| RefSeq | YP_002339877.1. NC_011658.1. |
3D structure databases | |
| ProteinModelPortal | B7HLM2. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B7HLM2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000093579; EBBACP00000088411; EBBACG00000093572. |
| GeneID | 7078329. |
| GenomeReviews | Gene locus BCAH187_A3937 in contig CP001177_GR. |
| KEGG | bcr:BCAH187_A3937. |
| PATRIC | 18833309. VBIBacCer120511_4125. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000001626. |
| HOGENOM | HBG724623. |
| OMA | CDVHPVG. |
| ProtClustDB | PRK09357. |
Family and domain databases | |
| HAMAP | MF_00220_B. PyrC_type2_B. [Tree] |
| InterPro | IPR006680. Amidohydro_1. IPR004722. DHOase. IPR002195. Dihydroorotase_CS. IPR011059. Metal-dep_hydrolase_composite. [Graphical view] |
| KO | K01465. |
| Pfam | PF01979. Amidohydro_1. 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_BACC7 | ||||||||
| Accession | Primary (citable) accession number: B7HLM2 | ||||||||
| 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 |

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