Reviewed,
UniProtKB/Swiss-Prot P25995 (PYRC_BACSU)
Last modified
February 9, 2010.
Version 86.
History...
Clusters with 100%,
90%,
50% identity |
 Documents (3) |
 Third-party data |
 Customize display | text xml rdf/xml gff fasta |
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Dihydroorotase Short name=DHOase EC=3.5.2.3 | ||||
| Gene names |
| ||||
| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
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 |
| Cofactor | Binds 2 zinc ions per subunit By similarity. HAMAP MF_00220 |
| Pathway | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00220 |
| Subunit structure | Homodimer. HAMAP MF_00220 |
| 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: HAMAP |
| Molecular function | dihydroorotase activity Inferred from electronic annotation. Source: HAMAP zinc ion bindingInferred from electronic annotation. Source: HAMAP |
| 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 | PRO_0000147229 | |||||
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 | ||||||
Experimental info | |||||||||
| Sequence conflict | 81 | 1 | A → G in AAA21268. Ref.1 | ||||||
| Sequence conflict | 220 – 222 | 3 | AEA → LG in AAA21268. Ref.1 | ||||||
| Sequence conflict | 323 – 351 | 29 | GIVGL…KQLID → RNCRLRNSIPASLHTLCQKW QLVTEAADLT in AAA21268. Ref.1 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Functional organization and nucleotide sequence of the Bacillus subtilis pyrimidine biosynthetic operon." Quinn C.L., Stephenson B.T., Switzer R.L. J. Biol. Chem. 266:9113-9127(1991) [PubMed: 1709162] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.  Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M59757 Genomic DNA. Translation: AAA21268.1. AL009126 Genomic DNA. Translation: CAB13424.2. |
| PIR | DEBSO. D39845. |
| RefSeq | NP_389433.2. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M38.972. |
Genome annotation databases | |
| GeneID | 937095. |
| GenomeReviews | Gene locus BSU15500 in contig AL009126_GR. |
| KEGG | bsu:BSU15500. |
| NMPDR | fig|224308.1.peg.1552. |
Organism-specific databases | |
| SubtiList | BG10714. pyrC. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG724623. |
Enzyme and pathway databases | |
| BRENDA | 3.5.2.3. 150. |
Family and domain databases | |
| HAMAP | MF_00220_B. PyrC_type2_B. [Tree] |
| InterPro | IPR006680. Amidohydro_1. IPR004722. DHOmult. IPR002195. Dihydroorotase_CS. IPR011059. Metal-dep_hydrolase_composite. [Graphical view] |
| Pfam | PF01979. Amidohydro_1. 1 hit. [Graphical view] |
| 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_BACSU | ||||||||
| Accession | Primary (citable) accession number: P25995 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |
