Reviewed,
UniProtKB/Swiss-Prot Q636D8 (PYRC_BACCZ)
Last modified
February 9, 2010.
Version 35.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Dihydroorotase Short name=DHOase EC=3.5.2.3 | ||||
| Gene names |
| ||||
| Organism | Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 288681 [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 |
| 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 By similarity. 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_0000325585 | |||||
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] | "Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. Gilna P.J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000001 Genomic DNA. Translation: AAU16619.1. |
| RefSeq | YP_085229.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1XRT based on UniProtKB O66990. |
| SMR | Q636D8. Positions 3-424. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q636D8. |
Genome annotation databases | |
| GeneID | 3024601. |
| GenomeReviews | Gene locus BCE33L3647 in contig CP000001_GR. |
| KEGG | bcz:BCZK3647. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0044. |
| HOGENOM | HBG724623. |
| OMA | VTTVVCQ. |
Enzyme and pathway databases | |
| BioCyc | BCER288681:BCE33L3647-MONOMER. |
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_BACCZ | ||||||||
| Accession | Primary (citable) accession number: Q636D8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


