B1X9H5 (PYRC_ECODH) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 29.
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 | Escherichia coli (strain K12 / DH10B) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 316385 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 348 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | (S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00219 |
| Cofactor | Binds 2 zinc ions per subunit By similarity. HAMAP MF_00219 |
| Pathway | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00219 |
| Subunit structure | Homodimer By similarity. HAMAP MF_00219 |
| Sequence similarities | Belongs to the DHOase family. Type 1 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyrimidine biosynthesis |
| Ligand | Metal-binding Zinc |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic processInferred 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 – 348 | 348 | Dihydroorotase HAMAP MF_00219 | PRO_1000100042 | |||||
Sites | |||||||||
| Metal binding | 17 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 19 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 103 | 1 | Zinc 1; via carbamate group By similarity | ||||||
| Metal binding | 103 | 1 | Zinc 2; via carbamate group By similarity | ||||||
| Metal binding | 140 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 178 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 251 | 1 | Zinc 1 By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 103 | 1 | N6-carboxylysine By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse." Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., Posfai G., Weinstock G.M., Blattner F.R. J. Bacteriol. 190:2597-2606(2008) [PubMed: 18245285] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / DH10B. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000948 Genomic DNA. Translation: ACB02255.1. |
| RefSeq | YP_001730033.1. NC_010473.1. |
3D structure databases | |
| ProteinModelPortal | B1X9H5. |
| SMR | B1X9H5. Positions 4-347. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B1X9H5. |
Protein family/group databases | |
| MEROPS | M38.A02. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000012279; EBESCP00000011807; EBESCG00000011341. |
| GeneID | 6059070. |
| GenomeReviews | Gene locus ECDH10B_1133 in contig CP000948_GR. |
| KEGG | ecd:ECDH10B_1133. |
| PATRIC | 18462116. VBIEscCol59506_1157. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000011208. |
| HOGENOM | HBG628648. |
| OMA | CLPVAKR. |
| ProtClustDB | PRK05451. |
Enzyme and pathway databases | |
| BioCyc | ECOL316385:ECDH10B_1133-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00219. PyrC_type1. [Tree] |
| InterPro | IPR006680. Amidohydro_1. IPR004721. DHOdimr. IPR002195. Dihydroorotase_CS. [Graphical view] |
| KO | K01465. |
| Pfam | PF01979. Amidohydro_1. 1 hit. [Graphical view] |
| PIRSF | PIRSF001237. DHOdimr. 1 hit. |
| TIGRFAMs | TIGR00856. PyrC_dimer. 1 hit. |
| PROSITE | PS00482. DIHYDROOROTASE_1. 1 hit. PS00483. DIHYDROOROTASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PYRC_ECODH | ||||||||
| Accession | Primary (citable) accession number: B1X9H5 | ||||||||
| 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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