Reviewed,
UniProtKB/Swiss-Prot Q8X8N8 (PYRC_ECO57)
Last modified
November 25, 2008.
Version 50.
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 |
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| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 348 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | (S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate. |
| Cofactor | Binds 2 zinc ions per subunit By similarity. |
| Pathway | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 3/6. |
| Subunit structure | Homodimer By similarity. |
| 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: 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 348 | 347 | Dihydroorotase | PRO_0000147207 | |||||
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] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| AE005174 Genomic DNA. Translation: AAG55808.1. BA000007 Genomic DNA. Translation: BAB34863.1. | |
| PIR | D85668. H90808. |
| RefSeq | NP_287196.1. NP_309467.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1J79 based on UniProtKB P05020. |
| SMR | Q8X8N8. Positions 5-347. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 914110. 959400. |
| GenomeReviews | Gene locus ECs1440 in contig BA000007_GR. Gene locus Z1699 in contig AE005174_GR. |
| KEGG | ece:Z1699. ecs:ECs1440. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8X8N8. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS1440-MON. |
Family and domain databases | |
| HAMAP | MF_00219. [Tree] |
| InterPro | IPR006680. Amidohydro_1. IPR004721. DHOdimr. IPR002195. Dihydroorotase_CS. [Graphical view] |
| 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_ECO57 | ||||||||
| Accession | Primary (citable) accession number: Q8X8N8 | ||||||||
| 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


