Reviewed,
UniProtKB/Swiss-Prot A4XKT2 (PYRC_CALS8)
Last modified
September 2, 2008.
Version 14.
History...
Clusters with 100%,
90%,
50% identity |
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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 | Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 351627 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Caldicellulosiruptor |
Protein attributes
| Sequence length | 430 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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 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 – 430 | 430 | Dihydroorotase | PRO_0000325590 | |||||
Sites | |||||||||
| Metal binding | 61 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 63 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 143 | 1 | Zinc 1; via carbamate group By similarity | ||||||
| Metal binding | 143 | 1 | Zinc 2; via carbamate group By similarity | ||||||
| Metal binding | 180 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 233 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 306 | 1 | Zinc 1 By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 143 | 1 | N6-carboxylysine By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. Richardson P.Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000679 Genomic DNA. Translation: ABP67517.1. | |
| RefSeq | YP_001180708.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5089294. |
| GenomeReviews | Gene locus Csac_1932 in contig CP000679_GR. |
| KEGG | csc:Csac_1932. |
Organism-specific databases | |
| CMR | Search... |
Family and domain databases | |
| HAMAP | MF_00220. [Tree] |
| InterPro | IPR006680. Amidohydro_1. IPR004722. DHOmult. IPR002195. Dihydroorotase_CS. [Graphical view] |
| Pfam | PF01979. Amidohydro_1. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00857. pyrC_multi. 1 hit. |
| PROSITE | PS00482. DIHYDROOROTASE_1. False negative. PS00483. DIHYDROOROTASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PYRC_CALS8 | ||||||||
| Accession | Primary (citable) accession number: A4XKT2 | ||||||||
| 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 |

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