Q6NH14 (Q6NH14_CORDI) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 58.
History...
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Dihydroorotase RuleBase RU003441 EC=3.5.2.3 RuleBase RU003441 | ||||
| Gene names |
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| Organism | Corynebacterium diphtheriae [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1717 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium |
Protein attributes
| Sequence length | 448 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | (S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. RuleBase RU003441 SAAS SAAS002195 |
| Cofactor | Binds 2 zinc ions per subunit By similarity. RuleBase RU003441 SAAS SAAS002195 |
| Pathway | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. RuleBase RU003441 SAAS SAAS002195 |
| Subunit structure | Homodimer By similarity. SAAS SAAS002195 |
| Sequence similarities | Belongs to the DHOase family. Type 2 subfamily. RuleBase RU003441 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyrimidine biosynthesis RuleBase RU003441 SAAS SAAS002195 |
| Ligand | Metal-binding RuleBase RU003441 SAAS SAAS002195 Zinc SAAS SAAS002195 RuleBase RU003441 |
| Molecular function | Hydrolase RuleBase RU003441 SAAS SAAS002195 EMBL CAE49861.1 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | pyrimidine nucleotide biosynthetic process Inferred 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... | |
Sequences
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References
| [1] | "The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129." Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D., De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K., Moule S. Parkhill J.Nucleic Acids Res. 31:6516-6523(2003) [PubMed: 14602910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700971 / NCTC 13129 / Biotype gravis. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX248357 Genomic DNA. Translation: CAE49861.1. |
| RefSeq | NP_939686.1. NC_002935.2. |
3D structure databases | |
| ProteinModelPortal | Q6NH14. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2649887. |
| GenomeReviews | Gene locus DIP1333 in contig BX248353_GR. |
| KEGG | cdi:DIP1333. |
| NMPDR | fig|257309.1.peg.1277. |
| PATRIC | 21483860. VBICorDip47633_1313. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG724623. |
| OMA | CDVHPVG. |
| PhylomeDB | Q6NH14. |
| ProtClustDB | PRK09357. |
Family and domain databases | |
| HAMAP | MF_00220_B. PyrC_type2_B. [Tree] |
| InterPro | IPR006680. Amidohydro_1. IPR004722. DHOase. IPR002195. Dihydroorotase_CS. IPR011059. Metal-dep_hydrolase_composite. [Graphical view] |
| KO | K01465. |
| Pfam | PF01979. Amidohydro_1. 1 hit. [Graphical view] |
| SUPFAM | SSF51338. Metalo_hydrolase. 1 hit. |
| 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 | Q6NH14_CORDI | ||||||||
| Accession | Primary (citable) accession number: Q6NH14 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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