Q5QWC6 (PYRC_IDILO) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 42.
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 | Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 283942 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Idiomarinaceae › Idiomarina |
Protein attributes
| Sequence length | 344 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 – 344 | 344 | Dihydroorotase HAMAP MF_00219 | PRO_1000024018 | |||||
Sites | |||||||||
| Metal binding | 13 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 15 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 99 | 1 | Zinc 1; via carbamate group By similarity | ||||||
| Metal binding | 99 | 1 | Zinc 2; via carbamate group By similarity | ||||||
| Metal binding | 136 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 174 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 247 | 1 | Zinc 1 By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 99 | 1 | N6-carboxylysine By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy." Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. Alam M.Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed: 15596722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-735 / DSM 15497 / L2-TR. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017340 Genomic DNA. Translation: AAV81205.1. |
| RefSeq | YP_154754.1. NC_006512.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1J79 based on UniProtKB P05020. |
| ProteinModelPortal | Q5QWC6. |
| SMR | Q5QWC6. Positions 2-343. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 3172502. |
| GenomeReviews | Gene locus IL0362 in contig AE017340_GR. |
| KEGG | ilo:IL0362. |
| NMPDR | fig|283942.3.peg.446. |
| PATRIC | 22138745. VBIIdiLoi21852_0364. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG628648. |
| OMA | CLPVAKR. |
| ProtClustDB | PRK05451. |
Enzyme and pathway databases | |
| BioCyc | ILOI283942:IL0362-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_IDILO | ||||||||
| Accession | Primary (citable) accession number: Q5QWC6 | ||||||||
| 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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