Q8UI99 (PYRC_AGRT5) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 62.
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 |
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| Organism | Agrobacterium tumefaciens (strain C58 / ATCC 33970) | ||||||
| Taxonomic identifier | 176299 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium |
Protein attributes
| Sequence length | 345 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 Reference 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 – 345 | 345 | Dihydroorotase HAMAP MF_00219 | PRO_0000147202 | |||||
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] | "The genome of the natural genetic engineer Agrobacterium tumefaciens C58." Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., Clendenning J. Nester E.W.Science 294:2317-2323(2001) [PubMed: 11743193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C58 / ATCC 33970. |
| [2] | "Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58." Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C. Slater S.Science 294:2323-2328(2001) [PubMed: 11743194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C58 / ATCC 33970. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE007869 Genomic DNA. Translation: AAK86214.2. |
| PIR | AF2625. E97407. |
| RefSeq | NP_353429.2. NC_003062.2. |
3D structure databases | |
| ProteinModelPortal | Q8UI99. |
| SMR | Q8UI99. Positions 2-345. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q8UI99. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1132437. |
| GenomeReviews | Gene locus Atu0399 in contig AE007869_GR. |
| KEGG | atu:Atu0399. |
| PATRIC | 20810483. VBIAgrTum91616_0390. |
Phylogenomic databases | |
| eggNOG | COG0418. |
| HOGENOM | HBG628648. |
| OMA | CLPVAKR. |
| PhylomeDB | Q8UI99. |
| ProtClustDB | PRK05451. |
Enzyme and pathway databases | |
| BioCyc | ATUM176299-1:ATU0399-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_AGRT5 | ||||||||
| Accession | Primary (citable) accession number: Q8UI99 | ||||||||
| 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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