B3DS59 (B3DS59_BIFLD) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 29.
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 | Submitted name: Dihydroorotase EMBL ACD97978.1 | ||||
| Gene names |
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| Organism | Bifidobacterium longum (strain DJO10A) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 205913 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium |
Protein attributes
| Sequence length | 498 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | (S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. SAAS SAAS002195 |
| Cofactor | Binds 2 zinc ions per subunit By similarity. SAAS SAAS002195 |
| Pathway | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. SAAS SAAS002195 |
| Subunit structure | Homodimer By similarity. SAAS SAAS002195 |
| Sequence similarities | Belongs to the DHOase family. RuleBase RU004949 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyrimidine biosynthesis SAAS SAAS002195 |
| Ligand | Metal-binding SAAS SAAS002195 RuleBase RU004949 Zinc SAAS SAAS002195 |
| Molecular function | Hydrolase SAAS SAAS002195 RuleBase RU004949 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides Inferred from electronic annotation. Source: InterPro metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequences
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References
| [1] | "Comparative genomic analysis of the gut bacterium Bifidobacterium longum reveals loci susceptible to deletion during pure culture growth." Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R., Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V., Slesarev A.I., Weimer B., O'Sullivan D.J. BMC Genomics 9:247-247(2008) [PubMed: 18505588] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000605 Genomic DNA. Translation: ACD97978.1. |
| RefSeq | YP_001954476.1. NC_010816.1. |
3D structure databases | |
| ProteinModelPortal | B3DS59. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B3DS59. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 6363346. |
| GenomeReviews | Gene locus BLD_0532 in contig CP000605_GR. |
| KEGG | blj:BLD_0532. |
| PATRIC | 21113990. VBIBifLon134794_0544. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG724623. |
| OMA | CDVHPVG. |
| ProtClustDB | CLSK572777. |
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. |
| PROSITE | PS00482. DIHYDROOROTASE_1. 1 hit. PS00483. DIHYDROOROTASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | B3DS59_BIFLD | ||||||||
| Accession | Primary (citable) accession number: B3DS59 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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