B3YRJ7 (B3YRJ7_BACCE) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 22.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Deoxyribose-phosphate aldolase HAMAP MF_00114 Short name=DERA HAMAP MF_00114 EC=4.1.2.4 HAMAP MF_00114 Alternative name(s): 2-deoxy-D-ribose 5-phosphate aldolase HAMAP MF_00114 Phosphodeoxyriboaldolase HAMAP MF_00114 | ||||||
| Gene names |
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| Organism | Bacillus cereus W EMBL EDX57765.1 | ||||||
| Taxonomic identifier | 405917 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 223 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate By similarity. HAMAP MF_00114 SAAS SAAS022979 |
| Catalytic activity | 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. HAMAP MF_00114 SAAS SAAS022979 |
| Pathway | Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2. HAMAP MF_00114 SAAS SAAS022979 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00114 SAAS SAAS022979. |
| Sequence similarities | Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily. HAMAP MF_00114 |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm HAMAP MF_00114 SAAS SAAS022979 |
| Ligand | Schiff base SAAS SAAS022979 HAMAP MF_00114 |
| Molecular function | Lyase HAMAP MF_00114 SAAS SAAS022979 EMBL EDX57765.1 |
| Gene Ontology (GO) | |
| Biological process | carbohydrate catabolic process Inferred from electronic annotation. Source: HAMAP deoxyribonucleotide catabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | deoxyribose-phosphate aldolase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 152 | 1 | Schiff-base intermediate with acetaldehyde By similarity HAMAP MF_00114 | ||||||
| Active site | 181 | 1 | By similarity HAMAP MF_00114 | ||||||
Sequences
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References
| [1] | "Genome sequence of Bacillus cereus W." Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Ravel J., Sutton G. Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: W EMBL EDX57765.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | ABCZ02000003 Genomic DNA. Translation: EDX57765.1. |
3D structure databases | |
| ProteinModelPortal | B3YRJ7. |
| SMR | B3YRJ7. Positions 2-213. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| PATRIC | 25108199. VBIBacCer31393_1385. |
Family and domain databases | |
| HAMAP | MF_00114. DeoC_type1. [Tree] |
| InterPro | IPR013785. Aldolase_TIM. IPR011343. DeoC. IPR002915. DeoC/AroFGH_arch. IPR022979. Deoxyribose_phosphate_aldo_1. [Graphical view] |
| Gene3D | G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. |
| PANTHER | PTHR10889. DeoC. 1 hit. |
| Pfam | PF01791. DeoC. 1 hit. [Graphical view] |
| PIRSF | PIRSF001357. DeoC. 1 hit. |
| TIGRFAMs | TIGR00126. DeoC. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | B3YRJ7_BACCE | ||||||||
| Accession | Primary (citable) accession number: B3YRJ7 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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