Reviewed,
UniProtKB/Swiss-Prot A7ZVS4 (DEOC_ECO24)
Last modified
June 16, 2009.
Version 13.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Deoxyribose-phosphate aldolase EC=4.1.2.4 Alternative name(s): Phosphodeoxyriboaldolase Short name=Deoxyriboaldolase Short name=DERA | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 331111 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 259 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. HAMAP MF_00592 |
| Pathway | Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-D-ribose 1-phosphate: step 2/2. HAMAP MF_00592 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the deoC/fbaB aldolase family. DeoC type 2 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Schiff base |
| Molecular function | Lyase |
| PTM | Acetylation |
| Technical term | Complete proteome |
| 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 | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 259 | 259 | Deoxyribose-phosphate aldolase HAMAP MF_00592 | PRO_1000072594 | |||||
Sites | |||||||||
| Active site | 167 | 1 | Schiff-base intermediate with acetaldehyde By similarity | ||||||
| Active site | 201 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 167 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000800 Genomic DNA. Translation: ABV18972.1. | |
| RefSeq | YP_001465903.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5588059. |
| GenomeReviews | Gene locus EcE24377A_4980 in contig CP000800_GR. |
| KEGG | ecw:EcE24377A_4980. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | A7ZVS4. CKEACGD. |
Family and domain databases | |
| HAMAP | MF_00592. [Tree] |
| InterPro | IPR013785. Aldolase_TIM. IPR011343. DeoC. IPR002915. DeoC/AroFGH_arch. [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 | DEOC_ECO24 | ||||||||
| Accession | Primary (citable) accession number: A7ZVS4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


