Q65D22 (DEOC2_BACLD) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 54.
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: Deoxyribose-phosphate aldolase 2 Short name=DERA 2 EC=4.1.2.4 Alternative name(s): 2-deoxy-D-ribose 5-phosphate aldolase 2 Phosphodeoxyriboaldolase 2 Short name=Deoxyriboaldolase 2 | ||||||
| Gene names |
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| Organism | Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 279010 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
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 |
| Catalytic activity | 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. HAMAP MF_00114 |
| 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 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00114. |
| Sequence similarities | Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Schiff base |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | deoxyribonucleotide catabolic process Inferred 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: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 223 | 223 | Deoxyribose-phosphate aldolase 2 HAMAP MF_00114 | PRO_0000231532 | |||||
Sites | |||||||||
| Active site | 152 | 1 | Schiff-base intermediate with acetaldehyde By similarity | ||||||
| Active site | 181 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580. |
| [2] | "Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. Berka R.M.Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017333 Genomic DNA. Translation: AAU43042.1. CP000002 Genomic DNA. Translation: AAU25663.1. |
| RefSeq | YP_081301.1. NC_006270.3. YP_093735.1. NC_006322.1. |
3D structure databases | |
| ProteinModelPortal | Q65D22. |
| SMR | Q65D22. Positions 3-218. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q65D22. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000055542; EBBACP00000054073; EBBACG00000055533. EBBACT00000060560; EBBACP00000058993; EBBACG00000060551. |
| GeneID | 3031406. 3100763. |
| GenomeReviews | Gene locus BLi04229 in contig AE017333_GR. Gene locus BL00229 in contig CP000002_GR. |
| KEGG | bld:BLi04229. bli:BL00229. |
| NMPDR | fig|279010.5.peg.3883. |
| PATRIC | 18954284. VBIBacLic203714_4317. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0274. |
| GeneTree | EBGT00050000000908. |
| HOGENOM | HBG636421. |
| OMA | IDHTNLK. |
| PhylomeDB | Q65D22. |
| ProtClustDB | CLSK929138. |
Enzyme and pathway databases | |
| BioCyc | BLIC279010-1:BLI04229-MONOMER. BLIC279010:BL00229-MONOMER. |
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. |
| KO | K01619. |
| 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 | DEOC2_BACLD | ||||||||
| Accession | Primary (citable) accession number: Q65D22 Secondary accession number(s): Q62NJ8 | ||||||||
| 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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