Q81RZ3 (DEOC_BACAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 70.
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 Short name=DERA EC=4.1.2.4 Alternative name(s): 2-deoxy-D-ribose 5-phosphate aldolase Phosphodeoxyriboaldolase Short name=Deoxyriboaldolase | ||||||
| Gene names |
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| Organism | Bacillus anthracis | ||||||
| Taxonomic identifier | 1392 [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 |
| 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 Reference 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 HAMAP MF_00114 | PRO_0000057221 | |||||
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 genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M.Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton. |
| [2] | "Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor. |
| [3] | "Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016879 Genomic DNA. Translation: AAP25789.1. AE017334 Genomic DNA. Translation: AAT31011.1. AE017225 Genomic DNA. Translation: AAT54069.1. |
| RefSeq | NP_844303.1. NC_003997.3. YP_018536.1. NC_007530.2. YP_028018.1. NC_005945.1. |
3D structure databases | |
| ProteinModelPortal | Q81RZ3. |
| SMR | Q81RZ3. Positions 2-213. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000009426; EBBACP00000009182; EBBACG00000009418. EBBACT00000016516; EBBACP00000016137; EBBACG00000016508. EBBACT00000021004; EBBACP00000020489; EBBACG00000020995. |
| GeneID | 1086144. 2817019. 2851412. |
| GenomeReviews | Gene locus BA_1892 in contig AE016879_GR. Gene locus BAS1754 in contig AE017225_GR. Gene locus GBAA_1892 in contig AE017334_GR. |
| KEGG | ban:BA_1892. bar:GBAA_1892. bat:BAS1754. |
| TIGR | BA_1892. GBAA_1892. |
Phylogenomic databases | |
| GeneTree | EBGT00050000000908. |
| HOGENOM | HBG636421. |
| OMA | CLEAREN. |
| ProtClustDB | PRK00507. |
Enzyme and pathway databases | |
| BioCyc | BANT260799:BAS1754-MONOMER. BANT261594:GBAA1892-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 | DEOC_BACAN | ||||||||
| Accession | Primary (citable) accession number: Q81RZ3 Secondary accession number(s): Q6I070, Q6KU47 | ||||||||
| 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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