Reviewed,
UniProtKB/Swiss-Prot P39071 (DHBA_BACSU)
Last modified
November 25, 2008.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase EC=1.3.1.28 Alternative name(s): Cold shock protein CSI14 | ||||||
| Gene names |
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| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 261 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | 2,3-dihydro-2,3-dihydroxybenzoate + NAD(+) = 2,3-dihydroxybenzoate + NADH. |
| Pathway | |
| Subcellular location | |
| Induction | In response to low temperature. |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Stress response |
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | enterobactin biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW response to stressInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase activity Inferred from electronic annotation. Source: InterPro bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 261 | 261 | 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase | PRO_0000054601 | |||||
Regions | |||||||||
| Nucleotide binding | 12 – 36 | 25 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 157 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 144 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 146 | 1 | P → D in AAA16899. Ref.3 | ||||||
| Sequence conflict | 231 – 234 | 4 | IADA → MRC in AAA16899. Ref.3 | ||||||
| Sequence conflict | 247 – 256 | 10 | TMHNLCVDGG → RCIFMRRCAT Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequence and genetic organization of a Bacillus subtilis operon encoding 2,3-dihydroxybenzoate biosynthetic enzymes." Rowland B.M., Grossman T.H., Osburne M.S., Taber H.W. Gene 178:119-123(1996) [PubMed: 8921902] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "Cloning and mapping of the Bacillus subtilis locus homologous to Escherichia coli ent genes." Adams R., Schumann W. Gene 133:119-121(1993) [PubMed: 8224884] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-256. Strain: 168. |
| [4] | Graumann P.L., Schmid R., Marahiel M.A. Submitted (OCT-1997) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-11. Strain: 168 / JH642. |
Cross-references
Sequence databases | |
|---|---|
| U26444 Genomic DNA. Translation: AAC44630.1. Z99120 Genomic DNA. Translation: CAB15190.1. L08644 Genomic DNA. Translation: AAA16899.2. | |
| PIR | A69615. |
| RefSeq | NP_391080.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CYD based on UniProtKB P08074. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 936579. |
| GenomeReviews | Gene locus BSU32000 in contig AL009126_GR. |
| KEGG | bsu:BSU32000. |
| NMPDR | fig|224308.1.peg.3206. |
Organism-specific databases | |
| SubtiList | BG11019. dhbA. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P39071. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU3197-MON. MetaCyc:MON-13913. |
Family and domain databases | |
| InterPro | IPR002198. DHase_sc/Rdtase_SDR. IPR003560. DHB_DHase. IPR016040. NAD(P)-bd. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| PANTHER | PTHR19410. ADH_short_C2. 1 hit. |
| Pfam | PF00106. adh_short. 1 hit. [Graphical view] |
| PRINTS | PR01397. DHBDHDRGNASE. PR00080. SDRFAMILY. |
| PROSITE | PS00061. ADH_SHORT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHBA_BACSU | ||||||||
| Accession | Primary (citable) accession number: P39071 | ||||||||
| 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
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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