P45513 (DHAT_CITFR) Reviewed, UniProtKB/Swiss-Prot
Last modified
June 28, 2011.
Version 44.
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: 1,3-propanediol dehydrogenase EC=1.1.1.202 Alternative name(s): 1,3-propanediol oxidoreductase 3-hydroxypropionaldehyde reductase | ||
| Gene names |
| ||
| Organism | Citrobacter freundii | ||
| Taxonomic identifier | 546 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Citrobacter |
Protein attributes
| Sequence length | 387 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Most active with substrates containing two primary alcohol groups separated by one or two carbon atoms. In the physiological direction, 3-hydroxypropionaldehyde is the preferred substrate. |
| Catalytic activity | Propane-1,3-diol + NAD+ = 3-hydroxypropanal + NADH. |
| Cofactor | Iron. |
| Subunit structure | Homooctamer. |
| Sequence similarities | Belongs to the iron-containing alcohol dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Iron NAD |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Molecular function | 1,3-propanediol dehydrogenase activity Inferred from electronic annotation. Source: EC metal ion 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 – 387 | 387 | 1,3-propanediol dehydrogenase | PRO_0000087841 | |||
Sequences
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References
| [1] | "Purification of 1,3-propanediol dehydrogenase from Citrobacter freundii and cloning, sequencing, and overexpression of the corresponding gene in Escherichia coli." Daniel R., Boenigk R., Gottschalk G. J. Bacteriol. 177:2151-2156(1995) [PubMed: 7721705] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U09771 Genomic DNA. Translation: AAB48848.1. |
| PIR | A56275. |
3D structure databases | |
| ProteinModelPortal | P45513. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR001670. ADH_Fe. IPR018211. ADH_Fe_CS. [Graphical view] |
| Pfam | PF00465. Fe-ADH. 1 hit. [Graphical view] |
| PROSITE | PS00913. ADH_IRON_1. 1 hit. PS00060. ADH_IRON_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHAT_CITFR | ||||||||
| Accession | Primary (citable) accession number: P45513 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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