Reviewed,
UniProtKB/Swiss-Prot Q48303 (DHDM_HYPSX)
Last modified
December 16, 2008.
Version 56.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Dimethylamine dehydrogenase Short name=DMADh EC=1.5.8.1 | ||
| Gene names |
| ||
| Organism | Hyphomicrobium sp. (strain x) | ||
| Taxonomic identifier | 79673 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Hyphomicrobiaceae › Hyphomicrobium |
Protein attributes
| Sequence length | 736 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Dimethylamine + H(2)O + electron-transferring flavoprotein = methylamine + formaldehyde + reduced electron-transferring flavoprotein. |
| Cofactor | Binds 1 FMN covalently per subunit By similarity. Binds 1 4Fe-4S cluster per subunit By similarity. |
| Sequence similarities | In the N-terminal section; belongs to the NADH:flavin oxidoreductase/NADH oxidase family. |
Ontologies
Keywords | |
|---|---|
| Ligand | 4Fe-4S FMN Flavoprotein Iron Iron-sulfur Metal-binding |
| Molecular function | Oxidoreductase |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FMN bindingInferred from electronic annotation. Source: InterPro dimethylamine dehydrogenase activityInferred from electronic annotation. Source: EC iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 736 | 735 | Dimethylamine dehydrogenase | PRO_0000194471 | |||||
Regions | |||||||||
| Nucleotide binding | 398 – 427 | 30 | ADP By similarity | ||||||
| Region | 176 – 179 | 4 | Substrate-binding By similarity | ||||||
Sites | |||||||||
| Active site | 181 | 1 | Proton donor By similarity | ||||||
| Metal binding | 352 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 355 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 358 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 371 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Binding site | 229 | 1 | FMN By similarity | ||||||
| Binding site | 329 | 1 | FMN By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 31 | 1 | S-6-FMN cysteine By similarity | ||||||
Sequences
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References
| [1] | "The primary structure of Hyphomicrobium X dimethylamine dehydrogenase. Relationship to trimethylamine dehydrogenase and implications for substrate recognition." Yang C.C., Packman L.C., Scrutton N.S. Eur. J. Biochem. 232:264-271(1995) [PubMed: 7556160] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| X89575 Genomic DNA. Translation: CAA61752.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1O94 based on UniProtKB P16099. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR013785. Aldolase_TIM. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR001155. OxRdtase_FMN_N. IPR001100. Pyr_nuc-diS_OxRdtase. [Graphical view] |
| Gene3D | G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. |
| Pfam | PF00724. Oxidored_FMN. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. PR00411. PNDRDTASEI. |
| ProtoNet | Search... |
Entry information
| Entry name | DHDM_HYPSX | ||||||||
| Accession | Primary (citable) accession number: Q48303 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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