Q59543 (DHML_METME) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 69.
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: Methylamine dehydrogenase light chain Short name=MADH EC=1.4.9.1 Alternative name(s): Methylamine dehydrogenase (amicyanin) | ||
| Gene names |
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| Organism | Methylophilus methylotrophus (Bacterium W3A1) | ||
| Taxonomic identifier | 17 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Methylophilales › Methylophilaceae › Methylophilus![]() |
Protein attributes
| Sequence length | 187 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin. |
| Catalytic activity | Methylamine + H2O + amicyanin = formaldehyde + ammonia + reduced amicyanin. |
| Cofactor | Contains 1 tryptophan tryptophylquinone per subunit By similarity. |
| Pathway | One-carbon metabolism; methylamine degradation; formaldehyde from methylamine: step 1/1. |
| Subunit structure | Heterotetramer of two light and two heavy chains. |
| Subcellular location | |
| Post-translational modification | Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. Tryptophan tryptophylquinone (TTQ) is formed by oxidation of the indole ring of a tryptophan to form tryptophylquinone followed by covalent cross-linking with another tryptophan residue. |
| Sequence similarities | Belongs to the aromatic amine dehydrogenase light chain family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Transport |
| Cellular component | Periplasm |
| Domain | Signal |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond TTQ |
| Gene Ontology (GO) | |
| Biological_process | amine metabolic process Inferred from electronic annotation. Source: InterPro electron transport chainInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro |
| Molecular_function | amine dehydrogenase activity Inferred from electronic annotation. Source: InterPro methylamine dehydrogenase (amicyanin) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 57 | 57 | Tat-type signal Potential | ||||||||
| Chain | 58 – 187 | 130 | Methylamine dehydrogenase light chain | PRO_0000025574 | |||||||
Amino acid modifications | |||||||||||
| Modified residue | 113 | 1 | Tryptophylquinone By similarity | ||||||||
| Disulfide bond | 79 ↔ 144 | By similarity | |||||||||
| Disulfide bond | 85 ↔ 117 | By similarity | |||||||||
| Disulfide bond | 92 ↔ 177 | By similarity | |||||||||
| Disulfide bond | 94 ↔ 142 | By similarity | |||||||||
| Disulfide bond | 102 ↔ 133 | By similarity | |||||||||
| Disulfide bond | 134 ↔ 165 | By similarity | |||||||||
| Cross-link | 113 ↔ 164 | Tryptophan tryptophylquinone (Trp-Trp) By similarity | |||||||||
Sequences
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References
| [1] | "Organization of the methylamine utilization (mau) genes in Methylophilus methylotrophus W3A1-NS." Chistoserdov A.Y., McIntire W.S., Mathews F.S., Lidstrom M.E. J. Bacteriol. 176:4073-4080(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L26407 Genomic DNA. Translation: AAB46951.1. |
| PIR | T10073. |
3D structure databases | |
| ProteinModelPortal | Q59543. |
| SMR | Q59543. Positions 66-186. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-3908. |
| UniPathway | UPA00895; UER00870. |
Family and domain databases | |
| Gene3D | 2.60.30.10. 1 hit. |
| InterPro | IPR016008. Amine_DH_Ltc. IPR013504. MADH/AADH_Ltc_C_dom. IPR004229. MeN_DH_Ltc. [Graphical view] |
| Pfam | PF02975. Me-amine-dh_L. 1 hit. [Graphical view] |
| PIRSF | PIRSF000192. Amine_dh_beta. 1 hit. |
| SUPFAM | SSF57561. MADH_Lt_C. 1 hit. |
| TIGRFAMs | TIGR02659. TTQ_MADH_Lt. 1 hit. |
| PROSITE | PS51318. TAT. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHML_METME | ||||||||
| Accession | Primary (citable) accession number: Q59543 | ||||||||
| 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 |

Clusters with
