Reviewed,
UniProtKB/Swiss-Prot Q50425 (DHML_METFK)
Last modified
June 16, 2009.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Methylamine dehydrogenase light chain Short name=MADH EC=1.4.99.3 | ||||
| Gene names |
| ||||
| Organism | Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 265072 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Methylophilales › Methylophilaceae › Methylobacillus |
Protein attributes
| Sequence length | 186 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 | RCH2NH2 + H2O + acceptor = RCHO + NH3 + reduced acceptor. |
| 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 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cellular amine metabolic process Inferred from electronic annotation. Source: InterPro electron transport chainInferred from electronic annotation. Source: UniProtKB-KW transportInferred 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: 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 – 186 | 129 | Methylamine dehydrogenase light chain | PRO_0000025573 | |||||||
Amino acid modifications | |||||||||||
| Modified residue | 112 | 1 | Tryptophylquinone By similarity | ||||||||
| Disulfide bond | 78 ↔ 143 | By similarity | |||||||||
| Disulfide bond | 84 ↔ 116 | By similarity | |||||||||
| Disulfide bond | 91 ↔ 176 | By similarity | |||||||||
| Disulfide bond | 93 ↔ 141 | By similarity | |||||||||
| Disulfide bond | 101 ↔ 132 | By similarity | |||||||||
| Disulfide bond | 133 ↔ 164 | By similarity | |||||||||
| Cross-link | 112 ↔ 163 | Tryptophan tryptophylquinone (Trp-Trp) By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Cloning, sequencing, and mutation of a gene for azurin in Methylobacillus flagellatum KT." Gak E.R., Chistoserdov A.Y., Lidstrom M.E. J. Bacteriol. 177:4575-4578(1995) [PubMed: 7635847] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Complete sequence of Methylobacillus flagellatus KT." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. Richardson P.Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| L37427 Genomic DNA. Translation: AAC41474.1. CP000284 Genomic DNA. Translation: ABE48821.1. | |
| RefSeq | YP_544662.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2BBK based on UniProtKB P22619. |
| SMR | Q50425. Positions 65-186. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 4000890. |
| GenomeReviews | Gene locus Mfla_0551 in contig CP000284_GR. |
| KEGG | mfa:Mfla_0551. |
| NMPDR | fig|265072.7.peg.549. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q50425. |
| OMA | Q50425. LFDSWFE. |
Enzyme and pathway databases | |
| BioCyc | MFLA265072:MFLA_0551-MON. |
Family and domain databases | |
| InterPro | IPR016008. Amine_DH_bsu. IPR004229. MeN_DH_Ltc. IPR013504. MeN_DH_Ltc_C. [Graphical view] |
| Gene3D | G3DSA:2.60.30.10. MADH_Lt_C. 1 hit. |
| Pfam | PF02975. Me-amine-dh_L. 1 hit. [Graphical view] |
| PIRSF | PIRSF000192. Amine_dh_beta. 1 hit. |
| TIGRFAMs | TIGR02659. TTQ_MADH_Lt. 1 hit. |
| PROSITE | PS51318. TAT. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHML_METFK | ||||||||
| Accession | Primary (citable) accession number: Q50425 Secondary accession number(s): Q1H3W6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


