Reviewed,
UniProtKB/Swiss-Prot P00372 (DHML_METEX)
Last modified
June 16, 2009.
Version 70.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Methylamine dehydrogenase light chain Short name=MADH EC=1.4.99.3 | ||
| Gene names |
| ||
| Organism | Methylobacterium extorquens (Protomonas extorquens) | ||
| Taxonomic identifier | 408 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Methylobacteriaceae › Methylobacterium |
Protein attributes
| Sequence length | 186 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
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. Ref.6 |
| 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 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 | Direct protein sequencing |
| 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 Ref.4 | ||||||||
| Chain | 58 – 186 | 129 | Methylamine dehydrogenase light chain | PRO_0000025572 | |||||||
Amino acid modifications | |||||||||||
| Modified residue | 112 | 1 | Tryptophylquinone | ||||||||
| 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) | |||||||||
Natural variations | |||||||||||
| Natural variant | 106 | 1 | K → L | ||||||||
Experimental info | |||||||||||
| Sequence conflict | 74 | 1 | D → N AA sequence Ref.4 | ||||||||
Sequences
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References
| [1] | "Genetic organization of methylamine utilization genes from Methylobacterium extorquens AM1." Chistoserdov A.Y., Tsygankov Y.D., Lidstrom M.E. J. Bacteriol. 173:5901-5908(1991) [PubMed: 1653226] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AM1 / NCIMB 9133. |
| [2] | "Genetic organization of the mau gene cluster in Methylobacterium extorquens AM1: complete nucleotide sequence and generation and characteristics of mau mutants." Chistoserdov A.Y., Chistoserdova L.V., McIntire W.S., Lidstrom M.E. J. Bacteriol. 176:4052-4065(1994) [PubMed: 8021187] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AM1 / NCIMB 9133. |
| [3] | "Cloning and sequencing of the structural gene for the small subunit of methylamine dehydrogenase from Methylobacterium extorquens AM1: evidence for two tryptophan residues involved in the active center." Chistoserdov A.Y., Tsygankov Y.D., Lidstrom M.E. Biochem. Biophys. Res. Commun. 172:211-216(1990) [PubMed: 2121141] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-186. Strain: AM1 / NCIMB 9133. |
| [4] | "Amino acid sequence studies of the light subunit of methylamine dehydrogenase from Pseudomonas AM1: existence of two residues binding the prosthetic group." Ishii Y., Hase T., Fukumori Y., Matsubara H., Tobari J. J. Biochem. 93:107-119(1983) [PubMed: 6841324] [Abstract] Cited for: PROTEIN SEQUENCE OF 58-186. Strain: AM1 / NCIMB 9133. |
| [5] | "The small-subunit polypeptide of methylamine dehydrogenase from Methylobacterium extorquens AM1 has an unusual leader sequence." Chistoserdov A.Y., Lidstrom M.E. J. Bacteriol. 173:5909-5913(1991) [PubMed: 1885555] [Abstract] Cited for: PRESENCE OF UNUSUAL LEADER SEQUENCE. Strain: AM1 / NCIMB 9133. |
| [6] | "A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase." McIntire W.S., Wemmer D.E., Chistoserdov A.Y., Lidstrom M.E. Science 252:817-824(1991) [PubMed: 2028257] [Abstract] Cited for: CHARACTERIZATION OF COFACTOR. |
Cross-references
Sequence databases | |
|---|---|
| M57963 Genomic DNA. Translation: AAA68894.1. L26406 Genomic DNA. Translation: AAB46936.1. M58517 Genomic DNA. Translation: AAA25379.1. | |
| PIR | DEPSNL. A36676. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2BBK based on UniProtKB P22619. |
| SMR | P00372. Positions 63-186. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MON-3906. |
| BRENDA | 1.4.99.3. 20440. |
Family and domain databases | |
| InterPro | IPR016008. Amine_DH_bsu. IPR004229. MeN_DH_Ltc. IPR013504. MeN_DH_Ltc_C. IPR006311. Tat. IPR017909. Twin_arg_translocation_Tat. [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 | TIGR01409. TAT_signal_seq. 1 hit. TIGR02659. TTQ_MADH_Lt. 1 hit. |
| PROSITE | PS51318. TAT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHML_METEX | ||||||||
| Accession | Primary (citable) accession number: P00372 Secondary accession number(s): Q60146 | ||||||||
| 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
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


