Methylamine dehydrogenase light chain
Details
- Name
- Methylamine dehydrogenase light chain
- Kind
- protein
- Synonyms
- 1.4.9.1
- MADH
- Methylamine dehydrogenase (amicyanin)
- Gene Name
- mauA
- UniProtKB Entry
- P22619Swiss-Prot
- Organism
- Paracoccus denitrificans
- NCBI Taxonomy ID
- 266
- Amino acid sequence
>lcl|BSEQ0013036|Methylamine dehydrogenase light chain MLGNFRFDDMVEKLSRRVAGQTSRRSVIGKLGTAMLGIGLVPLLPVDRRGRVSRANAADA PAGTDPRAKWVPQDNDIQACDYWRHCSIDGNICDCSGGSLTNCPPGTKLATASWVASCYN PTDGQSYLIAYRDCCGYNVSGRCPCLNTEGELPVYRPEFANDIIWCFGAEDDAMTYHCTI SPIVGKAS
- Number of residues
- 188
- Molecular Weight
- 20392.855
- Theoretical pI
- 6.45
- GO Classification
- Functionsamine dehydrogenase activity / methylamine dehydrogenase (amicyanin) activityProcessesamine metabolic processComponentsouter membrane-bounded periplasmic space
- General Function
- Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin.
- Specific Function
- amine dehydrogenase activity
- Pfam Domain Function
- Me-amine-dh_L (PF02975)
- Signal Regions
- 1-57
- Transmembrane Regions
- Not Available
- Cellular Location
- Periplasm
- Gene sequence
>lcl|BSEQ0008270|72 bp CTCGAGGCCGATAGGACCGGCTTCGCCTCGTTGCAGCAATACATGGCCAGCCGGAAGAAA CAGGCGGCCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P22619 UniProtKB Entry Name DHML_PARDE GenBank Protein ID 150581 GenBank Gene ID M90098 PDB ID(s) 1MG2, 1MG3, 2BBK, 2GC4, 2GC7, 2J55, 2J56, 2J57, 2MTA, 3ORV, 3PXS, 3PXT, 3PXW, 3RLM, 3RMZ, 3RN0, 3SLE, 4FA1, 4FA4, 4FA5, 4FA9, 4FAN, 4FAV, 4FB1, 4K3I, 4Y5R - General References
- Chistoserdov AY, Boyd J, Mathews FS, Lidstrom ME: The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans. Biochem Biophys Res Commun. 1992 May 15;184(3):1181-9. [Article]
- van Spanning RJ, Wansell CW, Reijnders WN, Oltmann LF, Stouthamer AH: Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation. FEBS Lett. 1990 Nov 26;275(1-2):217-20. [Article]
- Chen L, Mathews FS, Davidson VL, Huizinga EG, Vellieux FM, Hol WG: Three-dimensional structure of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans determined by molecular replacement at 2.8 A resolution. Proteins. 1992 Oct;14(2):288-99. [Article]
- Chen L, Durley R, Poliks BJ, Hamada K, Chen Z, Mathews FS, Davidson VL, Satow Y, Huizinga E, Vellieux FM, et al.: Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin. Biochemistry. 1992 Jun 2;31(21):4959-64. [Article]
- Chen L, Durley RC, Mathews FS, Davidson VL: Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i. Science. 1994 Apr 1;264(5155):86-90. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details TRW3-(2-AMINO-3-HYDROXY-PROPYL)-6-(N'-CYCLOHEXYL-HYDRAZINO)OCTAHYDRO-INDOL-7-OL experimental unknown target Details