Methylamine dehydrogenase light chain
Details
- Name
- Methylamine dehydrogenase light chain
- Synonyms
- 1.4.9.1
- MADH
- Methylamine dehydrogenase (amicyanin)
- Gene Name
- mauA
- Organism
- Paracoccus denitrificans
- 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 (amicyanin) activity
- Specific Function
- Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin.
- Pfam Domain Function
- Me-amine-dh_L (PF02975)
- 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 - 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]