Methylamine dehydrogenase heavy chain

Details

Name
Methylamine dehydrogenase heavy chain
Synonyms
  • 1.4.9.1
  • MADH
  • Methylamine dehydrogenase (amicyanin)
Gene Name
mauB
Organism
Paracoccus denitrificans
Amino acid sequence
>lcl|BSEQ0013035|Methylamine dehydrogenase heavy chain
MALPPNFMPLFRASLIGLGLGCSALALAASAQDAPEAETQAQETQGQAAARAAAADLAAG
QDDEPRILEAPAPDARRVYVNDPAHFAAVTQQFVIDGEAGRVIGMIDGGFLPNPVVADDG
SFIAHASTVFSRIARGERTDYVEVFDPVTLLPTADIELPDAPRFLVGTYPWMTSLTPDGK
TLLFYQFSPAPAVGVVDLEGKAFKRMLDVPDCYHIFPTAPDTFFMHCRDGSLAKVAFGTE
GTPEITHTEVFHPEDEFLINHPAYSQKAGRLVWPTYTGKIHQIDLSSGDAKFLPAVEALT
EAERADGWRPGGWQQVAYHRALDRIYLLVDQRDEWRHKTASRLLVVLDAKTGERLAKFEM
GHEIDSINVSQDEKPLLYALSTGDKTLYIHDAESGEELRSVNQLGHGPQVITTADMG
Number of residues
417
Molecular Weight
45439.73
Theoretical pI
4.58
GO Classification
Functions
amine dehydrogenase activity / methylamine dehydrogenase (amicyanin) activity
Processes
methylamine metabolic process
Components
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
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0008268|450 bp
GCCGGCTTTTCCGGTTTCGGCAGCACGGCCCTGCTGGTGCTGGGGCTGGTCGGCCTGGCT
TACGGTGCGCATCAGCTTGACTTCCTGCGCGTGCCCTATCCGCAGCGCCGGGCGCAGGTG
CCGCATGACGCACGCCAGCGTTTCCCGAAATGGGTCATCGGCGGGCTTTACGGGCTGTCG
CTGGGGCTCGATTACCTGACCTATGTGCAGACGCCGCTGCTTTACATGATGACGCTGGCG
GCGGTCTTTACCGGCAATATCGCCCATGCCATCGCCATTGTCGCGCTGTTCAACCTGGGC
CGGTTCCTGCCGGTCGCGGTCAACGCGCTGCCGATCCCCGATTACCGGGTGCAGGCATGG
CTGGCCCGGCACCAGGAAAACGCCGCGCTGGCCGACGGCGCCATCCTGACCGCGCTTGGC
GCGGGCTTCACGGTGCTGGCGCTGATCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP29894
UniProtKB Entry NameDHMH_PARDE
GenBank Protein ID150584
GenBank Gene IDM90099
General References
  1. 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]
  2. Van Spanning RJ, van der Palen CJ, Slotboom DJ, Reijnders WN, Stouthamer AH, Duine JA: Expression of the mau genes involved in methylamine metabolism in Paracoccus denitrificans is under control of a LysR-type transcriptional activator. Eur J Biochem. 1994 Nov 15;226(1):201-10. [Article]
  3. 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]
  4. 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]
  5. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB08646TRW3-(2-AMINO-3-HYDROXY-PROPYL)-6-(N'-CYCLOHEXYL-HYDRAZINO)OCTAHYDRO-INDOL-7-OLexperimentalunknownDetails