Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
A [auth H]SCOP2 FamilyMethylamine dehydrogenase H-chain8030467 4002731 SCOP2 (2022-06-29)
A [auth H]SCOP2 SuperfamilyYVTN repeat-like/Quinoprotein amine dehydrogenase8042846 3001671 SCOP2 (2022-06-29)
C [auth J]SCOP2B SuperfamilyYVTN repeat-like/Quinoprotein amine dehydrogenase8042846 3001671 SCOP2B (2022-06-29)
B [auth L]SCOP2B SuperfamilyMethylamine dehydrogenase L chain8041821 3000932 SCOP2B (2022-06-29)
D [auth M]SCOP2B SuperfamilyMethylamine dehydrogenase L chain8041821 3000932 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
A [auth H]PF06433e2bbkH1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF06433ECOD (1.6)
C [auth J]PF06433e2bbkJ1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF06433ECOD (1.6)
B [auth L]PF02975e2bbkL1 A: few secondary structure elementsX: Methylamine dehydrogenase, L chain (From Topology)H: Methylamine dehydrogenase, L chain (From Topology)T: Methylamine dehydrogenase, L chainF: PF02975ECOD (1.6)
D [auth M]PF02975e2bbkM1 A: few secondary structure elementsX: Methylamine dehydrogenase, L chain (From Topology)H: Methylamine dehydrogenase, L chain (From Topology)T: Methylamine dehydrogenase, L chainF: PF02975ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A [auth H],
C [auth J]
PF06433Methylamine dehydrogenase heavy chain (MADH) (Me-amine-dh_H)Methylamine dehydrogenase heavy chain (MADH)- Repeat
B [auth L],
D [auth M]
PF02975Methylamine dehydrogenase, L chain (Me-amine-dh_L)Methylamine dehydrogenase, L chain- Domain

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
B [auth L],
D [auth M]
TRQ Parent Component: TRP

RESIDAA0148

PSI-MOD :  oxidation of tryptophan to L-tryptophyl quinone MOD:00157

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
amine dehydrogenase  M-CSA #13

Methylamine dehydrogenase is a heterotetrameric, periplasmic quinoprotein found in several forms of constitutive and facultative methylotrophic bacteria. The enzyme catalyses the oxidative deamination of primary amines to their corresponding aldehydes with the release of two electrons and two protons. The enzyme is induced when the methylotrophic bacteria are grown on media containing methylamine as the sole carbon, and therefore energy, source.

The electron acceptor, Amicyanin, binds first to MADH to be reduced and then dissociates from MADH to react with cytochrome c-551i or cytochrome aa3 via the same binding site to be regenerated. Electrons can reach the terminal oxidase via different routes, and it cannot be concluded that one specific interaction is preferred.

Defined by 7 residues: PHE:A-48 [auth H-66]ASP:B-26 [auth L-32]TRP:B-51 [auth L-57]ASP:B-70 [auth L-76]TRP:B-102 [auth L-108]TYR:B-113 [auth L-119]THR:B-116 [auth L-122]
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