CRYSTAL STRUCTURE OF THE QUINOPROTEIN METHYLAMINE DEHYDROGENASE FROM PARACOCCUS DENITRIFICANS AT 1.75 ANGSTROMS
External Resource: Annotation
- Domain Annotation: SCOP/SCOPe Classification
- Domain Annotation: SCOP2 Classification
- Domain Annotation: ECOD Classification
- Domain Annotation: CATH
- Protein Family Annotation
- Gene Ontology: Gene Product Annotation
- InterPro: Protein Family Classification
- Protein Modification Annotation
- Structure Motif: Primary M-CSA Annotation
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Chains | Domain Info | Class | Fold | Superfamily | Family | Domain | Species | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A [auth H] | d2bbkh_ | All beta proteins | 7-bladed beta-propeller | YVTN repeat-like/Quinoprotein amine dehydrogenase | Methylamine dehydrogenase, H-chain | Methylamine dehydrogenase, H-chain | (Paracoccus denitrificans ) [TaxId: 266 ], | SCOPe (2.08) |
C [auth J] | d2bbkj_ | All beta proteins | 7-bladed beta-propeller | YVTN repeat-like/Quinoprotein amine dehydrogenase | Methylamine dehydrogenase, H-chain | Methylamine dehydrogenase, H-chain | (Paracoccus denitrificans ) [TaxId: 266 ], | SCOPe (2.08) |
B [auth L] | d2bbkl_ | Small proteins | Methylamine dehydrogenase, L chain | Methylamine dehydrogenase, L chain | Methylamine dehydrogenase, L chain | Methylamine dehydrogenase | (Paracoccus denitrificans ) [TaxId: 266 ], | SCOPe (2.08) |
D [auth M] | d2bbkm_ | Small proteins | Methylamine dehydrogenase, L chain | Methylamine dehydrogenase, L chain | Methylamine dehydrogenase, L chain | Methylamine dehydrogenase | (Paracoccus denitrificans ) [TaxId: 266 ], | SCOPe (2.08) |
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
A [auth H] | SCOP2 Family | Methylamine dehydrogenase, H-chain | 8030467 | 4002731 | SCOP2 (2022-06-29) |
A [auth H] | SCOP2 Superfamily | YVTN repeat-like/Quinoprotein amine dehydrogenase | 8042846 | 3001671 | SCOP2 (2022-06-29) |
C [auth J] | SCOP2B Superfamily | YVTN repeat-like/Quinoprotein amine dehydrogenase | 8042846 | 3001671 | SCOP2B (2022-06-29) |
B [auth L] | SCOP2B Superfamily | Methylamine dehydrogenase, L chain | 8041821 | 3000932 | SCOP2B (2022-06-29) |
D [auth M] | SCOP2B Superfamily | Methylamine dehydrogenase, L chain | 8041821 | 3000932 | SCOP2B (2022-06-29) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A [auth H] | Me-amine-dh_H | e2bbkH1 | A: beta duplicates or obligate multimers | X: beta-propeller-like | H: beta-propeller | T: 7-bladed | F: Me-amine-dh_H | ECOD (1.6) |
C [auth J] | Me-amine-dh_H | e2bbkJ1 | A: beta duplicates or obligate multimers | X: beta-propeller-like | H: beta-propeller | T: 7-bladed | F: Me-amine-dh_H | ECOD (1.6) |
B [auth L] | Me-amine-dh_L | e2bbkL1 | A: few secondary structure elements | X: Methylamine dehydrogenase, L chain (From Topology) | H: Methylamine dehydrogenase, L chain (From Topology) | T: Methylamine dehydrogenase, L chain | F: Me-amine-dh_L | ECOD (1.6) |
D [auth M] | Me-amine-dh_L | e2bbkM1 | A: few secondary structure elements | X: Methylamine dehydrogenase, L chain (From Topology) | H: Methylamine dehydrogenase, L chain (From Topology) | T: Methylamine dehydrogenase, L chain | F: Me-amine-dh_L | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
A [auth H] | 2.130.10.10 | Mainly Beta | 7 Propeller | Methylamine Dehydrogenase | Chain H | CATH (4.3.0) |
C [auth J] | 2.130.10.10 | Mainly Beta | 7 Propeller | Methylamine Dehydrogenase | Chain H | CATH (4.3.0) |
B [auth L] | 2.60.30.10 | Mainly Beta | Sandwich | Electron Transport Ethylamine Dehydrogenase | Methylamine/Aralkylamine dehydrogenase light chain | CATH (4.3.0) |
D [auth M] | 2.60.30.10 | Mainly Beta | Sandwich | Electron Transport Ethylamine Dehydrogenase | Methylamine/Aralkylamine dehydrogenase light chain | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
A [auth H], C [auth J] | PF06433 | Methylamine dehydrogenase heavy chain (MADH) (Me-amine-dh_H) | Methylamine dehydrogenase heavy chain (MADH) | - | Repeat |
B [auth L], D [auth M] | PF02975 | Methylamine dehydrogenase, L chain (Me-amine-dh_L) | Methylamine dehydrogenase, L chain | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
Chains | Polymer | Molecular Function | Biological Process | Cellular Component |
---|---|---|---|---|
A [auth H], C [auth J] | METHYLAMINE DEHYDROGENASE (HEAVY SUBUNIT) | |||
B [auth L], D [auth M] | METHYLAMINE DEHYDROGENASE (LIGHT SUBUNIT) |
InterPro: Protein Family Classification InterPro Database Homepage
Protein Modification Annotation
Modified Residue(s) | ||
---|---|---|
Chain | Residue(s) | Description |
B [auth L], D [auth M] | TRQ | Parent Component: TRP : AA0148 : oxidation of tryptophan to L-tryptophyl quinone MOD:00157 |
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage
Chains | Enzyme Name | Description | Catalytic 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. | 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] | EC: 1.4.99.3 (PDB Primary Data) EC: 1.4.9.1 (UniProt) |