Structure of L-Amino acid deaminase from Proteus myxofaciens
External Resource: Annotation
| Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
|---|
| A | soxB_like | e5fjmA2 | A: a+b two layers | X: FAD-linked reductases, C-terminal domain-like | H: FAD-linked reductases-C (From Topology) | T: FAD-linked reductases-C | F: soxB_like | ECOD (1.6) |
| A | DAO_1st | e5fjmA1 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: FAD/NAD(P)-binding domain | F: DAO_1st | ECOD (1.6) |
| B | soxB_like | e5fjmB1 | A: a+b two layers | X: FAD-linked reductases, C-terminal domain-like | H: FAD-linked reductases-C (From Topology) | T: FAD-linked reductases-C | F: soxB_like | ECOD (1.6) |
| B | DAO_1st | e5fjmB2 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: FAD/NAD(P)-binding domain | F: DAO_1st | ECOD (1.6) |
| Chains | Accession | Name | Description | Comments | Source |
|---|
| PF01266 | FAD dependent oxidoreductase (DAO) | FAD dependent oxidoreductase | This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1. | Domain |
| Chains | Polymer | Molecular Function | Biological Process | Cellular Component |
|---|
| L-AMINO ACID DEAMINASE | | - | |
