B3DYY7 · B3DYY7_METI4
- ProteinMercuric reductase
- GenemerA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids550 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Resistance to Hg2+ in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg0.
Catalytic activity
- Hg + NADP+ + H+ = Hg2+ + NADPH
Cofactor
Note: Binds 1 FAD per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 133 | FAD (UniProtKB | ChEBI) | |||
Binding site | 222-224 | FAD (UniProtKB | ChEBI) | |||
Binding site | 259-266 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 282 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 350 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 391 | FAD (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | mercury (II) reductase (NADP+) activity | |
Molecular Function | mercury ion binding | |
Molecular Function | NADP binding | |
Molecular Function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor | |
Biological Process | detoxification of mercury ion |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMercuric reductase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Verrucomicrobiota > Methylacidiphilae > Methylacidiphilales > Methylacidiphilaceae > Methylacidiphilum (ex Ratnadevi et al. 2023)
Accessions
- Primary accessionB3DYY7
Proteomes
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Disulfide bond | 124↔129 | Redox-active | |||
Keywords
- PTM
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 3-69 | HMA | |||
Sequence similarities
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length550
- Mass (Da)59,222
- Last updated2008-07-22 v1
- MD5 ChecksumCAF5B11C4A613CF0EFBFF94A6F7B8907
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000975 EMBL· GenBank· DDBJ | ACD82509.1 EMBL· GenBank· DDBJ | Genomic DNA |