A0A7W9HGB0 · A0A7W9HGB0_9PSEU
- ProteinAdenosylhomocysteinase
- GeneahcY
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids489 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
Catalytic activity
- S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
Cofactor
Note: Binds 1 NAD+ per subunit.
Pathway
Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 66 | substrate | ||||
Sequence: T | ||||||
Binding site | 150 | substrate | ||||
Sequence: D | ||||||
Binding site | 212 | substrate | ||||
Sequence: E | ||||||
Binding site | 242 | substrate | ||||
Sequence: K | ||||||
Binding site | 246 | substrate | ||||
Sequence: D | ||||||
Binding site | 247 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 276-281 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GYGDVG | ||||||
Binding site | 278-283 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GDVGKG | ||||||
Binding site | 299 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 334 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 403 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 410 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | adenosylhomocysteinase activity | |
Biological Process | L-homocysteine biosynthetic process | |
Biological Process | one-carbon metabolic process | |
Biological Process | S-adenosylmethionine cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenosylhomocysteinase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae > Saccharothrix
Accessions
- Primary accessionA0A7W9HGB0
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 247-409 | S-adenosyl-L-homocysteine hydrolase NAD binding | ||||
Sequence: NKYGIRHSLIDGINRATDVMIAGKLAVVCGYGDVGKGAVESLRGQGARVVVTEIDPICALQAAMDGLNVVLLEDVIADGDIFITTTGNRDIIMAEDMAKMKHNAVVGNVGHFDNEIDMAGLAKVPGIERIEIKPQVHEWKFADGHSIIVLSEGRLLNLGNATG |
Sequence similarities
Belongs to the adenosylhomocysteinase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length489
- Mass (Da)52,797
- Last updated2021-06-02 v1
- ChecksumFD8235D3C28DAF86
Keywords
- Technical term