A0A1I2B4F3 · A0A1I2B4F3_9GAMM
- ProteinAdenosylhomocysteinase
- GeneahcY
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids464 (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 | 64 | substrate | ||||
Sequence: T | ||||||
Binding site | 140 | substrate | ||||
Sequence: D | ||||||
Binding site | 165 | substrate | ||||
Sequence: E | ||||||
Binding site | 166-168 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TTT | ||||||
Binding site | 195 | substrate | ||||
Sequence: K | ||||||
Binding site | 199 | substrate | ||||
Sequence: D | ||||||
Binding site | 200 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 229-234 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GYGDVG | ||||||
Binding site | 231-236 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GDVGKG | ||||||
Binding site | 252 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 301 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 322-324 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: IGH | ||||||
Binding site | 370 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 377 | 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 > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Marinobacteraceae > Marinobacter
Accessions
- Primary accessionA0A1I2B4F3
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 200-376 | S-adenosyl-L-homocysteine hydrolase NAD binding | ||||
Sequence: NKYGCRHSLNDAIKRATDHLMAGKKALVIGYGDVGKGSAASLRQEGMIVKVTEADPICAMQACMDGFEVVSPYIDGVNTGTESAVNRDLLQNTDLLVTTTGNMNVCDAHMLKALKSGAVVCNIGHFDNEIDTAYMRKNWEWDEVKPQVHVVYRDKATNDHLILLSEGRLVNLGNATG |
Sequence similarities
Belongs to the adenosylhomocysteinase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length464
- Mass (Da)51,172
- Last updated2017-11-22 v1
- Checksum1CA6ABA513EF8EA2