D6C5C0 · D6C5C0_9POAL
- ProteinS-adenosylmethionine decarboxylase proenzyme
- GeneSAMDC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids397 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
Catalytic activity
- S-adenosyl-L-methionine + H+ = S-adenosyl 3-(methylsulfanyl)propylamine + CO2
Cofactor
Note: Binds 1 pyruvoyl group covalently per subunit.
Pathway
Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 17 | substrate | ||||
Sequence: F | ||||||
Binding site | 77 | substrate | ||||
Sequence: E | ||||||
Site | 77-78 | Cleavage (non-hydrolytic); by autolysis | ||||
Sequence: ES | ||||||
Active site | 78 | Schiff-base intermediate with substrate; via pyruvic acid | ||||
Sequence: S | ||||||
Active site | 92 | Proton donor; for catalytic activity | ||||
Sequence: C | ||||||
Binding site | 237 | substrate | ||||
Sequence: F | ||||||
Active site | 243 | Proton acceptor; for processing activity | ||||
Sequence: S | ||||||
Active site | 256 | Proton acceptor; for processing activity | ||||
Sequence: H | ||||||
Binding site | 260 | substrate | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | adenosylmethionine decarboxylase activity | |
Biological Process | spermidine biosynthetic process | |
Biological Process | spermine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameS-adenosylmethionine decarboxylase proenzyme
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Chloridoideae > Cynodonteae > Orininae > Cleistogenes
Accessions
- Primary accessionD6C5C0
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5042325133 | 1-77 | S-adenosylmethionine decarboxylase beta chain | |||
Sequence: MAVMRAGDVPPVSAIGFEGYEKRLEISFSEAPIFADPNGRGLRALSRAQIDSVLDLARCTIVSELSNEAFDSYVLSE | ||||||
Modified residue | 78 | Pyruvic acid (Ser); by autocatalysis | ||||
Sequence: S | ||||||
Chain | PRO_5042325134 | 78-397 | S-adenosylmethionine decarboxylase alpha chain | |||
Sequence: SSLFVYPYRVVIKTCGTTKLLLAIPRILELAEELSLPLAAVKYSRGTFIFPDAQPSPHKNFADEVAFLNRYFGGLKSGGNAYVIGDPAKPGQKWHIYYATEYPEKPVVTLEMCMTGLDKKKASVFFKTSANGHISCAKEMTKLSGISDIIPEMEICDFDFEPCGYSMNAIHGPAFSTIHVTPEDGFSYASYEVMGFNPASLAYGDLVKRVLKCFSPSEFSVAVTIFGERDNAKTWGKKLDVESYACGNMVEEELPSGGLLVYQSFTATGEVAVGSPRSVIHSFSDDDVENESMNASSDALLCWEADAVKTEGREAKKMKY |
Keywords
- PTM
Structure
Sequence
- Sequence statusComplete
- Length397
- Mass (Da)43,457
- Last updated2010-07-13 v1
- ChecksumB5D6847D458C113D