A0A2R6PB27 · A0A2R6PB27_ACTCC
- ProteinS-adenosylmethionine decarboxylase proenzyme
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids358 (go to sequence)
- Protein existenceInferred from homology
- 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 | 10 | substrate | ||||
Sequence: F | ||||||
Binding site | 70 | substrate | ||||
Sequence: E | ||||||
Site | 70-71 | Cleavage (non-hydrolytic); by autolysis | ||||
Sequence: ES | ||||||
Active site | 71 | Schiff-base intermediate with substrate; via pyruvic acid | ||||
Sequence: S | ||||||
Active site | 85 | Proton donor; for catalytic activity | ||||
Sequence: C | ||||||
Binding site | 228 | substrate | ||||
Sequence: F | ||||||
Active site | 234 | Proton acceptor; for processing activity | ||||
Sequence: S | ||||||
Active site | 247 | Proton acceptor; for processing activity | ||||
Sequence: H | ||||||
Binding site | 251 | 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
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > Ericales > Actinidiaceae > Actinidia
Accessions
- Primary accessionA0A2R6PB27
Proteomes
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5042323177 | 1-70 | S-adenosylmethionine decarboxylase beta chain | |||
Sequence: MALAVSAIGFEGYEKRLEISFFEPTIFADPKGRGLRSLSKAQLDEFLGPAECTIVSSLSNDHVDSYVLSE | ||||||
Modified residue | 71 | Pyruvic acid (Ser); by autocatalysis | ||||
Sequence: S | ||||||
Chain | PRO_5042323178 | 71-358 | S-adenosylmethionine decarboxylase alpha chain | |||
Sequence: SSLFVYSYKIIIKTCGTTKLLLAIPPILKLADTLFLTVRSVRYTRGSFIFPAAQSYPHRNFSEEVEVLDSYFGKLGSGGNAFVMGSFNKLQKWHVYSASAESVCSGNPVYTLEMCMTGLDKEMASVFYINQSGSAAVMTCTSGIRKILPESKICDFDFEPCGYSMNAIEGAAISTIHITPEDGFSYASFEAVGYDPKLVDLDLLVERVLACFNPSEFSISVHADVSSKLLEHTCSLGVKGFCLGDSSYEELGTTGGSMVYQKFVKTVGCGSPRSILNSCWKDEDGEME |
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length358
- Mass (Da)39,072
- Last updated2018-06-20 v1
- Checksum8017297971C30F63
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
NKQK01000027 EMBL· GenBank· DDBJ | PSR88222.1 EMBL· GenBank· DDBJ | Genomic DNA |