A0A4Q5DSN5 · A0A4Q5DSN5_9BACE
- ProteinS-adenosylmethionine decarboxylase proenzyme
- GenespeD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids555 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
Catalytic activity
- H+ + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
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 site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 457-458 | Cleavage (non-hydrolytic); by autolysis | ||||
Sequence: ES | ||||||
Active site | 458 | Schiff-base intermediate with substrate; via pyruvic acid | ||||
Sequence: S | ||||||
Active site | 463 | Proton acceptor; for processing activity | ||||
Sequence: H | ||||||
Active site | 478 | Proton donor; for catalytic activity | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | adenosylmethionine decarboxylase activity | |
Biological Process | spermidine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameS-adenosylmethionine decarboxylase proenzyme
- EC number
- Short namesAdoMetDC ; SAMDC
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Bacteroides
Accessions
- Primary accessionA0A4Q5DSN5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5026417213 | 1-457 | S-adenosylmethionine decarboxylase beta chain | |||
Sequence: MDYINKIFKTVSIKDNRRIIELYFQELYCCAPLSNKTLSQKLLLPVPIVTAIKNEGIKLGIFEQCGRGVGLTHNGKDYVEQALGFKGIDLCLYRRLAESEQARDAYADALSKKYRAAFDERPVADVALDQAQCTVQTAFRRALLCLANGTLTSRQIVCMGDDDFVSLAIGFLLKELYPGPSICPTHIHVLEMDGRYIECLNRLSERFSLPISCEQVDLRMPLPPHLCGRFDCLFTDPPYTQEGASLFLSRAISVLKEESGLRIFFSFGNKSATEVYFLQKCFQLHGLAIKDMFTRFNEYMGASLLGNKGQLFVLETTERTRALFPLEKRGRDDIYTADRNFRQNRYRCRQCSKVYAVGKEAEYQTIRELKKQGCSVCGATVFDRLHKNGNTDKKQYLPLGHHILADFYNCDPEKLDDVEQIRTFMHEAAVSAGATIVQENFHKYAPIGVSGVVVIQE | ||||||
Modified residue | 458 | Pyruvic acid (Ser); by autocatalysis | ||||
Sequence: S | ||||||
Chain | PRO_5026417212 | 458-555 | S-adenosylmethionine decarboxylase alpha chain | |||
Sequence: SHLTIHTWPECGYAAVDLFTCGTNVRPWTAFDYLQERLGCAKVEYSDLMRGAYERPSLLRYSETEQPAMRRKKRQRYDASSKWNRRAKSLTDCSVLSK |
Post-translational modification
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Keywords
- PTM
Interaction
Subunit
Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 111-303 | N4-bis(aminopropyl)spermidine synthase C-terminal | ||||
Sequence: SKKYRAAFDERPVADVALDQAQCTVQTAFRRALLCLANGTLTSRQIVCMGDDDFVSLAIGFLLKELYPGPSICPTHIHVLEMDGRYIECLNRLSERFSLPISCEQVDLRMPLPPHLCGRFDCLFTDPPYTQEGASLFLSRAISVLKEESGLRIFFSFGNKSATEVYFLQKCFQLHGLAIKDMFTRFNEYMGAS | ||||||
Region | 521-555 | Disordered | ||||
Sequence: TEQPAMRRKKRQRYDASSKWNRRAKSLTDCSVLSK | ||||||
Compositional bias | 522-542 | Basic and acidic residues | ||||
Sequence: EQPAMRRKKRQRYDASSKWNR |
Sequence similarities
Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length555
- Mass (Da)63,237
- Last updated2019-07-31 v1
- Checksum02D91954CEF690FD
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 522-542 | Basic and acidic residues | ||||
Sequence: EQPAMRRKKRQRYDASSKWNR |