A2XV58 · DCAM_ORYSI
- ProteinS-adenosylmethionine decarboxylase proenzyme
- GeneSAMDC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids398 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
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 active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 18 | |||||
Sequence: E | ||||||
Active site | 21 | |||||
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 | ||||||
Active site | 243 | Proton acceptor; for processing activity | ||||
Sequence: S | ||||||
Active site | 256 | Proton acceptor; for processing activity | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
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
- Short namesAdoMetDC; SAMDC
- Cleaved into 2 chains
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionA2XV58
- Secondary accessions
Proteomes
Genome annotation databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000302051 | 1-77 | S-adenosylmethionine decarboxylase beta chain | |||
Sequence: MGVLSAADPPPVSAIGFEGYEKRLEITFSEAPVFADPDGRGLRALSRAQIDSVLDLARCTIVSELSNKDFDSYVLSE | ||||||
Modified residue | 78 | Pyruvic acid (Ser); by autocatalysis | ||||
Sequence: S | ||||||
Chain | PRO_0000302052 | 78-398 | S-adenosylmethionine decarboxylase alpha chain | |||
Sequence: SSLFIYSDKIVIKTCGTTKLLLTIPRILELAEGLSMPLAAVKYSRGMFIFPSAQPAPHRSFSEEVAVLNRYFGHLKSGGNAYVIGDPAKPGQKWHIYYATQHPEQPMVTLEMCMTGLDKEKASVFFKTSADGHTSCAKEMTKLSGISDIIPEMEICDFDFEPCGYSMNAIHGLAFSTIHVTPEDGFSYASYEVVGFDASTLAYGDLVKRVLRCFGPSEFSVAVTIFGGHGHAGTWAKELNADAYKCNNMVEQELPCGGLLIYQSFDATEDVPVAVGSPKSVLHCFEAENMVNPAPVKEGKLGNLLPWGEDALEENDGVFDE |
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 (By similarity).
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length398
- Mass (Da)43,309
- Last updated2007-09-11 v2
- Checksum1324EDA871B2AF39
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 3 | in Ref. 3; AAX76987 | ||||
Sequence: V → D | ||||||
Sequence conflict | 96 | in Ref. 2; CAB64671 | ||||
Sequence: K → R | ||||||
Sequence conflict | 157 | in Ref. 3; AAX76987 | ||||
Sequence: N → Y | ||||||
Sequence conflict | 235 | in Ref. 3; AAX76987 | ||||
Sequence: F → L | ||||||
Sequence conflict | 294 | in Ref. 3; AAX76987 | ||||
Sequence: S → T | ||||||
Sequence conflict | 394 | in Ref. 3; AAX76987 | ||||
Sequence: G → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF067194 EMBL· GenBank· DDBJ | AAC79990.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ252213 EMBL· GenBank· DDBJ | CAB64671.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY966487 EMBL· GenBank· DDBJ | AAX76987.1 EMBL· GenBank· DDBJ | mRNA | ||
CM000129 EMBL· GenBank· DDBJ | EAY94718.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. |