Home  |  Contact
Annotation rule MF_00465
Send feedback

General rule information [?]

Accession MF_00465
Dates 18-OCT-2001 (Created)
18-NOV-2019 (Last updated, Version 29)
Name AdoMetDC_2
Scope
Bacteria; Firmicutes
Bacteria; Gammaproteobacteria
Template P0A7F6 (SPED_ECOLI)
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
SPED
Protein name
RecName: Full=S-adenosylmethionine decarboxylase proenzyme;
Short=AdoMetDC;
Short=SAMDC;
EC 4.1.1.50;
Contains:
RecName: Full=S-adenosylmethionine decarboxylase beta chain;
Contains:
RecName: Full=S-adenosylmethionine decarboxylase alpha chain;
Flags: Precursor;
Gene name
speD

Comments [?]

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 RHEA:15981: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
EC 4.1.1.50
Cofactor pyruvate
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.
Subunit Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.
Ptm 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.
Similarity Belongs to the prokaryotic AdoMetDC family. Type 2 subfamily.

Keywords [?]

Autocatalytic cleavage
Decarboxylase
Lyase
Polyamine biosynthesis
Pyruvate
S-adenosyl-L-methionine
Schiff base
Spermidine biosynthesis
Zymogen

Gene Ontology [?]

GO:0004014; Molecular function: adenosylmethionine decarboxylase activity.
GO:0006557; Biological process: S-adenosylmethioninamine biosynthetic process.
GO:0006596; Biological process: polyamine biosynthetic process.
GO:0008295; Biological process: spermidine biosynthetic process.

Cross-references [?]

Pfam PF02675; AdoMet_dc; 1;
TIGRFAMs TIGR03331; SAM_DCase_Eco; 1;

Features [?]

From: SPED_ECOLI (P0A7F6)
Key     From     To       Description   Tag   Condition   FTGroup
CHAIN     Nter     111       S-adenosylmethionine decarboxylase beta chain        
CHAIN     112     Cter       S-adenosylmethionine decarboxylase alpha chain        
ACT_SITE     112     112       Schiff-base intermediate with substrate; via pyruvic acid     S  
ACT_SITE     117     117       Proton acceptor; for processing activity     H  
ACT_SITE     140     140       Proton donor; for catalytic activity     C  
SITE     111     112       Cleavage (non-hydrolytic); by autolysis     K-S  
MOD_RES     112     112       Pyruvic acid (Ser); by autocatalysis     S  

Additional information [?]

Size range 263-290 amino acids
Related rules None
Fusion None
Comments The E.coli protein requires metal cation for activity, and an allosteric mechanism of cation activation has been suggested (PubMed=17567041). This may be the case for all the proteins from the prokaryotic AdoMetDC type 2 subfamily (this rule, MF_00465), but this is not the case for the prokaryotic AdoMetDC type 1 subfamily members (MF_00464).


View rule in raw text format (no links)