Home  |  Contact
Annotation rule MF_00464
Send feedback

General rule information [?]

Accession MF_00464
Dates 18-OCT-2001 (Created)
18-NOV-2019 (Last updated, Version 31)
Name AdoMetDC_1
Scope
Bacteria
Archaea
Templates Q57763 (SPEH_METJA); Q9UWY8 (SPEH_SACS2); Q9WZC3 (SPEH_THEMA); O34426 (SPEH_BACSU); O66615 (SPEH_AQUAE): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
SPEH
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
speH

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 Heterotetramer of two alpha and two beta chains arranged as a dimer 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 1 subfamily.

Keywords [?]


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;

Features [?]

From: SPEH_THEMA (Q9WZC3)
Key     From     To       Description   Tag   Condition   FTGroup
CHAIN     Nter     62       S-adenosylmethionine decarboxylase beta chain        
CHAIN     63     Cter       S-adenosylmethionine decarboxylase alpha chain        
ACT_SITE     63     63       Schiff-base intermediate with substrate; via pyruvic acid     S  
ACT_SITE     68     68       Proton acceptor; for processing activity     H  
ACT_SITE     83     83       Proton donor; for catalytic activity     C  
SITE     62     63       Cleavage (non-hydrolytic); by autolysis     E-S  
MOD_RES     63     63       Pyruvic acid (Ser); by autocatalysis     S  

Additional information [?]

Size range 105-160 amino acids
Related rules MF_01298 (ARGDC supersedes the current rule)
Fusion None
Comments Prokaryotic AdoMetDC type 1 subfamily comprises 2 branches, one with S-adenosylmethionine decarboxylase (AdoMetDC) activity (this rule, MF_00464) and the other with arginine decarboxylase (ArgDC) activity (see MF_01298). Crenarchaeota possess 2 paralogs, one protein from each branch associated with each function.