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HAMAP rule MF_00465

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General rule information [?]

Accession MF_00465
Dates 18-OCT-2001 (Created)
1-JUN-2023 (Last updated, Version 32)
Name AdoMetDC_2
Scope(s) Bacteria
Template(s) P0A7F6 (SPED_ECOLI); [ Recover all ]
Triggered by HAMAP; MF_00465 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier SPED
Protein name RecName: Full=S-adenosylmethionine decarboxylase proenzyme;
RecName: Full=S-adenosylmethionine decarboxylase beta chain;
RecName: Full=S-adenosylmethionine decarboxylase alpha chain;
                 Flags: Precursor;
Gene name Name=speD;

Comments [?]

FUNCTIONCatalyzes 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 Reaction=H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3- (methylsulfanyl)propylamine; Xref=Rhea:RHEA:15981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57443, ChEBI:CHEBI:59789; EC=;
COFACTOR Name=pyruvate; Xref=ChEBI:CHEBI:15361; Note=Binds 1 pyruvoyl group covalently per subunit.;
PATHWAYAmine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
SUBUNITHeterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.
PTMIs 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.
SIMILARITYBelongs to the prokaryotic AdoMetDC family. Type 2 subfamily.

Keywords [?]

Gene Ontology [?]

GO:0004014; Molecular function:adenosylmethionine decarboxylase activity
GO:0006596; Biological process:polyamine biosynthetic process
GO:0008295; Biological process:spermidine biosynthetic process

Cross-references [?]

Pfam PF02675; AdoMet_dc; 1;
NCBIfam TIGR03331; SAM_DCase_Eco; 1;

Features [?]

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

Additional information [?]

Size range 263-290 amino acids
Related rules None
Fusion Nter: None Cter: 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).

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