HAMAP rule MF_00465

General rule information [?]

PURL	https://purl.expasy.org/hamap/rule/MF_00465
Accession	MF_00465
Dates	28-FEB-2005 (Created) 03-SEP-2024 (Last updated, Version 23)
Name	AdoMetDC_2
Scope(s)	Bacteria Bacillota Gammaproteobacteria
Template(s)	P0A7F6; [ 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; 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	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	Reaction=S-adenosyl-L-methionine + H(+) = S-adenosyl 3- (methylsulfanyl)propylamine + CO2; Xref=Rhea:RHEA:15981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57443, ChEBI:CHEBI:59789; EC=4.1.1.50;
COFACTOR	Name=pyruvate; Xref=ChEBI:CHEBI:15361; 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: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 [?]

From: SPED_ECOLI (P0A7F6)

Key

From

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

/note="Schiff-base intermediate with substrate; via pyruvic acid"

ACT_SITE

117

/note="Proton acceptor; for processing activity"

ACT_SITE

140

/note="Proton donor; for catalytic activity"

SITE

111

112

/note="Cleavage (non-hydrolytic); by autolysis"

K-S

MOD_RES

112

/note="Pyruvic acid (Ser); by autocatalysis"

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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