HAMAP rule MF_00464

General rule information [?]

Accession	MF_00464
Dates	18-OCT-2001 (Created) 17-JAN-2023 (Last updated, Version 34)

Name	AdoMetDC_1

Scope

Bacteria

Archaea

Templates

Q57763 (SPEH_METJA); Q9UWY8 (SPEH_SACS2); Q9WZC3 (SPEH_THEMA); O34426 (SPEH_BACSU); O66615 (SPEH_AQUAE): [Recover all]

Triggered by

HAMAP; MF_00464 (Get profile general information and statistics)

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 [?]

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;

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.

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