AC   MF_00464;
DC   Protein; auto
TR   HAMAP; MF_00464; -; 1; level=0
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Names: AdoMetDC_1
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ID   SPEH
DE   RecName: Full=S-adenosylmethionine decarboxylase proenzyme;
DE            Short=AdoMetDC;
DE            Short=SAMDC;
DE            EC=4.1.1.50;
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase beta chain;
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase alpha chain;
DE   Flags: Precursor;
GN   Name=speH;
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CC   -!- FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to S-
CC       adenosylmethioninamine (dcAdoMet), the propylamine donor required for
CC       the synthesis of the polyamines spermine and spermidine from the
CC       diamine putrescine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-
CC         (methylsulfanyl)propylamine; Xref=Rhea:RHEA:15981, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57443, ChEBI:CHEBI:59789; EC=4.1.1.50;
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC       Note=Binds 1 pyruvoyl group covalently per subunit.;
CC   -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC       biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC       step 1/1.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC       dimer of alpha/beta heterodimers.
CC   -!- PTM: Is synthesized initially as an inactive proenzyme. Formation of
CC       the active enzyme involves a self-maturation process in which the
CC       active site pyruvoyl group is generated from an internal serine residue
CC       via an autocatalytic post-translational modification. Two non-identical
CC       subunits are generated from the proenzyme in this reaction, and the
CC       pyruvate is formed at the N-terminus of the alpha chain, which is
CC       derived from the carboxyl end of the proenzyme. The post-translation
CC       cleavage follows an unusual pathway, termed non-hydrolytic serinolysis,
CC       in which the side chain hydroxyl group of the serine supplies its
CC       oxygen atom to form the C-terminus of the beta chain, while the
CC       remainder of the serine residue undergoes an oxidative deamination to
CC       produce ammonia and the pyruvoyl group blocking the N-terminus of the
CC       alpha chain.
CC   -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1
CC       subfamily.
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DR   Pfam; PF02675; AdoMet_dc; 1; trigger=no
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KW   Autocatalytic cleavage
KW   Decarboxylase
KW   Lyase
KW   Polyamine biosynthesis
KW   Pyruvate
KW   S-adenosyl-L-methionine
KW   Schiff base
KW   Spermidine biosynthesis
KW   Zymogen
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GO   GO:0004014; F:adenosylmethionine decarboxylase activity
GO   GO:0006596; P:polyamine biosynthetic process
GO   GO:0008295; P:spermidine biosynthetic process
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FT   From: SPEH_THEMA (Q9WZC3)
FT   CHAIN           Nter..62
FT                   /note="S-adenosylmethionine decarboxylase beta chain"
FT   CHAIN           63..Cter
FT                   /note="S-adenosylmethionine decarboxylase alpha chain"
FT   ACT_SITE        63
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT   Condition: S
FT   ACT_SITE        68
FT                   /note="Proton acceptor; for processing activity"
FT   Condition: H
FT   ACT_SITE        83
FT                   /note="Proton donor; for catalytic activity"
FT   Condition: C
FT   SITE            62..63
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT   Condition: E-S
FT   MOD_RES         63
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT   Condition: S
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Size: 105-160;
Related: MF_01298!;
Template: Q57763; Q9UWY8; Q9WZC3; O34426; O66615;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in BACAN, BACCR, BACCZ, HALH5
Plasmid: 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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# Revision 1.34 2023/01/17
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