HAMAP rule MF_00465
General rule information
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Accession | MF_00465 |
Dates | 18-OCT-2001 (Created)
1-JUN-2023 (Last updated, Version 32) |
Name | AdoMetDC_2 |
Scope(s) |
Bacteria Bacillota Gammaproteobacteria |
Template(s) | P0A7F6 (SPED_ECOLI); [ Recover all ] |
Triggered by |
HAMAP; MF_00465 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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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
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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=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=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
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Autocatalytic cleavage |
Decarboxylase |
Lyase |
Polyamine biosynthesis |
Pyruvate |
S-adenosyl-L-methionine |
Schiff base |
Spermidine biosynthesis |
Zymogen |
Gene Ontology
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GO:0004014; Molecular function:adenosylmethionine decarboxylase activity |
GO:0006596; Biological process:polyamine biosynthetic process |
GO:0008295; Biological process:spermidine biosynthetic process |
Cross-references
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Features
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From: SPED_ECOLI (P0A7F6) | ||||||||||||
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
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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). |