HAMAP rule MF_00464
General rule information
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| Accession | MF_00464 |
| Dates | 18-OCT-2001 (Created)
17-JAN-2023 (Last updated, Version 34) |
| Name | AdoMetDC_1 |
| Scope(s) |
Bacteria Archaea |
| Template(s) | 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
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Identifier, protein and gene names
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| 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 | Name=speH; |
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 | 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
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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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| Pfam | PF02675; AdoMet_dc; 1; |
Features
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| From: SPEH_THEMA (Q9WZC3) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| CHAIN | Nter | 62 | /note="S-adenosylmethionine decarboxylase beta chain" | |||||||||
| CHAIN | 63 | Cter | /note="S-adenosylmethionine decarboxylase alpha chain" | |||||||||
| ACT_SITE | 63 | 63 | /note="Schiff-base intermediate with substrate; via pyruvic acid" | S | ||||||||
| ACT_SITE | 68 | 68 | /note="Proton acceptor; for processing activity" | H | ||||||||
| ACT_SITE | 83 | 83 | /note="Proton donor; for catalytic activity" | C | ||||||||
| SITE | 62 | 63 | /note="Cleavage (non-hydrolytic); by autolysis" | E-S | ||||||||
| MOD_RES | 63 | 63 | /note="Pyruvic acid (Ser); by autocatalysis" | S | ||||||||
Additional information
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| Size range | 105-160 amino acids |
| Related rules |
MF_01298 |
| Fusion | Nter: None Cter: 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. |