UniProt functional annotation for Q9WZC3



	UniProt functional annotation for Q9WZC3

UniProt code: Q9WZC3.

Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8).

Taxonomy: Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.

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. {ECO:0000250}.

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; Evidence={ECO:0000305}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000305};

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. {ECO:0000269|PubMed:15150268}.

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 (Probable). {ECO:0000305}.

Similarity: Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8).
Taxonomy:		Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.



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. {ECO:0000250}.


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; Evidence={ECO:0000305}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000305};
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. {ECO:0000269\|PubMed:15150268}.
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 (Probable). {ECO:0000305}.
Similarity:		Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. {ECO:0000305}.