UniProt functional annotation for P17707



	UniProt functional annotation for P17707

UniProt code: P17707.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels. {ECO:0000250|UniProtKB:P0DMN7}.

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; Evidence={ECO:0000269|PubMed:10029540, ECO:0000269|PubMed:10574985, ECO:0000269|PubMed:11583147, ECO:0000269|PubMed:1917972, ECO:0000269|PubMed:2460457, ECO:0000269|PubMed:2687270};

Cofactor: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000269|PubMed:11583147}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000269|PubMed:11583147};

Activity regulation: Both proenzyme processing and catalytic activity are stimulated by putrescine. Catalytic activity is inhibited by iodoacetic acid.

Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. {ECO:0000269|PubMed:10029540, ECO:0000269|PubMed:10574985, ECO:0000269|PubMed:11583147, ECO:0000269|PubMed:1917972, ECO:0000269|PubMed:2460457, ECO:0000269|PubMed:2687270}.

Subunit: Heterotetramer of two alpha and two beta chains. {ECO:0000269|PubMed:11583147}.

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. {ECO:0000269|PubMed:10574985, ECO:0000269|PubMed:1917972, ECO:0000269|PubMed:2460457, ECO:0000269|PubMed:2687270}.

Similarity: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels. {ECO:0000250\|UniProtKB:P0DMN7}.


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; Evidence={ECO:0000269\|PubMed:10029540, ECO:0000269\|PubMed:10574985, ECO:0000269\|PubMed:11583147, ECO:0000269\|PubMed:1917972, ECO:0000269\|PubMed:2460457, ECO:0000269\|PubMed:2687270};
Cofactor:		Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000269\|PubMed:11583147}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000269\|PubMed:11583147};
Activity regulation:		Both proenzyme processing and catalytic activity are stimulated by putrescine. Catalytic activity is inhibited by iodoacetic acid.
Pathway:		Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. {ECO:0000269\|PubMed:10029540, ECO:0000269\|PubMed:10574985, ECO:0000269\|PubMed:11583147, ECO:0000269\|PubMed:1917972, ECO:0000269\|PubMed:2460457, ECO:0000269\|PubMed:2687270}.
Subunit:		Heterotetramer of two alpha and two beta chains. {ECO:0000269\|PubMed:11583147}.
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. {ECO:0000269\|PubMed:10574985, ECO:0000269\|PubMed:1917972, ECO:0000269\|PubMed:2460457, ECO:0000269\|PubMed:2687270}.
Similarity:		Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.