Summary: Adenosylmethionine decarboxylase
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Adenosylmethionine decarboxylase Provide feedback
This is a family of S-adenosylmethionine decarboxylase (SAMDC) proenzymes. In the biosynthesis of polyamines SAMDC produces decarboxylated S-adenosylmethionine, which serves as the aminopropyl moiety necessary for spermidine and spermine biosynthesis from putrescine . The Pfam alignment contains both the alpha and beta chains that are cleaved to form the active enzyme.
Larsson J, Rasmuson-Lestander A; , Mol Gen Genet 1997;256:652-660.: Cloning, mapping and mutational analysis of the S-adenosylmethionine decarboxylase gene in Drosophila melanogaster. PUBMED:9435790 EPMC:9435790
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This tab holds annotation information from the InterPro database.
InterPro entry IPR001985
S-adenosylmethionine decarboxylase (AdoMetDC) [PUBMED:10378277] catalyzes the removal of the carboxylate group of S-adenosylmethionine to form S-adenosyl-5'-3-methylpropylamine which then acts as the n-propylamine group donor in the synthesis of the polyamines spermidine and spermine from putrescine.
The catalytic mechanism of AdoMetDC involves a covalently-bound pyruvoyl group. This group is post-translationally generated by a self-catalyzed intramolecular proteolytic cleavage reaction between a glutamate and a serine. This cleavage generates two chains, beta (N-terminal) and alpha (C-terminal). The N-terminal serine residue of the alpha chain is then converted by nonhydrolytic serinolysis into a pyruvyol group.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||adenosylmethionine decarboxylase activity (GO:0004014)|
|Biological process||spermine biosynthetic process (GO:0006597)|
|spermidine biosynthetic process (GO:0008295)|
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Curation and family details
|Seed source:||Pfam-B_600 (release 4.0)|
|Author:||Bashton M, Bateman A|
|Number in seed:||15|
|Number in full:||693|
|Average length of the domain:||293.80 aa|
|Average identity of full alignment:||34 %|
|Average coverage of the sequence by the domain:||87.33 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the SAM_decarbox domain has been found. There are 56 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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