The domain within your query sequence starts at position 2 and ends at position 329; the E-value for the SAM_decarbox domain shown below is 2.4e-128.

EAAHFFEGTEKLLEVWFSRQQSDASQGSGDLRTIPRSEWDVLLKDVQCSIISVTKTDKQE
AYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPS
HQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEILM
SELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATLFNPCGYSMNGMKSDGTYWT
IHITPEPEFSYVSFETNLSQTSYDHLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLSSPQK
IDGFKRLDCQSAMFNDYNFVFTSFAKKQ

SAM_decarbox

SAM_decarbox
PFAM accession number:PF01536
Interpro abstract (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.

GO process:spermine biosynthetic process (GO:0006597), spermidine biosynthetic process (GO:0008295)
GO function:adenosylmethionine decarboxylase activity (GO:0004014)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry SAM_decarbox