ID   DCAM2_DIACA             Reviewed;         377 AA.
AC   Q39677;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=S-adenosylmethionine decarboxylase proenzyme 2;
DE            Short=AdoMetDC 2;
DE            Short=SAMDC 2;
DE            EC=4.1.1.50;
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase 2 alpha chain;
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase 2 beta chain;
DE   Flags: Precursor;
GN   Name=SAMDC2; Synonyms=SAMDC16;
OS   Dianthus caryophyllus (Carnation) (Clove pink).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Caryophyllaceae; Caryophylleae; Dianthus.
OX   NCBI_TaxID=3570;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. White Sim; TISSUE=Petal;
RA   Lee M.M., Lee S.H., Park K.Y.;
RT   "Nucleotide sequence of cDNAs encoding S-adenosylmethionine decarboxylase
RT   from carnation flower.";
RL   (er) Plant Gene Register PGR95-139(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-
CC         (methylsulfanyl)propylamine; Xref=Rhea:RHEA:15981, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57443, ChEBI:CHEBI:59789; EC=4.1.1.50;
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000250};
CC       Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC       biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC       step 1/1.
CC   -!- PTM: Is synthesized initially as an inactive proenzyme. Formation of
CC       the active enzyme involves a self-maturation process in which the
CC       active site pyruvoyl group is generated from an internal serine residue
CC       via an autocatalytic post-translational modification. Two non-identical
CC       subunits are generated from the proenzyme in this reaction, and the
CC       pyruvate is formed at the N-terminus of the alpha chain, which is
CC       derived from the carboxyl end of the proenzyme. The post-translation
CC       cleavage follows an unusual pathway, termed non-hydrolytic serinolysis,
CC       in which the side chain hydroxyl group of the serine supplies its
CC       oxygen atom to form the C-terminus of the beta chain, while the
CC       remainder of the serine residue undergoes an oxidative deamination to
CC       produce ammonia and the pyruvoyl group blocking the N-terminus of the
CC       alpha chain (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
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DR   EMBL; U38527; AAD09840.1; -; mRNA.
DR   PIR; T10708; T10708.
DR   AlphaFoldDB; Q39677; -.
DR   SMR; Q39677; -.
DR   UniPathway; UPA00331; UER00451.
DR   GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006597; P:spermine biosynthetic process; IEA:InterPro.
DR   InterPro; IPR001985; S-AdoMet_decarboxylase.
DR   InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR   InterPro; IPR018166; S-AdoMet_deCO2ase_CS.
DR   PANTHER; PTHR11570; PTHR11570; 1.
DR   Pfam; PF01536; SAM_decarbox; 1.
DR   PIRSF; PIRSF001355; S-AdenosylMet_decarboxylase; 1.
DR   SUPFAM; SSF56276; SSF56276; 1.
DR   TIGRFAMs; TIGR00535; SAM_DCase; 1.
DR   PROSITE; PS01336; ADOMETDC; 1.
PE   2: Evidence at transcript level;
KW   Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis;
KW   Pyruvate; S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis;
KW   Zymogen.
FT   CHAIN           1..83
FT                   /note="S-adenosylmethionine decarboxylase 2 beta chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000030005"
FT   CHAIN           84..377
FT                   /note="S-adenosylmethionine decarboxylase 2 alpha chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000030006"
FT   ACT_SITE        24
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        27
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        84
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        98
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        246
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        259
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000250"
FT   SITE            83..84
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         84
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   377 AA;  41344 MW;  C3E58AAD143F1AD6 CRC64;
     MTIPMMGNTT DDNNNMTISA IGFEGFEKRL EISFFEPGIF VDPEGKGLRA LSKAHLDEIL
     GPAECTIVDS LANESVDSYV LSESSLFVYS YKIIIKTCGT TKLLNSIPPI LRLAETLFLD
     VKSVRYTRGS FIFPGAQSFP HRSFSEEVAV LDNYFAKLGA GSKAIVMGSP GKPQKWHVYS
     ATAETNYDDP VYTLEMCMTG LDKEKASVFF KSQSASAAVM TESSGIRKIL PDSVICDFDF
     EPCGYSMNAI EGPAVSTIHI TPEDGFSYAS FEAVGYDLQV VDLNLLVERV LACFEPKEFS
     IAVHADTDTA DKVLARNCSV NVIGYSREEG GIEELGLGGS VFYQKFCKGT APVCPPAPKK
     TLKCCWKEEE IDEEMEF