ID   DCAM_VICFA              Reviewed;         353 AA.
AC   Q9M4D8;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=S-adenosylmethionine decarboxylase proenzyme;
DE            Short=AdoMetDC;
DE            Short=SAMDC;
DE            EC=4.1.1.50;
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase alpha chain;
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase beta chain;
DE   Flags: Precursor;
GN   Name=SAMDC;
OS   Vicia faba (Broad bean) (Faba vulgaris).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Vicia.
OX   NCBI_TaxID=3906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Kleine Thueringer; TISSUE=Root nodule;
RA   Fruehling M., Puehler A., Perlick A.M.;
RT   "Isolation and characterization of a full-length cDNA encoding S-
RT   adenosylmethionine decarboxylase from broad bean (Vicia faba L.).";
RL   (er) Plant Gene Register PGR00-029(2000).
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; AJ250026; CAB76966.1; -; mRNA.
DR   AlphaFoldDB; Q9M4D8; -.
DR   SMR; Q9M4D8; -.
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..68
FT                   /note="S-adenosylmethionine decarboxylase beta chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000030029"
FT   CHAIN           69..353
FT                   /note="S-adenosylmethionine decarboxylase alpha chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000030030"
FT   ACT_SITE        9
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        12
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        69
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        83
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        232
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        245
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000250"
FT   SITE            68..69
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         69
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   353 AA;  38513 MW;  90AB36A7FE0F0454 CRC64;
     MAVSAIGFEG FEKRLEISFS DPGLFSDPQG RGLRSLTKSQ LDEILAPAEC TIVSSLANED
     VDSYVLSESS LFVYAYKIII KTCGTTKLLL AIPPILKLAE SISLDVRAVR YTRGSFIFPG
     AQSFPHRHFS EEVAVLDGFF GKLGSGSKAY IMGGSDEAQN WHVYCASADS VSPADSVYTL
     EMCMTGLDRE KASVFFKQQT GSAAEMTVNS GIRKILPNSE ICDFDFEPCG YSMNSVEGPA
     VSTIHITPED GFSYASFETA GYDLKAMNLN EMVMRVLACF QPTEFSVAVH VDNASKSFEQ
     GCLLDVKGYC CDEKSHQGLG MSGSVVYQKF VKASDCGSPR STLKCWKDED EEE