ID   DCAM_PEA                Reviewed;         353 AA.
AC   Q43820;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 58.
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   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Alaska;
RX   PubMed=11925048; DOI=10.1007/s004250100653;
RA   Marco F., Carrasco P.;
RT   "Expression of the pea S-adenosylmethionine decarboxylase gene is
RT   involved in developmental and environmental responses.";
RL   Planta 214:641-647(2002).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = (5-deoxy-5-
CC       adenosyl)(3-aminopropyl)-methylsulfonium salt + CO(2).
CC   -!- COFACTOR: Pyruvoyl group (By similarity).
CC   -!- PATHWAY: Amine and polyamine biosynthesis; S-
CC       adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from
CC       S-adenosyl-L-methionine: step 1/1.
CC   -!- PTM: Is synthesized initially as an inactive proenzyme. Formation
CC       of the active enzyme involves a self-maturation process in which
CC       the active site pyruvoyl group is generated from an internal
CC       serine residue via an autocatalytic post-translational
CC       modification. Two non-identical subunits are generated from the
CC       proenzyme in this reaction, and the pyruvate is formed at the N-
CC       terminus of the alpha chain, which is derived from the carboxyl
CC       end of the proenzyme. The post-translation cleavage follows an
CC       unusual pathway, termed non-hydrolytic serinolysis, in which the
CC       side chain hydroxyl group of the serine supplies its oxygen atom
CC       to form the C-terminus of the beta chain, while the remainder of
CC       the serine residue undergoes an oxidative deamination to produce
CC       ammonia and the pyruvoyl group blocking the N-terminus of the
CC       alpha chain (By similarity).
CC   -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family.
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DR   EMBL; U60592; AAB03865.1; -; mRNA.
DR   PIR; T06515; T06515.
DR   HSSP; P17707; 1JEN.
DR   BRENDA; 4.1.1.50; 287.
DR   GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:EC.
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; IPR018167; S-AdoMet_decarboxylase_sg.
DR   InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR   InterPro; IPR018166; S-AdoMet_deCO2ase_CS.
DR   Gene3D; G3DSA:3.60.90.10; SAM_decarbox; 1.
DR   PANTHER; PTHR11570; SAM_decarbox; 1.
DR   Pfam; PF01536; SAM_decarbox; 1.
DR   PIRSF; PIRSF001355; S-AdenosylMet_decarboxylase; 1.
DR   ProDom; PD002379; SAM_decarbox; 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;
KW   Spermidine biosynthesis; Zymogen.
FT   CHAIN         1     68       S-adenosylmethionine decarboxylase beta
FT                                chain (By similarity).
FT                                /FTId=PRO_0000030019.
FT   CHAIN        69    353       S-adenosylmethionine decarboxylase alpha
FT                                chain (By similarity).
FT                                /FTId=PRO_0000030020.
FT   ACT_SITE      9      9       By similarity.
FT   ACT_SITE     12     12       By similarity.
FT   ACT_SITE     69     69       Schiff-base intermediate with substrate;
FT                                via pyruvic acid (By similarity).
FT   ACT_SITE     83     83       Proton donor; for catalytic activity (By
FT                                similarity).
FT   ACT_SITE    232    232       Proton acceptor; for processing activity
FT                                (By similarity).
FT   ACT_SITE    245    245       Proton acceptor; for processing activity
FT                                (By similarity).
FT   SITE         68     69       Cleavage (non-hydrolytic); by autolysis
FT                                (By similarity).
FT   MOD_RES      69     69       Pyruvic acid (Ser); by autocatalysis (By
FT                                similarity).
SQ   SEQUENCE   353 AA;  38683 MW;  51FACD264FEBD30B CRC64;
     MAVSAIGFEG FEKRLEISFS DPGLFSDPQG RGLRSLTKSQ LDEILAPAEC TIVSSLANED
     VDSYVLSESS LFVYAYKLII KTCGTTKLLL SIPPILKLAD SISLNVRSVR YTRGSFIFPG
     AQSFPHRHFS EEVAVLDGFF GKLGSGSMAY ILGGSDEAQN WHIYCASSDS VSPEGSVYTL
     EMCMTGLDRE KASVFFKEQT GSAAEMTVNS GIRKILRNSE ICDFDFEPCG YSMNSVEGSA
     VSTIHITPED GFSYASFETA GYDLKAINLN EMVMRVLACF QPTEFSVAVH VDNASKSFEQ
     GCLLDVKGYC CEEKSHQGLG MSGSVVYQKF LKTSYCGSPR STLKCWKDED EEE
//