ID   DCAM_CATRO              Reviewed;         357 AA.
AC   Q42679;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 59.
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   Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC   Catharanthus.
OX   NCBI_TaxID=4058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PYRUVATE FORMATION AT SER-71, AND
RP   MUTAGENESIS OF SER-71.
RX   MEDLINE=95188916; PubMed=7883014;
RX   DOI=10.1111/j.1432-1033.1995.tb20231.x;
RA   Schroeder G., Schroeder J.;
RT   "cDNAs for S-adenosyl-L-methionine decarboxylase from Catharanthus
RT   roseus, heterologous expression, identification of the proenzyme-
RT   processing site, evidence for the presence of both subunits in the
RT   active enzyme, and a conserved region in the 5' mRNA leader.";
RL   Eur. J. Biochem. 228:74-78(1995).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = (5-deoxy-5-
CC       adenosyl)(3-aminopropyl)-methylsulfonium salt + CO(2).
CC   -!- COFACTOR: Pyruvoyl group.
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.
CC   -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family.
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DR   EMBL; U12573; AAC48989.1; -; mRNA.
DR   PIR; S68990; S68990.
DR   HSSP; P17707; 1JEN.
DR   BRENDA; 4.1.1.50; 20471.
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   1: Evidence at protein level;
KW   Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis;
KW   Pyruvate; S-adenosyl-L-methionine; Schiff base;
KW   Spermidine biosynthesis; Zymogen.
FT   CHAIN         1     70       S-adenosylmethionine decarboxylase beta
FT                                chain.
FT                                /FTId=PRO_0000029997.
FT   CHAIN        71    357       S-adenosylmethionine decarboxylase alpha
FT                                chain.
FT                                /FTId=PRO_0000029998.
FT   ACT_SITE     11     11       By similarity.
FT   ACT_SITE     14     14       By similarity.
FT   ACT_SITE     71     71       Schiff-base intermediate with substrate;
FT                                via pyruvic acid (By similarity).
FT   ACT_SITE     85     85       Proton donor; for catalytic activity (By
FT                                similarity).
FT   ACT_SITE    234    234       Proton acceptor; for processing activity
FT                                (By similarity).
FT   ACT_SITE    247    247       Proton acceptor; for processing activity
FT                                (By similarity).
FT   SITE         70     71       Cleavage (non-hydrolytic); by autolysis.
FT   MOD_RES      71     71       Pyruvic acid (Ser); by autocatalysis.
FT   MUTAGEN      71     71       S->A: Loss of activity.
SQ   SEQUENCE   357 AA;  39714 MW;  364918E116388301 CRC64;
     MALPASAIGF EGYEKRLEIS FFESSFFADP DGKGLRALNK SQIDEILEPA ECTIVDSLSN
     QYLDSYVLSE SSLFVYPYKI IIKTCGTTKL LLSIPAILKL AESLSLSVRN VKYTRGSFIF
     PGAQSFPHRS FSEEVELLDN YFGKLGLESN AFIMGNPDQP QKWHVYSASV GSEQSSDPTY
     TLEMCMTGLD REKASVFYKS ESSSAALMTT RSGIRKILPD SEICDFEFDP CGYSMNSIEE
     AAISTIHVTP EDGFSYASFE AAGYDLKAQN LGMMIERVLA CFQPSEFSVA VHCDVTCKSL
     EQICSLELKE YSLDEKINEE LGLGGSIIYK KFLRIDACGS PRSILKCCWK EDESEEE
//