DCAM_CATRO
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 25-MAY-2022, entry version 93.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Catharanthinae; Catharanthus.
OX NCBI_TaxID=4058;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PYRUVATE FORMATION AT SER-71, AND MUTAGENESIS
RP OF SER-71.
RX PubMed=7883014; DOI=10.1111/j.1432-1033.1995.0074o.x;
RA Schroeder G., Schroeder J.;
RT "cDNAs for S-adenosyl-L-methionine decarboxylase from Catharanthus roseus,
RT heterologous expression, identification of the proenzyme-processing site,
RT evidence for the presence of both subunits in the active enzyme, and a
RT conserved region in the 5' mRNA leader.";
RL Eur. J. Biochem. 228:74-78(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;
CC Note=Binds 1 pyruvoyl group covalently per subunit.;
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.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
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DR EMBL; U12573; AAC48989.1; -; mRNA.
DR PIR; S68990; S68990.
DR AlphaFoldDB; Q42679; -.
DR SMR; Q42679; -.
DR SABIO-RK; Q42679; -.
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 1: Evidence at protein level;
KW Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis;
KW Pyruvate; S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis;
KW Zymogen.
FT CHAIN 1..70
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /id="PRO_0000029997"
FT CHAIN 71..357
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /id="PRO_0000029998"
FT ACT_SITE 11
FT /evidence="ECO:0000250"
FT ACT_SITE 14
FT /evidence="ECO:0000250"
FT ACT_SITE 71
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250"
FT ACT_SITE 85
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 234
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 247
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT SITE 70..71
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT MOD_RES 71
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000269|PubMed:7883014"
FT MUTAGEN 71
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7883014"
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
