ID   DCAM_LEIIN              Reviewed;         392 AA.
AC   Q9NGA0;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 82.
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;
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Taladriz S., Hanke T., Ramiro M.J., Larraga V.;
RT   "Leishmania infantum S-adenosylmethionine decarboxylase.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
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; AF255345; AAF67754.1; -; mRNA.
DR   AlphaFoldDB; Q9NGA0; -.
DR   SMR; Q9NGA0; -.
DR   STRING; 5671.XP_001467161.1; -.
DR   VEuPathDB; TriTrypDB:LINF_300036700; -.
DR   eggNOG; KOG0788; Eukaryota.
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   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..99
FT                   /note="S-adenosylmethionine decarboxylase beta chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000029981"
FT   CHAIN           100..392
FT                   /note="S-adenosylmethionine decarboxylase alpha chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000029982"
FT   ACT_SITE        43
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        46
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        100
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        114
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        264
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        277
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000250"
FT   SITE            99..100
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         100
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   392 AA;  44068 MW;  BD3F70F0CCA8532E CRC64;
     MKHGNYSLAT MNVCSNTTKD PLTLMAMWGS MKGYNPEQGF SFEGPEKRLE VILRCTLETH
     VDGLRSLDDS VWSGVVGSLN AQIVSRESNE YINSYVLTES SLFVMKNRII LITCGTTTLL
     NSIPNILEAI SAVRGELEWV SFMHKNYSFP WMQKGPHTSL ADEFATLKQH FPTGKPYIFG
     PVDSDHYFLF CYDDIIRPCS SEDDTQLSMT MYGLDKEQTK HWFSDRFIST SAETAAIRAA
     THLDRVVDGT WTLHDLQFEP CGYSINAIRD EEYQTMHITP EDHCSFASYE TNSRAANYSD
     RMKKVLGVFR PQRFTVIVFL DPESPVGKAY NEGKGIGVEP EYYPEYNLLH RTTNEFAPGY
     VAMKINYVRT AAVEETVTAV GGAEAGAEGG PD