ID   DCAM2_MUSSP             Reviewed;         334 AA.
AC   P82185;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2000, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=S-adenosylmethionine decarboxylase proenzyme 2;
DE            Short=AdoMetDC 2;
DE            Short=SAMDC 2;
DE            EC=4.1.1.50 {ECO:0000250|UniProtKB:D3Z6H8};
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase 2 alpha chain;
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase 2 beta chain;
DE   Flags: Precursor;
GN   Name=Amd2;
OS   Mus spretus (Western Mediterranean mouse) (Algerian mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10096;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=10430664; DOI=10.1007/s003359901092;
RA   Persson K., Heby O., Berger F.G.;
RT   "The functional intronless S-adenosylmethionine decarboxylase gene of the
RT   mouse (Amd-2) is linked to the ornithine decarboxylase gene (Odc) on
RT   chromosome 12 and is present in distantly related species of the genus
RT   Mus.";
RL   Mamm. Genome 10:784-788(1999).
CC   -!- FUNCTION: Essential for biosynthesis of the polyamines spermidine and
CC       spermine. Promotes maintenance and self-renewal of embryonic stem
CC       cells, by maintaining spermine levels. {ECO:0000250|UniProtKB:P0DMN7}.
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         Evidence={ECO:0000250|UniProtKB:D3Z6H8};
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   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC       {ECO:0000250}.
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. {ECO:0000250|UniProtKB:P17707}.
CC   -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
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DR   EMBL; AF052604; AAD45965.1; -; Genomic_DNA.
DR   AlphaFoldDB; P82185; -.
DR   SMR; P82185; -.
DR   MGI; MGI:1333111; Amd2.
DR   UniPathway; UPA00331; UER00451.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0019810; F:putrescine binding; IBA:GO_Central.
DR   GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006597; P:spermine biosynthetic process; IBA:GO_Central.
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   3: Inferred from homology;
KW   Autocatalytic cleavage; Decarboxylase; Lyase; Phosphoprotein;
KW   Polyamine biosynthesis; Pyruvate; S-adenosyl-L-methionine; Schiff base;
KW   Spermidine biosynthesis; Zymogen.
FT   CHAIN           1..67
FT                   /note="S-adenosylmethionine decarboxylase 2 beta chain"
FT                   /id="PRO_0000029967"
FT   CHAIN           68..334
FT                   /note="S-adenosylmethionine decarboxylase 2 alpha chain"
FT                   /id="PRO_0000029968"
FT   ACT_SITE        8
FT                   /evidence="ECO:0000250|UniProtKB:P17707"
FT   ACT_SITE        11
FT                   /evidence="ECO:0000250|UniProtKB:P17707"
FT   ACT_SITE        68
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000250|UniProtKB:P17707"
FT   ACT_SITE        82
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:P17707"
FT   ACT_SITE        229
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000250|UniProtKB:P17707"
FT   ACT_SITE        243
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000250|UniProtKB:P17707"
FT   BINDING         7
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P17707"
FT   BINDING         67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P17707"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P17707"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P17707"
FT   SITE            67..68
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P17707"
FT   MOD_RES         68
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P17707"
FT   MOD_RES         298
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17707"
SQ   SEQUENCE   334 AA;  38301 MW;  A78BB36F2DB134F4 CRC64;
     MEAAHFFEGT EKLLEVWFSR QQSDASQGSG DLRTIPRSEW DVLLKDVQCS IISVTKTDKQ
     EAYVLSESSM FVSKRRFILK TCGTTLLLKA LVPLLKLARD YSGFDSIQSF FYSRKNFMKP
     SHQGYPHRNF QEEIEFLNVI FPNGAAYCMG RMNSDCWYLY TLDFPESRVI SQPDQTLEIL
     MSELDPAVMD QFYMKDGVTA KDVTRESGIR DLIPGSVIDA TLFNPCGYSM NGMKSDGTYW
     TIHITPEPEF SYVSFETNLS QTSYDDLIRK VVEVFKPGKF VTTLFVNQSS KCRTVLSSPQ
     KIDGFKRLDC QSAMFNDYNF VFTSFAKKQQ QQQS