ID   DCAM_YEAST              Reviewed;         396 AA.
AC   P21182; D6W216;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   04-NOV-2026, entry version 196.
DE   RecName: Full=S-adenosylmethionine decarboxylase proenzyme;
DE            Short=AdoMetDC;
DE            Short=SAMDC;
DE            EC=4.1.1.50 {ECO:0000269|PubMed:2266128};
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=SPE2; OrderedLocusNames=YOL052C; ORFNames=O1275;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20 AND 88-104,
RP   FUNCTION, CATALYTIC ACTIVITY, AND PYRUVATE FORMATION AT SER-88.
RX   PubMed=2266128; DOI=10.1016/s0021-9258(18)45708-0;
RA   Kashiwagi K., Taneja S.K., Liu T.-Y., Tabor C.W., Tabor H.;
RT   "Spermidine biosynthesis in Saccharomyces cerevisiae. Biosynthesis and
RT   processing of a proenzyme form of S-adenosylmethionine decarboxylase.";
RL   J. Biol. Chem. 265:22321-22328(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 90843 / S288c / FY73;
RX   PubMed=8789261;
RX   DOI=10.1002/(sici)1097-0061(199601)12:1<67::aid-yea884>3.0.co;2-f;
RA   Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.;
RT   "Analysis of a 26 kb region on the left arm of yeast chromosome XV.";
RL   Yeast 12:67-76(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874; DOI=10.1038/387s098;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine, a key
CC       step in the biosynthetic pathway for spermidine and spermine. It is
CC       essential for normal growth, sporulation, and maintenance of ds-RNA
CC       virus. {ECO:0000305|PubMed:2266128}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + H(+) = S-adenosyl 3-
CC         (methylsulfanyl)propylamine + CO2; Xref=Rhea:RHEA:15981,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57443,
CC         ChEBI:CHEBI:59789; EC=4.1.1.50;
CC         Evidence={ECO:0000269|PubMed:2266128};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15982;
CC         Evidence={ECO:0000305|PubMed:2266128};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC       Note=Binds 1 pyruvoyl group covalently per subunit.
CC       {ECO:0000269|PubMed:2266128};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC       biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC       step 1/1. {ECO:0000305|PubMed:2266128}.
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:0000269|PubMed:2266128}.
CC   -!- MISCELLANEOUS: Present with 7060 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M38434; AAA34421.1; -; Genomic_DNA.
DR   EMBL; X91067; CAA62536.1; -; Genomic_DNA.
DR   EMBL; Z74794; CAA99058.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10732.1; -; Genomic_DNA.
DR   PIR; S12772; DCBYDM.
DR   RefSeq; NP_014590.1; NM_001183306.1.
DR   SMR; P21182; -.
DR   BioGRID; 34352; 319.
DR   DIP; DIP-361N; -.
DR   IntAct; P21182; 1.
DR   STRING; 4932.YOL052C; -.
DR   iPTMnet; P21182; -.
DR   PaxDb; 4932-YOL052C; -.
DR   PeptideAtlas; P21182; -.
DR   EnsemblFungi; YOL052C_mRNA; YOL052C; YOL052C.
DR   GeneID; 854105; -.
DR   KEGG; sce:YOL052C; -.
DR   VEuPathDB; FungiDB:YOL052C; -.
DR   AGR; SGD:S000005412; -.
DR   SGD; S000005412; SPE2.
DR   eggNOG; KOG0788; Eukaryota.
DR   HOGENOM; CLU_023050_0_0_1; -.
DR   InParanoid; P21182; -.
DR   OMA; AACEHSA; -.
DR   OrthoDB; 1068353at2759; -.
DR   BioCyc; MetaCyc:MONOMER-20234; -.
DR   BioCyc; YEAST:MONOMER-20234; -.
DR   BRENDA; 4.1.1.50; 984.
DR   Reactome; R-SCE-351202; Metabolism of polyamines.
DR   UniPathway; UPA00331; UER00451.
DR   PRO; PR:P21182; -.
DR   FunFam; 3.60.90.10:FF:000011; S-adenosylmethionine decarboxylase proenzyme; 1.
DR   Gene3D; 3.60.90.10; S-adenosylmethionine decarboxylase; 1.
DR   InterPro; IPR048283; AdoMetDC-like.
DR   InterPro; IPR001985; S-AdoMet_decarboxylase_euk.
DR   InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR   InterPro; IPR018166; S-AdoMet_deCO2ase_CS.
DR   PANTHER; PTHR11570; S-ADENOSYLMETHIONINE DECARBOXYLASE; 1.
DR   PANTHER; PTHR11570:SF0; S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME; 1.
DR   Pfam; PF01536; SAM_decarbox; 1.
DR   PIRSF; PIRSF001355; S-AdenosylMet_decarboxylase; 1.
DR   SUPFAM; SSF56276; S-adenosylmethionine decarboxylase; 1.
DR   NCBIfam; TIGR00535; SAM_DCase; 1.
DR   PROSITE; PS01336; ADOMETDC; 1.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IDA:SGD.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IMP:SGD.
DR   GO; GO:0006597; P:spermine biosynthetic process; IMP:SGD.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P21182; protein.
DR   BioGRID-ORCS; 854105; 1 hit in 10 CRISPR screens.
DR   AlphaFoldDB; P21182; -.
DR   FunCoup; P21182; 732.
PE   1: Evidence at protein level;
KW   Autocatalytic cleavage; Decarboxylase; Direct protein sequencing; Lyase;
KW   Polyamine biosynthesis; Pyruvate; Reference proteome;
KW   S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis; Zymogen.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2266128"
FT   CHAIN           2..87
FT                   /note="S-adenosylmethionine decarboxylase beta chain"
FT                   /id="PRO_0000030033"
FT   CHAIN           88..396
FT                   /note="S-adenosylmethionine decarboxylase alpha chain"
FT                   /id="PRO_0000030034"
FT   ACT_SITE        29
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        32
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        88
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000269|PubMed:2266128"
FT   ACT_SITE        102
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        287
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        301
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000250"
FT   SITE            87..88
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT                   /evidence="ECO:0000269|PubMed:2266128"
FT   MOD_RES         88
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:2266128"
SQ   SEQUENCE   396 AA;  46232 MW;  8B63676CB5636D71 CRC64;
     MTVTIKELTN HNYIDHELSA TLDSTDAFEG PEKLLEIWFF PHKKSITTEK TLRNIGMDRW
     IEILKLVKCE VLSMKKTKEL DAFLLSESSL FVFDHKLTMK TCGTTTTLFC LEKLFQIVEQ
     ELSWAFRTTQ GGKYKPFKVF YSRRCFLFPC KQAAIHQNWA DEVDYLNKFF DNGKSYSVGR
     NDKSNHWNLY VTETDRSTPK GKEYIEDDDE TFEVLMTELD PECASKFVCG PEASTTALVE
     PNEDKGHNLG YQMTKNTRLD EIYVNSAQDS DLSFHHDAFA FTPCGYSSNM ILAEKYYYTL
     HVTPEKGWSY ASFESNIPVF DISQGKQDNL DVLLHILNVF QPREFSMTFF TKNYQNQSFQ
     KLLSINESLP DYIKLDKIVY DLDDYHLFYM KLQKKI
//