DCAM_YEAST
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 03-AUG-2022, entry version 178.
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;
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=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: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}.
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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 AlphaFoldDB; P21182; -.
DR SMR; P21182; -.
DR BioGRID; 34352; 312.
DR DIP; DIP-361N; -.
DR MINT; P21182; -.
DR STRING; 4932.YOL052C; -.
DR MaxQB; P21182; -.
DR PaxDb; P21182; -.
DR PRIDE; P21182; -.
DR EnsemblFungi; YOL052C_mRNA; YOL052C; YOL052C.
DR GeneID; 854105; -.
DR KEGG; sce:YOL052C; -.
DR SGD; S000005412; SPE2.
DR VEuPathDB; FungiDB:YOL052C; -.
DR eggNOG; KOG0788; Eukaryota.
DR GeneTree; ENSGT00390000011776; -.
DR HOGENOM; CLU_023050_0_0_1; -.
DR InParanoid; P21182; -.
DR OMA; LEIWFEE; -.
DR BioCyc; MetaCyc:MON-20234; -.
DR BioCyc; YEAST:MON-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 Proteomes; UP000002311; Chromosome XV.
DR RNAct; P21182; protein.
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:0015940; P:pantothenate biosynthetic process; IMP:SGD.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008295; P:spermidine biosynthetic process; IMP:SGD.
DR GO; GO:0006597; P:spermine biosynthetic process; IMP:SGD.
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; 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
