ID   A3PF61_PROM0            Unreviewed;       144 AA.
AC   A3PF61;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   18-JUN-2025, entry version 103.
DE   RecName: Full=S-adenosylmethionine decarboxylase proenzyme {ECO:0000256|HAMAP-Rule:MF_00464};
DE            Short=AdoMetDC {ECO:0000256|HAMAP-Rule:MF_00464};
DE            Short=SAMDC {ECO:0000256|HAMAP-Rule:MF_00464};
DE            EC=4.1.1.50 {ECO:0000256|HAMAP-Rule:MF_00464};
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase beta chain {ECO:0000256|HAMAP-Rule:MF_00464};
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00464};
GN   Name=speD {ECO:0000313|EMBL:ABO18386.1};
GN   Synonyms=speH {ECO:0000256|HAMAP-Rule:MF_00464};
GN   OrderedLocusNames=P9301_17631 {ECO:0000313|EMBL:ABO18386.1};
OS   Prochlorococcus marinus (strain MIT 9301).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=167546 {ECO:0000313|EMBL:ABO18386.1, ECO:0000313|Proteomes:UP000001430};
RN   [1] {ECO:0000313|EMBL:ABO18386.1, ECO:0000313|Proteomes:UP000001430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9301 {ECO:0000313|EMBL:ABO18386.1,
RC   ECO:0000313|Proteomes:UP000001430};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to S-
CC       adenosylmethioninamine (dcAdoMet), the propylamine donor required for
CC       the synthesis of the polyamines spermine and spermidine from the
CC       diamine putrescine. {ECO:0000256|HAMAP-Rule:MF_00464}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00464};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00464};
CC       Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00464};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC       biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC       step 1/1. {ECO:0000256|HAMAP-Rule:MF_00464}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC       dimer of alpha/beta heterodimers. {ECO:0000256|HAMAP-Rule:MF_00464}.
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:0000256|HAMAP-Rule:MF_00464}.
CC   -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00464}.
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DR   EMBL; CP000576; ABO18386.1; -; Genomic_DNA.
DR   RefSeq; WP_011863674.1; NC_009091.1.
DR   AlphaFoldDB; A3PF61; -.
DR   STRING; 167546.P9301_17631; -.
DR   KEGG; pmg:P9301_17631; -.
DR   eggNOG; COG1586; Bacteria.
DR   HOGENOM; CLU_125470_2_0_3; -.
DR   OrthoDB; 9793120at2; -.
DR   UniPathway; UPA00331; UER00451.
DR   Proteomes; UP000001430; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.60.90.10; S-adenosylmethionine decarboxylase; 1.
DR   HAMAP; MF_00464; AdoMetDC_1; 1.
DR   InterPro; IPR003826; AdoMetDC_fam_prok.
DR   InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR   InterPro; IPR017716; S-AdoMet_deCOase_pro-enz.
DR   NCBIfam; TIGR03330; SAM_DCase_Bsu; 1.
DR   PANTHER; PTHR33866; S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME; 1.
DR   PANTHER; PTHR33866:SF2; S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME; 1.
DR   Pfam; PF02675; AdoMet_dc; 1.
DR   SUPFAM; SSF56276; S-adenosylmethionine decarboxylase; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, ECO:0000256|HAMAP-
KW   Rule:MF_00464};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_00464};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00464};
KW   Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|HAMAP-
KW   Rule:MF_00464};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|HAMAP-Rule:MF_00464};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001430};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_00464};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW   Rule:MF_00464};
KW   Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066, ECO:0000256|HAMAP-
KW   Rule:MF_00464};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_00464}.
FT   CHAIN           1..80
FT                   /note="S-adenosylmethionine decarboxylase beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT                   /id="PRO_5023578048"
FT   CHAIN           81..144
FT                   /note="S-adenosylmethionine decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT                   /id="PRO_5023578049"
FT   ACT_SITE        81
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT   ACT_SITE        86
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT   ACT_SITE        101
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT   SITE            80..81
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT   MOD_RES         81
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
SQ   SEQUENCE   144 AA;  16363 MW;  7C77971DE3CF8B1E CRC64;
     MEIYKKSQIL SSLSNEQKLS HQSKHLLLEL YRCDREKLND ESFLRCILNR AAKLANATIL
     NLISNKFEPH GVTAIALLAE SHISIHTWPE SNYSAVDIFT CGKNMMPELA SQYLIESLMA
     KEHSLRVIER NPPSAVSKQI RTVV
//