ID   Q2JWR6_SYNJA            Unreviewed;       152 AA.
AC   Q2JWR6;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 106.
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=speH {ECO:0000256|HAMAP-Rule:MF_00464};
GN   OrderedLocusNames=CYA_0574 {ECO:0000313|EMBL:ABC98790.1};
OS   Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS   A-Prime).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=321327 {ECO:0000313|EMBL:ABC98790.1, ECO:0000313|Proteomes:UP000008818};
RN   [1] {ECO:0000313|EMBL:ABC98790.1, ECO:0000313|Proteomes:UP000008818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-3-3Ab {ECO:0000313|EMBL:ABC98790.1,
RC   ECO:0000313|Proteomes:UP000008818};
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(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=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:0000256|HAMAP-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; CP000239; ABC98790.1; -; Genomic_DNA.
DR   RefSeq; WP_011429477.1; NC_007775.1.
DR   AlphaFoldDB; Q2JWR6; -.
DR   STRING; 321327.CYA_0574; -.
DR   KEGG; cya:CYA_0574; -.
DR   eggNOG; COG1586; Bacteria.
DR   HOGENOM; CLU_125470_2_0_3; -.
DR   OrthoDB; 9793120at2; -.
DR   UniPathway; UPA00331; UER00451.
DR   Proteomes; UP000008818; Chromosome.
DR   GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.160.750; -; 1.
DR   Gene3D; 3.30.360.110; S-adenosylmethionine decarboxylase domain; 1.
DR   HAMAP; MF_00464; AdoMetDC_1; 1.
DR   InterPro; IPR042286; AdoMetDC_C.
DR   InterPro; IPR003826; AdoMetDC_fam_prok.
DR   InterPro; IPR042284; AdoMetDC_N.
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   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..75
FT                   /note="S-adenosylmethionine decarboxylase beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT                   /id="PRO_5023254787"
FT   CHAIN           76..152
FT                   /note="S-adenosylmethionine decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT                   /id="PRO_5023254786"
FT   ACT_SITE        76
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT   ACT_SITE        81
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT   ACT_SITE        96
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT   SITE            75..76
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT   MOD_RES         76
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
SQ   SEQUENCE   152 AA;  16870 MW;  8A9D3D82BB8AF51A CRC64;
     MLHTLSGQLG DRSLALIGIH CILELYDCPA KLLDDVSLVQ QALREAARRS NSTLLGELCH
     PFEPQGITAL ALLGESHISI HTWPEAGYAA VDVFTCGRHT RPEAACEYLI QVFQARRYSL
     RKLPRRTTDA APIEEMADFP KALSCETAGR RR
//