ID   A8FG39_BACP2            Unreviewed;       126 AA.
AC   A8FG39;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 2.
DT   02-SEP-2026, entry version 102.
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=BPUM_2546 {ECO:0000313|EMBL:ABV63206.2};
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV63206.2, ECO:0000313|Proteomes:UP000001355};
RN   [1] {ECO:0000313|EMBL:ABV63206.2, ECO:0000313|Proteomes:UP000001355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV63206.2,
RC   ECO:0000313|Proteomes:UP000001355};
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
RN   [2] {ECO:0000313|EMBL:ABV63206.2, ECO:0000313|Proteomes:UP000001355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV63206.2,
RC   ECO:0000313|Proteomes:UP000001355};
RX   PubMed=23812891; DOI=10.1007/s00792-013-0559-z;
RA   Tirumalai M.R., Fox G.E.;
RT   "An ICEBs1-like element may be associated with the extreme radiation and
RT   desiccation resistance of Bacillus pumilus SAFR-032 spores.";
RL   Extremophiles 17:767-774(2013).
RN   [3] {ECO:0000313|EMBL:ABV63206.2, ECO:0000313|Proteomes:UP000001355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV63206.2,
RC   ECO:0000313|Proteomes:UP000001355};
RX   PubMed=23799069;
RA   Tirumalai M.R., Rastogi R., Zamani N., O'Bryant Williams E., Allen S.,
RA   Diouf F., Kwende S., Weinstock G.M., Venkateswaran K.J., Fox G.E.;
RT   "Candidate genes that may be responsible for the unusual resistances
RT   exhibited by Bacillus pumilus SAFR-032 spores.";
RL   PLoS ONE 8:E66012-E66012(2013).
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|ARBA:ARBA00056215, ECO:0000256|HAMAP-
CC       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;
CC         Evidence={ECO:0000256|ARBA:ARBA00048112, 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|ARBA:ARBA00004911, ECO:0000256|HAMAP-
CC       Rule:MF_00464}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC       dimer of alpha/beta heterodimers. {ECO:0000256|ARBA:ARBA00011601,
CC       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|ARBA:ARBA00061583, ECO:0000256|HAMAP-
CC       Rule:MF_00464}.
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DR   EMBL; CP000813; ABV63206.2; -; Genomic_DNA.
DR   RefSeq; WP_041815828.1; NC_009848.4.
DR   AlphaFoldDB; A8FG39; -.
DR   STRING; 315750.BPUM_2546; -.
DR   PaxDb; 315750-BPUM_2546; -.
DR   GeneID; 5621811; -.
DR   KEGG; bpu:BPUM_2546; -.
DR   eggNOG; COG1586; Bacteria.
DR   OrthoDB; 9793120at2; -.
DR   UniPathway; UPA00331; UER00451.
DR   Proteomes; UP000001355; 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   FunFam; 3.30.160.750:FF:000001; S-adenosylmethionine decarboxylase proenzyme; 1.
DR   FunFam; 3.30.360.110:FF:000001; S-adenosylmethionine decarboxylase proenzyme; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000001355};
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..62
FT                   /note="S-adenosylmethionine decarboxylase beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT                   /id="PRO_5023521266"
FT   CHAIN           63..126
FT                   /note="S-adenosylmethionine decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT                   /id="PRO_5023521265"
FT   ACT_SITE        63
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT   ACT_SITE        68
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT   ACT_SITE        83
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT   SITE            62..63
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT   MOD_RES         63
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
SQ   SEQUENCE   126 AA;  13749 MW;  DE8DCE78FCF9AD58 CRC64;
     METIGRHVIS ELWGCDCDKL NDMDFIEKTF VNAALKSGAE VREVAFHKFA PQGVSGVVII
     SESHLTIHSF PEHGYASIDV YTCGDLDPNI AADHIGDELG AETRENIEIP RGMGPVQVKQ
     AQVKAL
//