ID W4F3D0_9BACL Unreviewed; 143 AA.
AC W4F3D0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 ORFNames=C176_07502 {ECO:0000313|EMBL:ETT86541.1};
OS Viridibacillus arenosi FSL R5-213.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Viridibacillus.
OX NCBI_TaxID=1227360 {ECO:0000313|EMBL:ETT86541.1, ECO:0000313|Proteomes:UP000019062};
RN [1] {ECO:0000313|EMBL:ETT86541.1, ECO:0000313|Proteomes:UP000019062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-213 {ECO:0000313|EMBL:ETT86541.1,
RC ECO:0000313|Proteomes:UP000019062};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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;
CC Evidence={ECO:0000256|HAMAP-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETT86541.1}.
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DR EMBL; ASQA01000013; ETT86541.1; -; Genomic_DNA.
DR AlphaFoldDB; W4F3D0; -.
DR PATRIC; fig|1227360.4.peg.1527; -.
DR eggNOG; COG1586; Bacteria.
DR UniPathway; UPA00331; UER00451.
DR Proteomes; UP000019062; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000019062};
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..66
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT /id="PRO_5023318803"
FT CHAIN 67..143
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT /id="PRO_5023318804"
FT ACT_SITE 67
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT ACT_SITE 72
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT ACT_SITE 87
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT SITE 66..67
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT MOD_RES 67
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
SQ SEQUENCE 143 AA; 16068 MW; D94292768A7E6C87 CRC64;
MGIELSTLGR HVLIEFYGCP SEVIENNALI ERFMNEAADY SGATIVESVF HHFNPYGVSG
AVIIEESHLT IHTWPEYGFA SVDVYTCGDS VNPWKAADYL SEKLHATKTE SFEIPRGMAD
KIRQFAEQEI DQIKVKIELE GVK
//