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SPEH_BREBN
ID   SPEH_BREBN              Reviewed;         133 AA.
AC   C0ZGF5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=S-adenosylmethionine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_00464};
DE            Short=AdoMetDC {ECO:0000255|HAMAP-Rule:MF_00464};
DE            Short=SAMDC {ECO:0000255|HAMAP-Rule:MF_00464};
DE            EC=4.1.1.50 {ECO:0000255|HAMAP-Rule:MF_00464};
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00464};
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00464};
DE   Flags: Precursor;
GN   Name=speH {ECO:0000255|HAMAP-Rule:MF_00464}; OrderedLocusNames=BBR47_38870;
OS   Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=358681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47 / JCM 6285 / NBRC 100599;
RA   Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA   Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA   Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA   Udaka S., Tanikawa S., Fujita N.;
RT   "Brevibacillus brevis strain 47, complete genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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:0000255|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:0000255|HAMAP-Rule:MF_00464};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00464};
CC       Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00464}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC       dimer of alpha/beta heterodimers. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00464}.
CC   -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00464}.
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DR   EMBL; AP008955; BAH44864.1; -; Genomic_DNA.
DR   RefSeq; WP_007723244.1; NC_012491.1.
DR   AlphaFoldDB; C0ZGF5; -.
DR   SMR; C0ZGF5; -.
DR   STRING; 358681.BBR47_38870; -.
DR   EnsemblBacteria; BAH44864; BAH44864; BBR47_38870.
DR   GeneID; 61032286; -.
DR   KEGG; bbe:BBR47_38870; -.
DR   eggNOG; COG1586; Bacteria.
DR   HOGENOM; CLU_125470_2_3_9; -.
DR   OMA; VYTCGEH; -.
DR   OrthoDB; 1613081at2; -.
DR   UniPathway; UPA00331; UER00451.
DR   Proteomes; UP000001877; Chromosome.
DR   GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; 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; -; 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   PANTHER; PTHR33866; PTHR33866; 1.
DR   Pfam; PF02675; AdoMet_dc; 1.
DR   SUPFAM; SSF56276; SSF56276; 1.
DR   TIGRFAMs; TIGR03330; SAM_DCase_Bsu; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis;
KW   Pyruvate; Reference proteome; S-adenosyl-L-methionine; Schiff base;
KW   Spermidine biosynthesis; Zymogen.
FT   CHAIN           1..64
FT                   /note="S-adenosylmethionine decarboxylase beta chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT                   /id="PRO_1000193173"
FT   CHAIN           65..133
FT                   /note="S-adenosylmethionine decarboxylase alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT                   /id="PRO_1000193174"
FT   ACT_SITE        65
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT   ACT_SITE        70
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT   ACT_SITE        85
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT   SITE            64..65
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT   MOD_RES         65
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
SQ   SEQUENCE   133 AA;  14638 MW;  1D4F51FEF7B07A82 CRC64;
     MEYSTFGRHV AVDTWGVQFD LLNDAEFLKK EMIEAAEACG ATVLSVQAKQ FSPQGATVLV
     LLSESHLSIH TYPERGFAAL DCYTCGETVD PQIAIDYLVS VLKPEKTYAK KLVRGLGELQ
     VVEPEMKLVE AAK
 
 
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