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SPEH_SULSY
ID   SPEH_SULSY              Reviewed;         133 AA.
AC   B2V7P6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
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};
GN   OrderedLocusNames=SYO3AOP1_0324;
OS   Sulfurihydrogenibium sp. (strain YO3AOP1).
OC   Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Sulfurihydrogenibium; unclassified Sulfurihydrogenibium.
OX   NCBI_TaxID=436114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YO3AOP1;
RX   PubMed=19136599; DOI=10.1128/jb.01645-08;
RA   Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
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; CP001080; ACD65969.1; -; Genomic_DNA.
DR   RefSeq; WP_007545558.1; NC_010730.1.
DR   AlphaFoldDB; B2V7P6; -.
DR   SMR; B2V7P6; -.
DR   STRING; 436114.SYO3AOP1_0324; -.
DR   EnsemblBacteria; ACD65969; ACD65969; SYO3AOP1_0324.
DR   KEGG; sul:SYO3AOP1_0324; -.
DR   eggNOG; COG1586; Bacteria.
DR   HOGENOM; CLU_125470_2_3_0; -.
DR   OMA; HTWPEKG; -.
DR   OrthoDB; 1613081at2; -.
DR   UniPathway; UPA00331; UER00451.
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   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   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; S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis;
KW   Zymogen.
FT   CHAIN           1..63
FT                   /note="S-adenosylmethionine decarboxylase beta chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT                   /id="PRO_1000125461"
FT   CHAIN           64..133
FT                   /note="S-adenosylmethionine decarboxylase alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT                   /id="PRO_1000125462"
FT   ACT_SITE        64
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT   ACT_SITE        69
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT   ACT_SITE        84
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT   SITE            63..64
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
FT   MOD_RES         64
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00464"
SQ   SEQUENCE   133 AA;  14893 MW;  D5F060AD901F6851 CRC64;
     MEKTLGLHIL ADLYGVDFEK IDHVEDVKAL LEGAVKYANL SKLSSHFHQF NPHGATGVIL
     LEESHISIHT WPEHGYAAID VYTCGGKEKT FKAMEYIIKT LKPKRIDEKI AERGVVPVNP
     EGVNIEKMQL AQV
 
 
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