ID   SPED_CLOP1              Reviewed;         271 AA.
AC   Q0TTQ9;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=S-adenosylmethionine decarboxylase proenzyme;
DE            Short=AdoMetDC;
DE            Short=SAMDC;
DE            EC=4.1.1.50;
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase beta chain;
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase alpha chain;
DE   Flags: Precursor;
GN   Name=speD; OrderedLocusNames=CPF_0527;
OS   Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R.,
RA   DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C.,
RA   Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J.,
RA   Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S.,
RA   Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H.,
RA   Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I.,
RA   Melville S.B., Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial
RT   pathogen, Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
CC   -!- FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to
CC       S-adenosylmethioninamine (dcAdoMet), the propylamine donor
CC       required for the synthesis of the polyamines spermine and
CC       spermidine from the diamine putrescine (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = (5-deoxy-5-
CC       adenosyl)(3-aminopropyl)-methylsulfonium salt + CO(2).
CC   -!- COFACTOR: Pyruvoyl group (By similarity).
CC   -!- PATHWAY: Amine and polyamine biosynthesis; S-
CC       adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from
CC       S-adenosyl-L-methionine: step 1/1.
CC   -!- SUBUNIT: Heterooctamer of four alpha and four beta chains arranged
CC       as a tetramer of alpha/beta heterodimers (By similarity).
CC   -!- PTM: Is synthesized initially as an inactive proenzyme. Formation
CC       of the active enzyme involves a self-maturation process in which
CC       the active site pyruvoyl group is generated from an internal
CC       serine residue via an autocatalytic post-translational
CC       modification. Two non-identical subunits are generated from the
CC       proenzyme in this reaction, and the pyruvate is formed at the N-
CC       terminus of the alpha chain, which is derived from the carboxyl
CC       end of the proenzyme. The post-translation cleavage follows an
CC       unusual pathway, termed non-hydrolytic serinolysis, in which the
CC       side chain hydroxyl group of the serine supplies its oxygen atom
CC       to form the C-terminus of the beta chain, while the remainder of
CC       the serine residue undergoes an oxidative deamination to produce
CC       ammonia and the pyruvoyl group blocking the N-terminus of the
CC       alpha chain (By similarity).
CC   -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 2
CC       subfamily.
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DR   EMBL; CP000246; ABG84466.1; -; Genomic_DNA.
DR   RefSeq; YP_694981.1; -.
DR   GeneID; 4203924; -.
DR   GenomeReviews; CP000246_GR; CPF_0527.
DR   KEGG; cpf:CPF_0527; -.
DR   TIGR; CPF_0527; -.
DR   HOGENOM; Q0TTQ9; -.
DR   OMA; Q0TTQ9; YNAERLT.
DR   GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:HAMAP.
DR   GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00465; -; 1.
DR   InterPro; IPR003826; S-AdoMet_decarboxylase-bac/arc.
DR   InterPro; IPR009165; S-AdoMet_deCO2ase_bac.
DR   InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR   Gene3D; G3DSA:3.60.90.10; SAM_decarbox; 1.
DR   Pfam; PF02675; AdoMet_dc; 1.
DR   PIRSF; PIRSF001356; SAM_decarboxylas; 1.
DR   TIGRFAMs; TIGR03331; SAM_DCase_Eco; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Complete proteome; Decarboxylase; Lyase;
KW   Polyamine biosynthesis; Pyruvate; S-adenosyl-L-methionine;
KW   Schiff base; Spermidine biosynthesis; Zymogen.
FT   CHAIN         1    120       S-adenosylmethionine decarboxylase beta
FT                                chain (By similarity).
FT                                /FTId=PRO_0000273591.
FT   CHAIN       121    271       S-adenosylmethionine decarboxylase alpha
FT                                chain (By similarity).
FT                                /FTId=PRO_0000273592.
FT   ACT_SITE    121    121       Schiff-base intermediate with substrate;
FT                                via pyruvic acid (By similarity).
FT   ACT_SITE    126    126       Proton acceptor; for processing activity
FT                                (By similarity).
FT   ACT_SITE    149    149       Proton donor; for catalytic activity (By
FT                                similarity).
FT   SITE        120    121       Cleavage (non-hydrolytic); by autolysis
FT                                (By similarity).
FT   MOD_RES     121    121       Pyruvic acid (Ser); by autocatalysis (By
FT                                similarity).
SQ   SEQUENCE   271 AA;  31322 MW;  FE4EE5EF75E778A8 CRC64;
     MLGLKEKICL YGFNNLTKTL SFNIYDICYA KTEREKEDYI KYIDEQYNSE RLTKILCDVT
     EMIGAHVLNI SKQDYEPQGA SVNVLITEEA LPVALIDPSC NKGELSYLEL RDSVVGHLDK
     SHLTVHTYPE FHPNNDIISF RVDIDVSTCG KISPLNALDY LIGSFDSDVI TIDYRVRGFT
     RDVDGRKCYI DHDIKSIQDY IDGETLKKYD AMDVNVYQSN IFHTKMMLKD IVLNNYLFNS
     DPYELSPNDR REIRDRISKE MIEIYGGVNI Y
//