ID   SPED_XANOM              Reviewed;         264 AA.
AC   Q2NYE0;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=XOO3932;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests
RT   contribution of large numbers of effector genes and insertion
RT   sequences to its race diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
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; AP008229; BAE70687.1; -; Genomic_DNA.
DR   RefSeq; YP_452961.1; -.
DR   GeneID; 3858772; -.
DR   GenomeReviews; AP008229_GR; XOO3932.
DR   KEGG; xom:XOO_3932; -.
DR   HOGENOM; Q2NYE0; -.
DR   OMA; Q2NYE0; YNAERLT.
DR   BioCyc; XORY342109:XOO3932-MON; -.
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    112       S-adenosylmethionine decarboxylase beta
FT                                chain (By similarity).
FT                                /FTId=PRO_0000273621.
FT   CHAIN       113    264       S-adenosylmethionine decarboxylase alpha
FT                                chain (By similarity).
FT                                /FTId=PRO_0000273622.
FT   ACT_SITE    113    113       Schiff-base intermediate with substrate;
FT                                via pyruvic acid (By similarity).
FT   ACT_SITE    118    118       Proton acceptor; for processing activity
FT                                (By similarity).
FT   ACT_SITE    141    141       Proton donor; for catalytic activity (By
FT                                similarity).
FT   SITE        112    113       Cleavage (non-hydrolytic); by autolysis
FT                                (By similarity).
FT   MOD_RES     113    113       Pyruvic acid (Ser); by autocatalysis (By
FT                                similarity).
SQ   SEQUENCE   264 AA;  30823 MW;  0BF355BDD6B50E5C CRC64;
     MVKPLPRLRL QGFNNLTKAL SFNIYDVCYA RTEEERQRYI EYIDEQYDAD RLTQILTDVA
     EIIGANILNI ARQDYDPQGA SVTILISEEP VIDKKQAGRE LISDAVVAHM DKSHITVHTY
     PETHPQEGIA TFRADIDVAT CGVISPLKAL NYLIETLESD IVIMDYRVRG FTRDVKGKKH
     YIDHKINSIQ HFLAKNVKSR YEMIDVNVYQ ENIFHTKMHL KDFDLDQYLF EERAKNLSFK
     ERMKIETLLK REIEELFHGR NLSE
//