ID   SPED_SODGM              Reviewed;         264 AA.
AC   Q2NVS2;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=SG0478;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K.,
RA   Hattori M., Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights
RT   into the symbiotic lifestyle of Sodalis glossinidius in the tsetse
RT   host.";
RL   Genome Res. 16:149-156(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; AP008232; BAE73753.1; -; Genomic_DNA.
DR   RefSeq; YP_454158.1; -.
DR   GeneID; 3868692; -.
DR   GenomeReviews; AP008232_GR; SG0478.
DR   KEGG; sgl:SG0478; -.
DR   NMPDR; fig|343509.6.peg.1081; -.
DR   HOGENOM; Q2NVS2; -.
DR   OMA; Q2NVS2; YNAERLT.
DR   BioCyc; SGLO343509:SG0478-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    111       S-adenosylmethionine decarboxylase beta
FT                                chain (By similarity).
FT                                /FTId=PRO_0000273615.
FT   CHAIN       112    264       S-adenosylmethionine decarboxylase alpha
FT                                chain (By similarity).
FT                                /FTId=PRO_0000273616.
FT   ACT_SITE    112    112       Schiff-base intermediate with substrate;
FT                                via pyruvic acid (By similarity).
FT   ACT_SITE    117    117       Proton acceptor; for processing activity
FT                                (By similarity).
FT   ACT_SITE    140    140       Proton donor; for catalytic activity (By
FT                                similarity).
FT   SITE        111    112       Cleavage (non-hydrolytic); by autolysis
FT                                (By similarity).
FT   MOD_RES     112    112       Pyruvic acid (Ser); by autocatalysis (By
FT                                similarity).
SQ   SEQUENCE   264 AA;  30250 MW;  1F5D8F8E95E7365B CRC64;
     MQKLKLHGFN NLTKSLSFCI YDICYAKTAD DRDGYITYID EQYNANRLTE ILSETCSMIG
     ANILNIARQD YEPQGASVTI LVSEEPVDPG SIDTSEHPGP LPESVVAHLD KSHICVHTYP
     ESHPEGGLCT FRADIEVSTC GVISPLKALN YLIHQLESDI VTMDYRVRGF TRDINGVKHY
     IDHEINSIQN FMSKDMKALY HMMDVNVYQE NIFHTKIMLK DFDLKHYLFN ARPDDLSAEE
     RKAITDLLYK EMQEIYYGRN LPVL
//