ID   DCAM_HORCH              Reviewed;         393 AA.
AC   Q42829;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 54.
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 alpha chain;
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase beta chain;
DE   Flags: Precursor;
GN   Name=SAMDC;
OS   Hordeum chilense (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Pooideae; Triticeae; Hordeum.
OX   NCBI_TaxID=15565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   MEDLINE=96270379; PubMed=8639739; DOI=10.1007/BF00020812;
RA   Dresselhaus T., Barcelo P., Hagel C., Loerz H., Humbeck K.;
RT   "Isolation and characterization of a Tritordeum cDNA encoding S-
RT   adenosylmethionine decarboxylase that is circadian-clock-regulated.";
RL   Plant Mol. Biol. 30:1021-1033(1996).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = (5-deoxy-5-
CC       adenosyl)(3-aminopropyl)-methylsulfonium salt + CO(2).
CC   -!- COFACTOR: Pyruvoyl group.
CC   -!- PATHWAY: Amine and polyamine biosynthesis; S-
CC       adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from
CC       S-adenosyl-L-methionine: step 1/1.
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 eukaryotic AdoMetDC family.
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DR   EMBL; X83881; CAA58762.1; -; mRNA.
DR   PIR; S69191; S69191.
DR   HSSP; P17707; 1JEN.
DR   Gramene; Q42829; -.
DR   BRENDA; 4.1.1.50; 293551.
DR   GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:EC.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006597; P:spermine biosynthetic process; IEA:InterPro.
DR   InterPro; IPR001985; S-AdoMet_decarboxylase.
DR   InterPro; IPR018167; S-AdoMet_decarboxylase_sg.
DR   InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR   InterPro; IPR018166; S-AdoMet_deCO2ase_CS.
DR   Gene3D; G3DSA:3.60.90.10; SAM_decarbox; 1.
DR   PANTHER; PTHR11570; SAM_decarbox; 1.
DR   Pfam; PF01536; SAM_decarbox; 1.
DR   PIRSF; PIRSF001355; S-AdenosylMet_decarboxylase; 1.
DR   ProDom; PD002379; SAM_decarbox; 1.
DR   TIGRFAMs; TIGR00535; SAM_DCase; 1.
DR   PROSITE; PS01336; ADOMETDC; 1.
PE   2: Evidence at transcript level;
KW   Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis;
KW   Pyruvate; S-adenosyl-L-methionine; Schiff base;
KW   Spermidine biosynthesis; Zymogen.
FT   CHAIN         1     70       S-adenosylmethionine decarboxylase beta
FT                                chain (By similarity).
FT                                /FTId=PRO_0000030009.
FT   CHAIN        71    393       S-adenosylmethionine decarboxylase alpha
FT                                chain (By similarity).
FT                                /FTId=PRO_0000030010.
FT   ACT_SITE     11     11       By similarity.
FT   ACT_SITE     14     14       By similarity.
FT   ACT_SITE     71     71       Schiff-base intermediate with substrate;
FT                                via pyruvic acid (By similarity).
FT   ACT_SITE     85     85       Proton donor; for catalytic activity (By
FT                                similarity).
FT   ACT_SITE    236    236       Proton acceptor; for processing activity
FT                                (By similarity).
FT   ACT_SITE    249    249       Proton acceptor; for processing activity
FT                                (By similarity).
FT   SITE         70     71       Cleavage (non-hydrolytic); by autolysis
FT                                (By similarity).
FT   MOD_RES      71     71       Pyruvic acid (Ser); by autocatalysis (By
FT                                similarity).
SQ   SEQUENCE   393 AA;  42896 MW;  6CD1AA94792AF6CB CRC64;
     MAAPVSAIGF EGYEKRLEIT FSEASIFADP HGRGLRALSR AQIDSVLDLA RCTIVSELSN
     KDFDSYVLSE SSLFIYSQKI VIKTCGTTML LLTIPRILEL AEELCMPLAA VKYSRGMFIF
     PGAQPAPHRS FSEEVDVLNR YFGHLNSGGN AYVIGDPAKP GQKWHIYYAT EQPEQPMVTL
     EMCMTGLDKT KASVFFKTHA DGHVSCAKEM TKLSGISDII PEMEVCDFDF EPCGYSMNAI
     NGSAFSTIHV TPEDGFSYAS YEVQGMDASA LAYGDIVKRV LRCFGPSEFS VAVTIFGGRG
     HAATWGKKLD AEAYDCNNVV EQELPCGGVL IYQSFAANEE LAVSAGSPRS VFHCFENVES
     GHPLVKEGKL ANLLAWRAEE ESLEEGTGAL LCE
//