DCAM_TOBAC
ID DCAM_TOBAC Reviewed; 361 AA.
AC O04009; O49005;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 98.
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 Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Samsun;
RA Paramale S.R., Ernst S.G.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Xanthi;
RA Paramale S.R., Ernst S.G.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000250};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000250};
CC -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC step 1/1.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
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DR EMBL; U91924; AAB51301.1; -; mRNA.
DR EMBL; AF033100; AAB88854.1; -; Genomic_DNA.
DR PIR; T01934; T01934.
DR RefSeq; NP_001312627.1; NM_001325698.2.
DR AlphaFoldDB; O04009; -.
DR SMR; O04009; -.
DR STRING; 4097.O04009; -.
DR GeneID; 107801519; -.
DR KEGG; nta:107801519; -.
DR UniPathway; UPA00331; UER00451.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008295; P:spermidine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006597; P:spermine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR001985; S-AdoMet_decarboxylase.
DR InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR InterPro; IPR018166; S-AdoMet_deCO2ase_CS.
DR PANTHER; PTHR11570; PTHR11570; 1.
DR Pfam; PF01536; SAM_decarbox; 1.
DR PIRSF; PIRSF001355; S-AdenosylMet_decarboxylase; 1.
DR SUPFAM; SSF56276; SSF56276; 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; Reference proteome; S-adenosyl-L-methionine; Schiff base;
KW Spermidine biosynthesis; Zymogen.
FT CHAIN 1..72
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030027"
FT CHAIN 73..361
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030028"
FT ACT_SITE 13
FT /evidence="ECO:0000250"
FT ACT_SITE 16
FT /evidence="ECO:0000250"
FT ACT_SITE 73
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250"
FT ACT_SITE 87
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 236
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 249
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT SITE 72..73
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000250"
FT MOD_RES 73
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 285
FT /note="E -> Q (in Ref. 2; AAB88854)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="V -> L (in Ref. 2; AAB88854)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 39637 MW; 119AE5D256545461 CRC64;
MDSALPVSAI GFEGFEKRLE ISFFEPGLFA DPNGKGLRSL SKAQLDEILG PAECTIVDSL
SNDDVDSYVL SESSLFVYSY KIIIKTCGTT KLLLAIPPIL KLAETLSLKV QDVRYTRGSF
IFPGAQSFPH RHFSEEVAVL DGYFGKLAAG SKAVIMGSPD KAQKWHVYSA SAGPIQSNDP
VYTLEMCMTG LDREKASVFY KTEGSSAAHM TVRSGIRKIL PNSEICDFEF EPCGYSMNSI
EGAALSTIHI TPEDGFSYAS FEAVGYDMKT MKLGPLVERV LACFEPDEFS IALHADVATK
LLERVCSVDV KGYSLAEWSP EEFGKGGSIV YQKFTRTPFC GSPKSVLKGC WKEDEEKEEK
E
