DCAM_MAIZE
ID DCAM_MAIZE Reviewed; 400 AA.
AC O24575;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
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 Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Michael A.J.;
RL Submitted (SEP-1996) 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; Y07767; CAA69075.1; -; mRNA.
DR PIR; T03947; T03947.
DR RefSeq; NP_001105713.1; NM_001112243.2.
DR AlphaFoldDB; O24575; -.
DR SMR; O24575; -.
DR STRING; 4577.GRMZM2G154397_P01; -.
DR PaxDb; O24575; -.
DR PRIDE; O24575; -.
DR EnsemblPlants; Zm00001eb078440_T001; Zm00001eb078440_P001; Zm00001eb078440.
DR EnsemblPlants; Zm00001eb078440_T002; Zm00001eb078440_P002; Zm00001eb078440.
DR GeneID; 542733; -.
DR Gramene; Zm00001eb078440_T001; Zm00001eb078440_P001; Zm00001eb078440.
DR Gramene; Zm00001eb078440_T002; Zm00001eb078440_P002; Zm00001eb078440.
DR KEGG; zma:542733; -.
DR eggNOG; KOG0788; Eukaryota.
DR HOGENOM; CLU_023050_2_0_1; -.
DR OMA; WANELHV; -.
DR OrthoDB; 932490at2759; -.
DR UniPathway; UPA00331; UER00451.
DR Proteomes; UP000007305; Chromosome 2.
DR ExpressionAtlas; O24575; baseline and differential.
DR Genevisible; O24575; ZM.
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..77
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030013"
FT CHAIN 78..400
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030014"
FT ACT_SITE 18
FT /evidence="ECO:0000250"
FT ACT_SITE 21
FT /evidence="ECO:0000250"
FT ACT_SITE 78
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250"
FT ACT_SITE 92
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 243
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 256
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT SITE 77..78
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000250"
FT MOD_RES 78
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 400 AA; 43516 MW; 1B2445775F55714A CRC64;
MAVLSAADAS PVSAIGFEGY EKRLEITFSE APVFVDPHGR GLRALSRAQI DSVLDLARCT
IVSELSNKDF DSYVLSESSL FIYPLKIVIK TCGTTKLLLT IPRILELAEE LSMPLAAVKY
SRGTFIFPGA QPAPHRSFSE EVAALNRYFG GLKSGGNAYV IGDPARPGQK WHVFYATEYP
EQPMVNLEMC MTGLDKKKAC VFFKTNADGN TTCAKEMTKL SGISEIIPEM EICDFDFEPC
GYSMNAIHGS AFSTIHVTPE DGFSYASYEV MGLDATALSY GDLVKRVLRC FGPSEFSVAV
TIFGGRGHAG TWGKALGAEV YDCNNMVEQE LPGGGLLVYQ SFCAAEDAVA TSPKSVFHCF
DGENVESAPP PMKKDYKLAN LLCWEEEADA MEEKAGVLDE
