DCAM1_DIACA
ID DCAM1_DIACA Reviewed; 381 AA.
AC Q39676;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme 1;
DE Short=AdoMetDC 1;
DE Short=SAMDC 1;
DE EC=4.1.1.50;
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase 1 alpha chain;
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase 1 beta chain;
DE Flags: Precursor;
GN Name=SAMDC1; Synonyms=SAMDC9;
OS Dianthus caryophyllus (Carnation) (Clove pink).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Caryophyllaceae; Caryophylleae; Dianthus.
OX NCBI_TaxID=3570;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. White Sim; TISSUE=Petal;
RA Lee M.M., Lee S.H., Park K.Y.;
RT "Nucleotide sequence of cDNAs encoding S-adenosylmethionine decarboxylase
RT from carnation flower.";
RL (er) Plant Gene Register PGR95-139(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. White Sim; TISSUE=Leaf;
RA Kim Y.J., Lee M.M., Lee S.H., Park K.Y.;
RT "Cloning and sequence analysis of genomic clone encoding S-
RT adenosylmethionine decarboxylase from carnation (Dianthus caryophyllus L.
RT cv White Sim).";
RL (er) Plant Gene Register PGR97-095(1997).
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; U38526; AAD09839.1; -; mRNA.
DR EMBL; U94786; AAB70461.1; -; Genomic_DNA.
DR PIR; T10707; T10707.
DR AlphaFoldDB; Q39676; -.
DR SMR; Q39676; -.
DR UniPathway; UPA00331; UER00451.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR016067; S-AdoMet_deCO2ase_core.
DR InterPro; IPR018166; S-AdoMet_deCO2ase_CS.
DR PANTHER; PTHR11570; PTHR11570; 1.
DR Pfam; PF01536; SAM_decarbox; 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; S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis;
KW Zymogen.
FT CHAIN 1..92
FT /note="S-adenosylmethionine decarboxylase 1 beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030003"
FT CHAIN 93..381
FT /note="S-adenosylmethionine decarboxylase 1 alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030004"
FT ACT_SITE 33
FT /evidence="ECO:0000250"
FT ACT_SITE 36
FT /evidence="ECO:0000250"
FT ACT_SITE 93
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250"
FT ACT_SITE 107
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 255
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 268
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT SITE 92..93
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000250"
FT MOD_RES 93
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 381 AA; 41416 MW; 8CAEE86CF7402FB1 CRC64;
MMVPTLGNSN YNTVSPMNGD DNNTMALSAI GFEGFEKRLE ISFFEPGIFV DPEGKGLRAL
SKAQLDEILG PAECTIVDSL ANESVDSYVL SESSLFVYSY KIIIKTCGTT KLLHSILPIL
TLADGLCLDV KSVRYTRGSF IFPGAQSYPH RSFSEEVAVL DKYFGNLGTG SKAFVMGSPA
KPQKWHVYSA TAEPSYDDPV YTLEMCMTGL DKGKASVFFK SESASAAVMT ETSGIRKILP
DSAICDFDFE PCGYSMNAIE GPAVSTIHIT PEDGFSYASF EAVGYDLKIV DVNQLVERVL
NCFQPREFSI AVSVDTADKV LEQYCAVNVA GYCREEGGVE GLGVGGSVLY QKFGKVATVS
GLNKSPKCCR KEEENDEKRE C
