DCAM_SPIOL
ID DCAM_SPIOL Reviewed; 363 AA.
AC P46255;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 90.
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 Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Monatol;
RX PubMed=7770535; DOI=10.1104/pp.107.4.1461;
RA Bolle C., Herrmann R.G., Oelmueller R.;
RT "A spinach cDNA with homology to S-Adenosylmethionine decarboxylase.";
RL Plant Physiol. 107:1461-1462(1995).
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; X81414; CAA57170.1; -; mRNA.
DR PIR; S49222; S49222.
DR AlphaFoldDB; P46255; -.
DR SMR; P46255; -.
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 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; S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis;
KW Zymogen.
FT CHAIN 1..68
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030025"
FT CHAIN 69..363
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030026"
FT ACT_SITE 9
FT /evidence="ECO:0000250"
FT ACT_SITE 12
FT /evidence="ECO:0000250"
FT ACT_SITE 69
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250"
FT ACT_SITE 83
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 232
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 245
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT SITE 68..69
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000250"
FT MOD_RES 69
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 363 AA; 39960 MW; CE4D6DDE4E8A3220 CRC64;
MAISAIGFEG FEKRLEITFF EPSIFVDPEG KGLRALCKAQ LDEILGPAEC TIVDSLANES
VDSYVLSESS LFIYAYKIII KTCGTTKLLR AIPPILRLAG KLSLDVKSVR YTRGSFIFPG
AQSYAHRSFS EEVAVLDGYF GKLAAGSKAF VMGDPAKPQK WHVYSASAET ISFEEPVYTL
EMCMTGLKKE KASVFFKSQS PNAAVMTESS GIRKILPDSK ICDFDFEPCG YSMNAIEGPA
ISTIHITPED GFSYASFEAV GYDLKKTDLN QLVERVLACF EPSEFSIAIH AEIAANSMEH
NCYVNVNGYS REEGGIEELG FGAASVFYQK FCKASTGFGA TNKPKPALKC CWKEDKFEEE
KDY