ID   A0A7G2F7W5_ARATH        Unreviewed;       363 AA.
AC   A0A7G2F7W5;
DT   10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2021, sequence version 1.
DT   29-MAY-2024, entry version 15.
DE   RecName: Full=S-adenosylmethionine decarboxylase proenzyme {ECO:0000256|PIRNR:PIRNR001355};
DE            EC=4.1.1.50 {ECO:0000256|PIRNR:PIRNR001355};
GN   ORFNames=AT9943_LOCUS19261 {ECO:0000313|EMBL:CAD5331815.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000313|EMBL:CAD5331815.1, ECO:0000313|Proteomes:UP000516314};
RN   [1] {ECO:0000313|EMBL:CAD5331815.1, ECO:0000313|Proteomes:UP000516314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Cdm-0 {ECO:0000313|Proteomes:UP000516314};
RA   Ashkenazy H.;
RL   Submitted (SEP-2020) 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         Evidence={ECO:0000256|ARBA:ARBA00000475,
CC         ECO:0000256|PIRNR:PIRNR001355};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001355};
CC       Note=Binds 1 pyruvoyl group covalently per subunit.
CC       {ECO:0000256|PIRNR:PIRNR001355};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC       biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC       step 1/1. {ECO:0000256|ARBA:ARBA00004911,
CC       ECO:0000256|PIRNR:PIRNR001355}.
CC   -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family.
CC       {ECO:0000256|ARBA:ARBA00008466, ECO:0000256|PIRNR:PIRNR001355}.
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DR   EMBL; LR881470; CAD5331815.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7G2F7W5; -.
DR   UniPathway; UPA00331; UER00451.
DR   Proteomes; UP000516314; Chromosome 5.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006597; P:spermine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.360.50; S-adenosylmethionine decarboxylase; 1.
DR   Gene3D; 3.60.90.10; S-adenosylmethionine decarboxylase; 1.
DR   InterPro; IPR048283; AdoMetDC-like.
DR   InterPro; IPR001985; S-AdoMet_decarboxylase_euk.
DR   InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR   InterPro; IPR018166; S-AdoMet_deCO2ase_CS.
DR   NCBIfam; TIGR00535; SAM_DCase; 1.
DR   PANTHER; PTHR11570; S-ADENOSYLMETHIONINE DECARBOXYLASE; 1.
DR   PANTHER; PTHR11570:SF15; S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME 2; 1.
DR   Pfam; PF01536; SAM_decarbox; 1.
DR   PIRSF; PIRSF001355; S-AdenosylMet_decarboxylase; 1.
DR   SUPFAM; SSF56276; S-adenosylmethionine decarboxylase; 1.
DR   PROSITE; PS01336; ADOMETDC; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage {ECO:0000256|PIRSR:PIRSR001355-4};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793,
KW   ECO:0000256|PIRNR:PIRNR001355};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001355};
KW   Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115,
KW   ECO:0000256|PIRNR:PIRNR001355};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|PIRNR:PIRNR001355};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR001355};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|PIRNR:PIRNR001355};
KW   Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066,
KW   ECO:0000256|PIRNR:PIRNR001355};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|PIRNR:PIRNR001355}.
FT   CHAIN           1..68
FT                   /note="S-adenosylmethionine decarboxylase beta chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-5"
FT                   /id="PRO_5036528689"
FT   CHAIN           69..363
FT                   /note="S-adenosylmethionine decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-5"
FT                   /id="PRO_5036528688"
FT   ACT_SITE        69
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-1"
FT   ACT_SITE        83
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-1"
FT   ACT_SITE        232
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-1"
FT   ACT_SITE        245
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-1"
FT   BINDING         8
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-2"
FT   BINDING         68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-2"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-2"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-2"
FT   SITE            68..69
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-4"
FT   MOD_RES         69
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-3"
SQ   SEQUENCE   363 AA;  40174 MW;  59E0B15E66D38749 CRC64;
     MAMSAIGFEG YEKRLEVTFF EPGLFLDTQG KGLRALAKSQ IDEILQPAEC TIVSSLSNDQ
     LDSYVLSESS LFIFPYKIVI KTCGTTKLLL SIEPLLRLAG ELSLDVKAVR YTRGSFLCPG
     GQPFPHRNFS EEVSVLDGHF AKLGLSSVAY LMGNDDETKK WHVYSASSAN SNNKNNVYTL
     EMCMTGLDKD KASVFYKNES SSAGSMTDNS GIRKILPQSQ ICDFEFEPCG YSMNSIEGDA
     ISTIHVTPED GFSYASFEAV GYDFTTMDLS HLVSKVLTCF EPKQFSVAVH STVAQKSYDS
     GLSVDLDDYG CKESTMESLG EERGTVMYQR FEKLGRYYCG SPRSTLKCEW SSNSSCNSED
     EKE
//