ID   A0A7G2F7W5_ARATH        Unreviewed;       363 AA.
AC   A0A7G2F7W5;
DT   10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2021, sequence version 1.
DT   07-APR-2021, entry version 2.
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].
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   UniPathway; UPA00331; UER00451.
DR   Proteomes; UP000516314; Chromosome 5.
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   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|PIRNR:PIRNR001355};
KW   Lyase {ECO:0000256|PIRNR:PIRNR001355};
KW   Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115,
KW   ECO:0000256|PIRNR:PIRNR001355}; Pyruvate {ECO:0000256|PIRNR:PIRNR001355};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR001355};
KW   Schiff base {ECO:0000256|PIRNR:PIRNR001355};
KW   Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066,
KW   ECO:0000256|PIRNR:PIRNR001355}; Zymogen {ECO:0000256|PIRNR:PIRNR001355}.
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
//