ID   DCAM_ONCVO              Reviewed;         365 AA.
AC   Q27883;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=smd-1; Synonyms=samdc;
OS   Onchocerca volvulus.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=6282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE, AND
RP   PYRUVATE FORMATION AT SER-87.
RX   PubMed=8973561; DOI=10.1042/bj3200519;
RA   Da'Dara A.A., Henkle-Duehrsen K., Walter R.D.;
RT   "A novel trans-spliced mRNA from Onchocerca volvulus encodes a functional
RT   S-adenosylmethionine decarboxylase.";
RL   Biochem. J. 320:519-530(1996).
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;
CC       Note=Binds 1 pyruvoyl group covalently per subunit.;
CC   -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC       biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC       step 1/1.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
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; X95714; CAA65018.1; -; Genomic_DNA.
DR   EMBL; X95713; CAA65017.1; -; mRNA.
DR   AlphaFoldDB; Q27883; -.
DR   SMR; Q27883; -.
DR   STRING; 6282.Q27883; -.
DR   HOGENOM; CLU_023050_1_0_1; -.
DR   UniPathway; UPA00331; UER00451.
DR   Proteomes; UP000024404; Unassembled WGS sequence.
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   1: Evidence at protein level;
KW   Autocatalytic cleavage; Decarboxylase; Direct protein sequencing; Lyase;
KW   Polyamine biosynthesis; Pyruvate; Reference proteome;
KW   S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis; Zymogen.
FT   CHAIN           1..86
FT                   /note="S-adenosylmethionine decarboxylase beta chain"
FT                   /id="PRO_0000029977"
FT   CHAIN           87..365
FT                   /note="S-adenosylmethionine decarboxylase alpha chain"
FT                   /id="PRO_0000029978"
FT   ACT_SITE        31
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        34
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        87
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        101
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        248
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        263
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000250"
FT   SITE            86..87
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT   MOD_RES         87
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:8973561"
SQ   SEQUENCE   365 AA;  41893 MW;  F8615CE029BA40B8 CRC64;
     MSTSTLSDGS LDEGTFAAED VSGVIEDYFF EGAEKLLEIW FDKNQNGATS LRNIPYSELV
     SMLDIAQCRI LHSKSNECMD SYVLSESSMF ISDFRIILKT CGTTRLLHAI ERILHIAKIY
     CNMDNVVSVF YSRKNFMHPE KQPYPHSSFE TEVDYLEEHF AGGSAYCIGP QRQDRWFLYT
     MVTPQAVFPF PEHTLEILMN GLPEDVLSTF SPNVSKDGKD CRMKSAINTI LPPDIVVHEE
     LFSPCGYSLN GLIPHSDHYI TIHVTPEPDF SYVSFETNQH TLNLCEQMLK VLEIFKPSKF
     LLTIFTNELS NEGKKMQKNL WDLKICGCRR TNLQFLELPT ETLIYVQFER IKSAEQVTCK
     EVFDR