ID   A0A2K5I351_COLAP        Unreviewed;       334 AA.
AC   A0A2K5I351;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   12-OCT-2022, entry version 20.
DE   RecName: Full=S-adenosylmethionine decarboxylase proenzyme {ECO:0000256|PIRNR:PIRNR001355};
DE            EC=4.1.1.50 {ECO:0000256|PIRNR:PIRNR001355};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000011069, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000011069}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2018) to UniProtKB.
CC   -!- FUNCTION: Essential for biosynthesis of the polyamines spermidine and
CC       spermine. Promotes maintenance and self-renewal of embryonic stem
CC       cells, by maintaining spermine levels. {ECO:0000256|ARBA:ARBA00002587}.
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|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   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC       {ECO:0000256|ARBA:ARBA00011475}.
CC   -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family.
CC       {ECO:0000256|ARBA:ARBA00008466, ECO:0000256|PIRNR:PIRNR001355}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_011808173.1; XM_011952783.1.
DR   STRING; 336983.ENSCANP00000011069; -.
DR   Ensembl; ENSCANT00000033963.1; ENSCANP00000011069.1; ENSCANG00000028929.1.
DR   GeneID; 105519438; -.
DR   CTD; 262; -.
DR   OMA; LEIWFEE; -.
DR   OrthoDB; 932490at2759; -.
DR   UniPathway; UPA00331; UER00451.
DR   Proteomes; UP000233080; Unplaced.
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   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   Autocatalytic cleavage {ECO:0000256|PIRSR:PIRSR001355-4};
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   Reference proteome {ECO:0000313|Proteomes:UP000233080};
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}.
FT   CHAIN           1..67
FT                   /note="S-adenosylmethionine decarboxylase beta chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-5"
FT                   /id="PRO_5035506886"
FT   CHAIN           68..334
FT                   /note="S-adenosylmethionine decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-5"
FT                   /id="PRO_5035506885"
FT   ACT_SITE        68
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-1"
FT   ACT_SITE        82
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-1"
FT   ACT_SITE        229
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-1"
FT   ACT_SITE        243
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-1"
FT   BINDING         7
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-2"
FT   BINDING         67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-2"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-2"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-2"
FT   SITE            67..68
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-4"
FT   MOD_RES         68
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001355-3"
SQ   SEQUENCE   334 AA;  38320 MW;  4EB4765AF98E21BE CRC64;
     MEAAHFFEGT EKLLEVWFSR QQPEANQGSG DLRTIPRSEW DILLKDVQCS IISVTKTDKQ
     EAYVLSESSM FVSKRRFILK TCGTTLLLKA LVPLLKLARD YSGFDSIQSF FYSRKNFMKP
     SHQGYPHRNF QEEIEFLNAI FPNGAAYCMG RMNSDCWYLY TLDFPESRVI SQPDQTLEIL
     MSELDPAVMD QFYMKDGVTA KDVTRESGIR DLIPGSVIDA TMFNPCGYSM NGMKSDGTYW
     TIHITPEPEF SYVSFETNLS QTSYDDLIRK VVEVFKPGKF VTTLFVNQSS KCRTVLASPQ
     KIEGFKRLDC QSAMFNDYNF VLTSFAKKQQ QQQS
//