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 //