ID A0A2K5I351_COLAP Unreviewed; 334 AA. AC A0A2K5I351; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 20-JUN-2018, entry version 4. DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme {ECO:0000256|PIRNR:PIRNR001355}; DE EC=4.1.1.50 {ECO:0000256|PIRNR:PIRNR001355}; GN Name=AMD1 {ECO:0000313|Ensembl:ENSCANP00000011069}; OS Colobus angolensis palliatus (Peters' Angolan colobus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Colobinae; Colobus. OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000011069, ECO:0000313|Proteomes:UP000233080}; RN [1] {ECO:0000313|Ensembl:ENSCANP00000011069, ECO:0000313|Proteomes:UP000233080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Hughes D.S., Murali S., Raveendran M., Korchina V., Bandaranaike D., RA Bellair M., Blankenburg K., Chao H., Dahdouli M., Dinh H., RA Doddapaneni H., Gnanaolivu R., Gross S., Jayaseelan J., Jones J., RA Khan Z., Kovar C., Kurapati P., Le B., Lee S., Mathew T., RA Narasimhan A., Okwuonu G., Ongeri F., Osuji N., Qu C., Quiroz J., RA Rajbhandari K., Reid J.G., Santibanez J., Skinner E., Wang Y., Xin Y., RA Han Y., Muzny D.M., Richards S., Worley K.C., Rogers J., Gibbs R.A.; RT "Black and white colobus reference genome project."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCANP00000011069} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2018) to UniProtKB. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = S-adenosyl 3- CC (methylthio)propylamine + CO(2). {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- CC adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from CC S-adenosyl-L-methionine: step 1/1. CC {ECO:0000256|PIRNR:PIRNR001355}. CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. CC {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 Ensembl; ENSCANT00000033963; ENSCANP00000011069; ENSCANG00000028929. DR GeneID; 105519438; -. DR GeneTree; ENSGT00390000011776; -. DR UniPathway; UPA00331; UER00451. DR Proteomes; UP000233080; Whole Genome Shotgun Assembly. 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 3: Inferred from homology; KW Autocatalytic cleavage {ECO:0000256|PIRSR:PIRSR001355-4}; KW Complete proteome {ECO:0000313|Proteomes:UP000233080}; KW Decarboxylase {ECO:0000256|PIRNR:PIRNR001355}; KW Lyase {ECO:0000256|PIRNR:PIRNR001355}; KW Polyamine biosynthesis {ECO:0000256|PIRNR:PIRNR001355}; KW 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|PIRNR:PIRNR001355}; KW Zymogen {ECO:0000256|PIRNR:PIRNR001355}. FT CHAIN 1 67 S-adenosylmethionine decarboxylase FT proenzyme. {ECO:0000256|PIRSR: FT PIRSR001355-5}. FT /FTId=PRO_5014496354. FT CHAIN 68 334 S-adenosylmethionine decarboxylase FT proenzyme. {ECO:0000256|PIRSR: FT PIRSR001355-5}. FT /FTId=PRO_5014496355. FT ACT_SITE 68 68 Schiff-base intermediate with substrate; FT via pyruvic acid. {ECO:0000256|PIRSR: FT PIRSR001355-1}. FT ACT_SITE 82 82 Proton donor; for catalytic activity. FT {ECO:0000256|PIRSR:PIRSR001355-1}. FT ACT_SITE 229 229 Proton acceptor; for processing activity. FT {ECO:0000256|PIRSR:PIRSR001355-1}. FT ACT_SITE 243 243 Proton acceptor; for processing activity. FT {ECO:0000256|PIRSR:PIRSR001355-1}. FT BINDING 7 7 Substrate. {ECO:0000256|PIRSR: FT PIRSR001355-2}. FT BINDING 67 67 Substrate. {ECO:0000256|PIRSR: FT PIRSR001355-2}. FT BINDING 223 223 Substrate. {ECO:0000256|PIRSR: FT PIRSR001355-2}. FT BINDING 247 247 Substrate. {ECO:0000256|PIRSR: FT PIRSR001355-2}. FT SITE 67 68 Cleavage (non-hydrolytic); by autolysis. FT {ECO:0000256|PIRSR:PIRSR001355-4}. FT MOD_RES 68 68 Pyruvic acid (Ser); by autocatalysis. FT {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 //