ID   A0A2K5I351_COLAP        Unreviewed;       334 AA.
AC   A0A2K5I351;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   16-JAN-2019, entry version 7.
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:
CC       Reaction=H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-
CC         (methylsulfanyl)propylamine; Xref=Rhea:RHEA:15981,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57443,
CC         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-
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}.
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DR   RefSeq; XP_011808173.1; XM_011952783.1.
DR   Ensembl; ENSCANT00000033963; ENSCANP00000011069; ENSCANG00000028929.
DR   GeneID; 105519438; -.
DR   CTD; 262; -.
DR   GeneTree; ENSGT00390000011776; -.
DR   OrthoDB; 932490at2759; -.
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
//