DCAM_BOVIN
ID DCAM_BOVIN Reviewed; 334 AA.
AC P50243; Q08DE3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme;
DE Short=AdoMetDC;
DE Short=SAMDC;
DE EC=4.1.1.50 {ECO:0000250|UniProtKB:P17707};
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=AMD1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8416975; DOI=10.1016/s0021-9258(18)54212-5;
RA Hill J.R., Morris D.R.;
RT "Cell-specific translational regulation of S-adenosylmethionine
RT decarboxylase mRNA. Dependence on translation and coding capacity of the
RT cis-acting upstream open reading frame.";
RL J. Biol. Chem. 268:726-731(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 209-232, PARTIAL PROTEIN SEQUENCE,
RP PROTEOLYTIC CLEAVAGE, AND PYRUVATE FORMATION AT SER-68.
RX PubMed=3017942; DOI=10.1016/s0021-9258(18)67300-4;
RA Mach M., White M.W., Neubauer M., Degen J.L., Morris D.R.;
RT "Isolation of a cDNA clone encoding S-adenosylmethionine decarboxylase.
RT Expression of the gene in mitogen-activated lymphocytes.";
RL J. Biol. Chem. 261:11697-11703(1986).
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:0000250|UniProtKB:P0DMN7}.
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:0000250|UniProtKB:P17707};
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 {ECO:0000250}.
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. {ECO:0000250|UniProtKB:P17707,
CC ECO:0000269|PubMed:3017942}.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
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DR EMBL; M95605; AAA30359.1; -; mRNA.
DR EMBL; BC123795; AAI23796.1; -; mRNA.
DR EMBL; M14289; AAA30360.1; -; mRNA.
DR PIR; I45851; I45851.
DR RefSeq; NP_776415.1; NM_173990.2.
DR AlphaFoldDB; P50243; -.
DR SMR; P50243; -.
DR STRING; 9913.ENSBTAP00000004338; -.
DR PaxDb; P50243; -.
DR PRIDE; P50243; -.
DR Ensembl; ENSBTAT00000004338; ENSBTAP00000004338; ENSBTAG00000003342.
DR GeneID; 280997; -.
DR KEGG; bta:280997; -.
DR CTD; 262; -.
DR VEuPathDB; HostDB:ENSBTAG00000003342; -.
DR VGNC; VGNC:25859; AMD1.
DR eggNOG; KOG0788; Eukaryota.
DR GeneTree; ENSGT00390000011776; -.
DR HOGENOM; CLU_023050_1_0_1; -.
DR InParanoid; P50243; -.
DR OrthoDB; 932490at2759; -.
DR TreeFam; TF313561; -.
DR UniPathway; UPA00331; UER00451.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000003342; Expressed in oocyte and 108 other tissues.
DR ExpressionAtlas; P50243; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0019810; F:putrescine binding; IBA:GO_Central.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008295; P:spermidine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006597; P:spermine biosynthetic process; IBA:GO_Central.
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 Phosphoprotein; Polyamine biosynthesis; Pyruvate; Reference proteome;
KW S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis; Zymogen.
FT CHAIN 1..67
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /id="PRO_0000029957"
FT CHAIN 68..334
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /id="PRO_0000029958"
FT ACT_SITE 8
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 11
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 68
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 82
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 229
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 243
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT BINDING 7
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT SITE 67..68
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000269|PubMed:3017942"
FT MOD_RES 68
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000269|PubMed:3017942"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17707"
SQ SEQUENCE 334 AA; 38365 MW; D8AFB98C9DD8A1E9 CRC64;
MEAAHFFEGT EKLLEVWFSR QQPDANQGSG DLRTIPRSEW DILLKDVQCS IISVTKTDKQ
EAYVLSESSM FVSKRRFILK TCGTTLLLKA LVPLLKLARD YSGFDSIQSF FYSRKNFMKP
SHQGYPHRNF QEEIEFLNAI FPNGAAYCMG RMNSDCWYLY TLDFPESRVI NQPDQTLEIL
MSELDPAVMD QFYMKDGVTA KDVTRESGIR DLIPGSVIDA TMFNPCGYSM NGMKSDGTYW
TIHITPEPEF SYVSFETNLS QTSYDDLIRK VVEVFKPGKF VTTLFVNQSS KCRTVLSSPQ
KIEGFKRLDC QSALFNDYNF VFTSFAKKQQ QQQS
