DCAM_RAT
ID DCAM_RAT Reviewed; 333 AA.
AC P17708;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 3.
DT 03-AUG-2022, entry version 161.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2323572; DOI=10.1016/0378-1119(90)90279-z;
RA Pulkka A., Keraenen M.R., Salmela A., Salmikangas P., Ihalainen R.,
RA Pajunen A.;
RT "Nucleotide sequence of rat S-adenosylmethionine decarboxylase cDNA.
RT Comparison with an intronless rat pseudogene.";
RL Gene 86:193-199(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEOLYTIC CLEAVAGE.
RX PubMed=2460457; DOI=10.1016/s0021-9258(18)37495-7;
RA Pajunen A., Crozat A., Jaenne O.A., Ihalainen R., Laitinen P.H.,
RA Stanley B., Madhubala R., Pegg A.E.;
RT "Structure and regulation of mammalian S-adenosylmethionine
RT decarboxylase.";
RL J. Biol. Chem. 263:17040-17049(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1936275; DOI=10.1016/0014-5793(91)81304-q;
RA Pulkka A., Ihalainen R., Aatsinki J., Pajunen A.;
RT "Structure and organization of the gene encoding rat S-adenosylmethionine
RT decarboxylase.";
RL FEBS Lett. 291:289-295(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar; TISSUE=Spleen;
RX PubMed=8314573; DOI=10.1006/geno.1993.1195;
RA Pulkka A., Ihalainen R., Suorsa A., Riviere M., Szpirer J., Pajunen A.;
RT "Structures and chromosomal localizations of two rat genes encoding S-
RT adenosylmethionine decarboxylase.";
RL Genomics 16:342-349(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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:2460457}.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
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DR EMBL; M34464; AAA40683.1; -; mRNA.
DR EMBL; M64274; AAA42105.1; -; Genomic_DNA.
DR EMBL; Z15109; CAA78814.1; -; Genomic_DNA.
DR EMBL; Z15122; CAA78814.1; JOINED; Genomic_DNA.
DR EMBL; Z15123; CAA78814.1; JOINED; Genomic_DNA.
DR EMBL; BC061532; AAH61532.1; -; mRNA.
DR PIR; JQ0439; DCRTDM.
DR RefSeq; NP_112273.3; NM_031011.3.
DR AlphaFoldDB; P17708; -.
DR SMR; P17708; -.
DR STRING; 10116.ENSRNOP00000000715; -.
DR BindingDB; P17708; -.
DR ChEMBL; CHEMBL3808; -.
DR DrugCentral; P17708; -.
DR iPTMnet; P17708; -.
DR PhosphoSitePlus; P17708; -.
DR PaxDb; P17708; -.
DR PRIDE; P17708; -.
DR GeneID; 81640; -.
DR KEGG; rno:81640; -.
DR UCSC; RGD:2104; rat.
DR CTD; 262; -.
DR RGD; 2104; Amd1.
DR VEuPathDB; HostDB:ENSRNOG00000000585; -.
DR eggNOG; KOG0788; Eukaryota.
DR HOGENOM; CLU_023050_1_0_1; -.
DR InParanoid; P17708; -.
DR OMA; LEIWFEE; -.
DR OrthoDB; 932490at2759; -.
DR Reactome; R-RNO-351202; Metabolism of polyamines.
DR UniPathway; UPA00331; UER00451.
DR PRO; PR:P17708; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000585; Expressed in stomach and 19 other tissues.
DR Genevisible; P17708; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019810; F:putrescine binding; IDA:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0006595; P:polyamine metabolic process; IDA:RGD.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IDA:RGD.
DR GO; GO:0008295; P:spermidine biosynthetic process; IDA:RGD.
DR GO; GO:0006597; P:spermine biosynthetic process; IDA:RGD.
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; Lyase; Phosphoprotein;
KW 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_0000029969"
FT CHAIN 68..333
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /id="PRO_0000029970"
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:0000250|UniProtKB:P17707"
FT MOD_RES 68
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT CONFLICT 5
FT /note="H -> P (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="A -> G (in Ref. 1; AAA40683)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 38137 MW; 9323E2D38BD8FEF1 CRC64;
MEAAHFFEGT EKLLEVWFSR QQSDASQGSG DLRTIPRSEW DVLLKDVQCS IISVTKTDKQ
EAYVLSESSM FVSKRRFILK TCGTTLLLKA LVPLLKLARD YSGFDSIQSF FYSRKNFMKP
SHQGYPHRNF QEEIEFLNAI FPNGAAYCMG RMNSDCWYLY TLDLPESRVI NQPDQTLEIL
MSELDPAVMD QFYMKDGVTA KDVTRESGIR DLIPGSVIDA TLFNPCGYSM NGMKSDGTYW
TIHITPEPEF SYVSFETNLS QTSYDDLIRK VVEVFKPGKF VTTLFVNQSS KCRTVLSSPQ
KIDGFKRLDC QSAMFNDYNF VFTSFAKKQQ QQS
