DCAM2_MOUSE
ID DCAM2_MOUSE Reviewed; 334 AA.
AC D3Z6H8; P82184; Q58E47;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme 2;
DE Short=AdoMetDC 2;
DE Short=SAMDC 2;
DE EC=4.1.1.50 {ECO:0000269|PubMed:7890685, ECO:0000269|PubMed:9620866};
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase 2 alpha chain;
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase 2 beta chain;
DE Flags: Precursor;
GN Name=Amd2; Synonyms=Amd-2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND PROTEOLYTIC
RP CLEAVAGE.
RC TISSUE=Spleen;
RX PubMed=7890685; DOI=10.1074/jbc.270.10.5642;
RA Persson K., Holm I., Heby O.;
RT "Cloning and sequencing of an intronless mouse S-adenosylmethionine
RT decarboxylase gene coding for a functional enzyme strongly expressed in the
RT liver.";
RL J. Biol. Chem. 270:5642-5648(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND PROTEOLYTIC
RP CLEAVAGE.
RC STRAIN=129/SvJ;
RX PubMed=9620866; DOI=10.1042/bj3320651;
RA Nishimura K., Liisanantti M., Muta Y., Kashiwagi K., Shirahata A.,
RA Janne M., Kankare K., Janne O.A., Igarashi K.;
RT "Structure and activity of mouse S-adenosylmethionine decarboxylase gene
RT promoters and properties of the encoded proteins.";
RL Biochem. J. 332:651-659(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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:0000269|PubMed:7890685, ECO:0000269|PubMed:9620866};
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, ECO:0000269|PubMed:7890685,
CC ECO:0000269|PubMed:9620866}.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
CC -!- CAUTION: Product of an intronless, probably retrotransposed, copy of
CC AMD1. mRNA levels are 10-40 times lower than AMD1 (PubMed:9620866).
CC {ECO:0000305|PubMed:9620866}.
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DR EMBL; Z23077; CAA80614.1; -; Genomic_DNA.
DR EMBL; AC147238; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS48536.1; -.
DR PIR; A55948; A55948.
DR RefSeq; NP_031470.3; NM_007444.3.
DR AlphaFoldDB; D3Z6H8; -.
DR SMR; D3Z6H8; -.
DR STRING; 10090.ENSMUSP00000079703; -.
DR MaxQB; D3Z6H8; -.
DR PaxDb; D3Z6H8; -.
DR PeptideAtlas; D3Z6H8; -.
DR PRIDE; D3Z6H8; -.
DR DNASU; 100041585; -.
DR Ensembl; ENSMUST00000080898; ENSMUSP00000079703; ENSMUSG00000063953.
DR GeneID; 100041585; -.
DR KEGG; mmu:100041585; -.
DR UCSC; uc007ews.3; mouse.
DR CTD; 100041585; -.
DR MGI; MGI:1333111; Amd2.
DR VEuPathDB; HostDB:ENSMUSG00000063953; -.
DR eggNOG; KOG0788; Eukaryota.
DR GeneTree; ENSGT00390000011776; -.
DR HOGENOM; CLU_023050_1_0_1; -.
DR OMA; CYQRKNE; -.
DR OrthoDB; 932490at2759; -.
DR PhylomeDB; D3Z6H8; -.
DR TreeFam; TF313561; -.
DR UniPathway; UPA00331; UER00451.
DR BioGRID-ORCS; 100041585; 5 hits in 39 CRISPR screens.
DR ChiTaRS; Amd2; mouse.
DR PRO; PR:D3Z6H8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; D3Z6H8; protein.
DR Bgee; ENSMUSG00000063953; Expressed in quadriceps femoris and 100 other tissues.
DR Genevisible; D3Z6H8; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019810; F:putrescine binding; ISO:MGI.
DR GO; GO:0006595; P:polyamine metabolic process; ISO:MGI.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; ISO:MGI.
DR GO; GO:0008295; P:spermidine biosynthetic process; ISO:MGI.
DR GO; GO:0006597; P:spermine biosynthetic process; ISO:MGI.
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 2 beta chain"
FT /id="PRO_0000029965"
FT CHAIN 68..334
FT /note="S-adenosylmethionine decarboxylase 2 alpha chain"
FT /id="PRO_0000029966"
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 70
FT /note="M -> I (in Ref. 1; CAA80614)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="A -> V (in Ref. 1; CAA80614)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="H -> D (in Ref. 1; CAA80614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 38295 MW; 1A6CA1E9A2E7FD79 CRC64;
MEAAHFFEGT EKLLEVWFSR QQSDASQGSG DLRTIPRSEW DVLLKDVQCS IISVTKTDKQ
EAYVLSESSM FVSKRRFILK TCGTTLLLKA LVPLLKLARD YSGFDSIQSF FYSRKNFMKP
SHQGYPHRNF QEEIEFLNAI FPNGAAYCMG RMNSDCWYLY TLDFPESRVI SQPDQTLEIL
MSELDPAVMD QFYMKDGVTA KDVTRESGIR DLIPGSVIDA TLFNPCGYSM NGMKSDGTYW
TIHITPEPEF SYVSFETNLS QTSYDHLIRK VVEVFKPGKF VTTLFVNQSS KCRTVLSSPQ
KIDGFKRLDC QSAMFNDYNF VFTSFAKKQQ QQQS
