DCAM_XENLA
ID DCAM_XENLA Reviewed; 335 AA.
AC P79888; Q5D0C5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme;
DE Short=AdoMetDC;
DE Short=SAMDC;
DE EC=4.1.1.50;
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tail bud;
RX PubMed=8765748; DOI=10.1016/0167-4781(96)00020-6;
RA Shinga J., Kashiwagi K., Tashiro K., Igarashi K., Shiokawa K.;
RT "Maternal and zygotic expression of mRNA for S-adenosylmethionine
RT decarboxylase and its relevance to the unique polyamine composition in
RT Xenopus oocytes and embryos.";
RL Biochim. Biophys. Acta 1308:31-40(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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.
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 -!- 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 -!- DEVELOPMENTAL STAGE: First expressed at stage I of oocyte development,
CC and is maximally expressed at stage II. Levels decline during oocyte
CC maturation and after fertilization, and also in the early neurula.
CC Levels increase dramatically during the late neurula stage reaching a
CC maximum at the tail bud stage.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
CC {ECO:0000305}.
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DR EMBL; S82621; AAB36519.1; -; mRNA.
DR EMBL; BC042281; AAH42281.1; -; mRNA.
DR PIR; S72197; S72197.
DR RefSeq; NP_001080360.1; NM_001086891.1.
DR AlphaFoldDB; P79888; -.
DR SMR; P79888; -.
DR DNASU; 380052; -.
DR GeneID; 380052; -.
DR KEGG; xla:380052; -.
DR CTD; 380052; -.
DR Xenbase; XB-GENE-484615; amd1.L.
DR OrthoDB; 932490at2759; -.
DR UniPathway; UPA00331; UER00451.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 380052; Expressed in brain and 19 other tissues.
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 2: Evidence at transcript level;
KW Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis;
KW Pyruvate; Reference proteome; S-adenosyl-L-methionine; Schiff base;
KW Spermidine biosynthesis; Zymogen.
FT CHAIN 1..69
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /id="PRO_0000029971"
FT CHAIN 70..335
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /id="PRO_0000029972"
FT ACT_SITE 12
FT /evidence="ECO:0000250"
FT ACT_SITE 15
FT /evidence="ECO:0000250"
FT ACT_SITE 70
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250"
FT ACT_SITE 84
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 231
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 245
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT SITE 69..70
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000250"
FT MOD_RES 70
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 335 AA; 38819 MW; BA158A226F21F28C CRC64;
MKMEESAAHF FEGTEKLLEL WFSQQDASKG SGDLRDIPRF EWDKLLENVH CLIISVTKTD
KQEAYVLSES SMFVSKRRFI LKTCGTTLLL QALVPLLELA REYCGFDGIQ NFFYSRKNFM
KPNHQEYPHR NFHEEVEFLN QIFPNGAAYC MGRINSDCWY LYTLDIPDEY VISQPDQTLE
ILMSELDPEV MDQFYMKEGV TANDVTRVSG IRDLITGSVI DATMFSPCGY SMNGMKSDGT
YWTIHITPEP DFSYVSFETN VSLTTYDDLI SKVVDVFKPR KFVTTLFVNQ SSKCRTTFSC
AQKIEGFRRV DRQFAQFNDY NFVFTSFAKI QPQQS
