DCAM_LEIDO
ID DCAM_LEIDO Reviewed; 382 AA.
AC Q25264;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 97.
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;
OS Leishmania donovani.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5661;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MHOM/SD/62/1S;
RX PubMed=11734561; DOI=10.1074/jbc.m110118200;
RA Roberts S.C., Scott J., Gasteier J.E., Jiang Y., Brooks B., Jardim A.,
RA Carter N.S., Heby O., Ullman B.;
RT "S-adenosylmethionine decarboxylase from Leishmania donovani. Molecular,
RT genetic, and biochemical characterization of null mutants and
RT overproducers.";
RL J. Biol. Chem. 277:5902-5909(2002).
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 -!- 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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U20091; AAA61968.2; -; Genomic_DNA.
DR AlphaFoldDB; Q25264; -.
DR SMR; Q25264; -.
DR VEuPathDB; TriTrypDB:LdBPK_303150.1; -.
DR VEuPathDB; TriTrypDB:LdCL_300037100; -.
DR VEuPathDB; TriTrypDB:LDHU3_30.4190; -.
DR BRENDA; 4.1.1.50; 2947.
DR UniPathway; UPA00331; UER00451.
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 PROSITE; PS01336; ADOMETDC; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis;
KW Pyruvate; S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis;
KW Zymogen.
FT CHAIN 1..89
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000029979"
FT CHAIN 90..382
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000029980"
FT ACT_SITE 33
FT /evidence="ECO:0000250"
FT ACT_SITE 36
FT /evidence="ECO:0000250"
FT ACT_SITE 90
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250"
FT ACT_SITE 104
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 254
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 267
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 89..90
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000250"
FT SITE 254
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT MOD_RES 90
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 382 AA; 43006 MW; B96C8902AAA15502 CRC64;
MNVCSNTTKD PLTLMAMWGS MKGYNPEQGF SFEGPEKRLE VILRCTLETH VDGLRSLDDS
VWSGVVGSLN AQIVSRESNE YINSYVLTES SLFVMKNRII LITCGTTTLL NSIPNILEAI
SAVRGELEWV SFMHKNYSFP WMQKGPHTSL ADEFATLKQH FPTGKPYIFG PVDSDHYFLF
CYDDIIRPCS SEDDTQLSMT MYGLDKEQTK HWFSDRFIST SAETAAIRAA THLDRVVDGT
WTLHDLQFEP CGYSINAIRD EEYQTMHITP EDHCSFASYE TNSRAANYSD RMKKVLGVFR
PQRFTVIVFL DPESPVGKAY NEGKGIGVEP EYYPEYNLLH RTTNEFAPGY VAMKINYVRT
AAVEETDTAV GGAEPGAEGG PD
