SPED_ECOLI
ID SPED_ECOLI Reviewed; 264 AA.
AC P0A7F6; P09159;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 beta chain;
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase alpha chain;
DE Flags: Precursor;
GN Name=speD; OrderedLocusNames=b0120, JW0116;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SELF-PROCESSING, CLEAVAGE SITE,
RP COFACTOR, AND PYRUVATE FORMATION AT SER-112.
RX PubMed=3316212; DOI=10.1016/s0021-9258(18)47692-2;
RA Tabor C.W., Tabor H.;
RT "The speEspeD operon of Escherichia coli. Formation and processing of a
RT proenzyme form of S-adenosylmethionine decarboxylase.";
RL J. Biol. Chem. 262:16037-16040(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-21 AND 112-143, SELF-PROCESSING, CLEAVAGE SITE,
RP COFACTOR, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=3546296; DOI=10.1016/s0021-9258(18)61579-0;
RA Anton D.L., Kutny R.;
RT "Escherichia coli S-adenosylmethionine decarboxylase. Subunit structure,
RT reductive amination, and NH2-terminal sequences.";
RL J. Biol. Chem. 262:2817-2822(1987).
RN [6]
RP CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SCHIFF BASE FORMATION.
RC STRAIN=K12;
RX PubMed=6749853; DOI=10.1016/s0021-9258(18)33678-0;
RA Markham G.D., Tabor C.W., Tabor H.;
RT "S-adenosylmethionine decarboxylase of Escherichia coli. Studies on the
RT covalently linked pyruvate required for activity.";
RL J. Biol. Chem. 257:12063-12068(1982).
RN [7]
RP SENSITIVITY OF MUTANTS.
RX PubMed=2181453; DOI=10.1073/pnas.87.7.2851;
RA Minton K.W., Tabor H., Tabor C.W.;
RT "Paraquat toxicity is increased in Escherichia coli defective in the
RT synthesis of polyamines.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2851-2855(1990).
RN [8]
RP ALLOSTERIC METAL ION ACTIVATION, ACTIVITY REGULATION, AND PH DEPENDENCE.
RX PubMed=17567041; DOI=10.1021/bi6025962;
RA Lu Z.J., Markham G.D.;
RT "Metal ion activation of S-adenosylmethionine decarboxylase reflects cation
RT charge density.";
RL Biochemistry 46:8172-8180(2007).
CC -!- FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to S-
CC adenosylmethioninamine (dcAdoMet), the propylamine donor required for
CC the synthesis of the polyamines spermine and spermidine from the
CC diamine putrescine.
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:6749853};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000269|PubMed:3316212, ECO:0000269|PubMed:3546296,
CC ECO:0000269|PubMed:6749853};
CC Note=Binds 1 pyruvoyl group covalently per subunit.
CC {ECO:0000269|PubMed:3316212, ECO:0000269|PubMed:3546296,
CC ECO:0000269|PubMed:6749853};
CC -!- ACTIVITY REGULATION: Allosterically activated by metal cations, which
CC are absolutely required for activity. The presumed physiological
CC activator is Mg(2+), but can also be activated in vitro by other
CC divalent cations such as Mn(2+), Fe(2+) and Ca(2+), by the monovalent
CC cation Li(+), and by trivalent cations such as Eu(3+), Tb(3+) and
CC Gd(3+). Competitively inhibited by methylglyoxal bis-guanylhydrazone.
CC Also inhibited by Zn(2+), inhibition may be due to interaction with the
CC active site cysteine. Inactivated by treatment with the imine reductant
CC NaCNBH(3) only in the presence of substrate.
CC {ECO:0000269|PubMed:17567041, ECO:0000269|PubMed:3546296,
CC ECO:0000269|PubMed:6749853}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=60 uM for S-adenosyl-L-methionine (at 25 degrees Celsius in the
CC presence of 0.01 M MgCl(2)) {ECO:0000269|PubMed:6749853};
CC Vmax=3.8 umol/min/mg enzyme (at 25 degrees Celsius in the presence of
CC 0.01M MgCl(2)) {ECO:0000269|PubMed:6749853};
CC Vmax=6.8 umol/min/mg enzyme (at 37 degrees Celsius in the presence of
CC 0.1M MgCl(2)) {ECO:0000269|PubMed:6749853};
CC pH dependence:
CC Optimum pH is 7.4. Active from pH 6.7 to 8.5.
CC {ECO:0000269|PubMed:17567041, ECO:0000269|PubMed:6749853};
CC -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC step 1/1.
CC -!- SUBUNIT: Heterooctamer of four alpha and four beta chains arranged as a
CC tetramer of alpha/beta heterodimers. {ECO:0000269|PubMed:3546296}.
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:0000269|PubMed:3316212, ECO:0000269|PubMed:3546296}.
CC -!- MISCELLANEOUS: Spermidine-deficient mutants show a small decrease in
CC growth rate and increased sensibility to superoxide toxicity.
CC -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; J02804; AAA24644.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73231.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96694.1; -; Genomic_DNA.
DR PIR; B29778; DCECDM.
DR RefSeq; NP_414662.1; NC_000913.3.
DR RefSeq; WP_000734287.1; NZ_STEB01000010.1.
DR AlphaFoldDB; P0A7F6; -.
DR BioGRID; 4262031; 9.
DR DIP; DIP-47936N; -.
DR IntAct; P0A7F6; 4.
DR STRING; 511145.b0120; -.
DR jPOST; P0A7F6; -.
DR PaxDb; P0A7F6; -.
DR PRIDE; P0A7F6; -.
DR EnsemblBacteria; AAC73231; AAC73231; b0120.
DR EnsemblBacteria; BAB96694; BAB96694; BAB96694.
DR GeneID; 66671592; -.
DR GeneID; 947719; -.
DR KEGG; ecj:JW0116; -.
DR KEGG; eco:b0120; -.
DR PATRIC; fig|1411691.4.peg.2162; -.
DR EchoBASE; EB0955; -.
DR eggNOG; COG1586; Bacteria.
DR HOGENOM; CLU_092007_0_0_6; -.
DR InParanoid; P0A7F6; -.
DR OMA; HVTVHTY; -.
DR PhylomeDB; P0A7F6; -.
DR BioCyc; EcoCyc:SPED-MON; -.
DR BioCyc; MetaCyc:SPED-MON; -.
DR SABIO-RK; P0A7F6; -.
DR UniPathway; UPA00331; UER00451.
DR PRO; PR:P0A7F6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0097264; P:self proteolysis; IDA:EcoCyc.
DR GO; GO:0008295; P:spermidine biosynthetic process; IMP:EcoCyc.
DR HAMAP; MF_00465; AdoMetDC_2; 1.
DR InterPro; IPR003826; AdoMetDC_fam_prok.
DR InterPro; IPR009165; S-AdoMet_deCO2ase_bac.
DR InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR PANTHER; PTHR33866; PTHR33866; 1.
DR Pfam; PF02675; AdoMet_dc; 1.
DR PIRSF; PIRSF001356; SAM_decarboxylas; 1.
DR SUPFAM; SSF56276; SSF56276; 1.
DR TIGRFAMs; TIGR03331; SAM_DCase_Eco; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Autocatalytic cleavage; Decarboxylase;
KW Direct protein sequencing; Lyase; Magnesium; Polyamine biosynthesis;
KW Pyruvate; Reference proteome; S-adenosyl-L-methionine; Schiff base;
KW Spermidine biosynthesis; Zymogen.
FT CHAIN 1..111
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /id="PRO_0000030043"
FT CHAIN 112..264
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /id="PRO_0000030044"
FT ACT_SITE 112
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT ACT_SITE 117
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 140
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 111..112
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT MOD_RES 112
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000269|PubMed:3316212"
SQ SEQUENCE 264 AA; 30385 MW; E228BCF8EBDD0325 CRC64;
MKKLKLHGFN NLTKSLSFCI YDICYAKTAE ERDGYIAYID ELYNANRLTE ILSETCSIIG
ANILNIARQD YEPQGASVTI LVSEEPVDPK LIDKTEHPGP LPETVVAHLD KSHICVHTYP
ESHPEGGLCT FRADIEVSTC GVISPLKALN YLIHQLESDI VTIDYRVRGF TRDINGMKHF
IDHEINSIQN FMSDDMKALY DMVDVNVYQE NIFHTKMLLK EFDLKHYMFH TKPEDLTDSE
RQEITAALWK EMREIYYGRN MPAV
