SPEH_METJA
ID SPEH_METJA Reviewed; 124 AA.
AC Q57763;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 126.
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=speH; OrderedLocusNames=MJ0315;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, SELF-PROCESSING, CLEAVAGE SITE, MASS
RP SPECTROMETRY, AND PYRUVATE FORMATION AT SER-64.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=11073910; DOI=10.1128/jb.182.23.6667-6672.2000;
RA Kim A.D., Graham D.E., Seeholzer S.H., Markham G.D.;
RT "S-adenosylmethionine decarboxylase from the archaeon Methanococcus
RT jannaschii: identification of a novel family of pyruvoyl enzymes.";
RL J. Bacteriol. 182:6667-6672(2000).
RN [3]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP SCHIFF BASE FORMATION, AND CATALYTIC MECHANISM.
RX PubMed=14573607; DOI=10.1074/jbc.m308793200;
RA Lu Z.J., Markham G.D.;
RT "Catalytic properties of the archaeal S-adenosylmethionine decarboxylase
RT from Methanococcus jannaschii.";
RL J. Biol. Chem. 279:265-273(2004).
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:11073910, ECO:0000269|PubMed:14573607};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000269|PubMed:11073910};
CC Note=Binds 1 pyruvoyl group covalently per subunit.
CC {ECO:0000269|PubMed:11073910};
CC -!- ACTIVITY REGULATION: Competitively inhibited by methylglyoxal bis-
CC guanylhydrazone. Inactivated by treatment with the imine reductant
CC NaCNBH(3) only in the presence of substrate.
CC {ECO:0000269|PubMed:14573607}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=95 uM for S-adenosyl-L-methionine (at pH 7.5 and 22 degrees
CC Celsius) {ECO:0000269|PubMed:14573607};
CC Vmax=37 nmol/min/mg enzyme (at pH 7.5 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:14573607};
CC Note=The turnover number increases 30-fold when temperature is
CC increased from 22 to 70 degrees Celsius, whereas the Km increases 3-
CC fold.;
CC pH dependence:
CC Optimum pH is 6-8. {ECO:0000269|PubMed:14573607};
CC Temperature dependence:
CC Optimum temperature is superior to 90 degrees Celsius. Thermostable.
CC Retains full activity after 3 hours at 70 degrees Celsius.
CC {ECO:0000269|PubMed:14573607};
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 arranged as a
CC dimer of alpha/beta heterodimers. {ECO:0000269|PubMed:11073910}.
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:11073910}.
CC -!- MASS SPECTROMETRY: [S-adenosylmethionine decarboxylase beta chain]:
CC Mass=6793.1; Method=MALDI; Evidence={ECO:0000269|PubMed:11073910};
CC -!- MASS SPECTROMETRY: [S-adenosylmethionine decarboxylase alpha chain]:
CC Mass=6990.2; Method=MALDI; Note=Pyruvoyl group-containing alpha
CC subunit.; Evidence={ECO:0000269|PubMed:11073910};
CC -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB98301.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L77117; AAB98301.1; ALT_INIT; Genomic_DNA.
DR PIR; D64339; D64339.
DR RefSeq; WP_064496461.1; NC_000909.1.
DR AlphaFoldDB; Q57763; -.
DR SMR; Q57763; -.
DR STRING; 243232.MJ_0315; -.
DR EnsemblBacteria; AAB98301; AAB98301; MJ_0315.
DR GeneID; 1451170; -.
DR KEGG; mja:MJ_0315; -.
DR eggNOG; arCOG00279; Archaea.
DR HOGENOM; CLU_125470_2_3_2; -.
DR InParanoid; Q57763; -.
DR OMA; VYTCGEH; -.
DR OrthoDB; 106151at2157; -.
DR PhylomeDB; Q57763; -.
DR SABIO-RK; Q57763; -.
DR UniPathway; UPA00331; UER00451.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008295; P:spermidine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.30.160.750; -; 1.
DR Gene3D; 3.30.360.110; -; 1.
DR HAMAP; MF_00464; AdoMetDC_1; 1.
DR InterPro; IPR042286; AdoMetDC_C.
DR InterPro; IPR003826; AdoMetDC_fam_prok.
DR InterPro; IPR042284; AdoMetDC_N.
DR InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR InterPro; IPR017716; S-AdoMet_deCOase_pro-enz.
DR PANTHER; PTHR33866; PTHR33866; 1.
DR Pfam; PF02675; AdoMet_dc; 1.
DR SUPFAM; SSF56276; SSF56276; 1.
DR TIGRFAMs; TIGR03330; SAM_DCase_Bsu; 1.
PE 1: Evidence at protein 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..63
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /id="PRO_0000030133"
FT CHAIN 64..124
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /id="PRO_0000030134"
FT ACT_SITE 64
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT ACT_SITE 69
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 84
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000305"
FT SITE 63..64
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT MOD_RES 64
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000269|PubMed:11073910"
SQ SEQUENCE 124 AA; 13792 MW; BC1152CDE080F113 CRC64;
MLKYLGKHLI LELWGCDPKA LDDIEGIEKM LVDSVKACGA TLICVRTHKF SPQGATGVAV
LAESHIAIHT YPEYGYAALD VFTCGEHTDP YKALEVIREF LKPKSIQIID LKRGLMENGT
FELK
