SPEH_SACS2
ID SPEH_SACS2 Reviewed; 124 AA.
AC Q9UWY8;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 117.
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=SSO0585; ORFNames=C21_014;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10701121; DOI=10.1139/g99-108;
RA Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT "Gene content and organization of a 281-kbp contig from the genome of the
RT extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL Genome 43:116-136(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SCHIFF BASE FORMATION.
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=1649051; DOI=10.1111/j.1432-1033.1991.tb16136.x;
RA Cacciapuoti G., Porcelli M., De Rosa M., Gambacorta A., Bertoldo C.,
RA Zappia V.;
RT "S-adenosylmethionine decarboxylase from the thermophilic archaebacterium
RT Sulfolobus solfataricus. Purification, molecular properties and studies on
RT the covalently bound pyruvate.";
RL Eur. J. Biochem. 199:395-400(1991).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY
RP REGULATION, SUBUNIT, MASS SPECTROMETRY, SELF-PROCESSING, CLEAVAGE SITE, AND
RP PYRUVATE FORMATION AT SER-71.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=18650422; DOI=10.1074/jbc.m802674200;
RA Giles T.N., Graham D.E.;
RT "Crenarchaeal arginine decarboxylase evolved from an S-adenosylmethionine
RT decarboxylase enzyme.";
RL J. Biol. Chem. 283:25829-25838(2008).
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. Has no arginine decarboxylase (ArgDC) activity.
CC {ECO:0000269|PubMed:18650422}.
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:1649051, ECO:0000269|PubMed:18650422};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000269|PubMed:1649051, ECO:0000269|PubMed:18650422};
CC Note=Binds 1 pyruvoyl group covalently per subunit.
CC {ECO:0000269|PubMed:1649051, ECO:0000269|PubMed:18650422};
CC -!- ACTIVITY REGULATION: Competitively inhibited by methylglyoxal bis-
CC guanylhydrazone. Irreversibly inhibited by NaBH(4) in vitro.
CC {ECO:0000269|PubMed:1649051, ECO:0000269|PubMed:18650422}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=96 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:1649051};
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:1649051};
CC Temperature dependence:
CC Optimum temperature is 75 degrees Celsius. Thermostable. Retains 20%
CC activity after incubation at 100 degrees Celsius for 1 hour, 80%
CC after 16 hours at 70 degrees Celsius, while no loss of activity is
CC observed after 16 hours at 50 degrees Celsius.
CC {ECO:0000269|PubMed:1649051};
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:18650422}.
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:18650422}.
CC -!- MASS SPECTROMETRY: [S-adenosylmethionine decarboxylase alpha chain]:
CC Mass=6258; Method=Electrospray; Note=Pyruvoyl group-containing alpha
CC subunit.; Evidence={ECO:0000269|PubMed:18650422};
CC -!- MISCELLANEOUS: A chimeric protein containing the beta subunit of
CC SSO0536 and the alpha subunit of SSO0585 (SpeH) has ArgDC activity and
CC no AdoMetDC activity, implicating residues responsible for substrate
CC specificity in the beta subunit. But additional factors in the alpha
CC subunit are required for efficient cleavage and turnover.
CC -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; Y18930; CAB57715.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK40898.1; -; Genomic_DNA.
DR PIR; C90205; C90205.
DR AlphaFoldDB; Q9UWY8; -.
DR SMR; Q9UWY8; -.
DR STRING; 273057.SSO0585; -.
DR PRIDE; Q9UWY8; -.
DR EnsemblBacteria; AAK40898; AAK40898; SSO0585.
DR KEGG; sso:SSO0585; -.
DR PATRIC; fig|273057.12.peg.594; -.
DR eggNOG; arCOG00279; Archaea.
DR HOGENOM; CLU_125470_2_1_2; -.
DR InParanoid; Q9UWY8; -.
DR OMA; FMCGACD; -.
DR PhylomeDB; Q9UWY8; -.
DR BRENDA; 4.1.1.50; 6163.
DR SABIO-RK; Q9UWY8; -.
DR UniPathway; UPA00331; UER00451.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008295; P:spermidine biosynthetic process; IDA:UniProtKB.
DR HAMAP; MF_00464; AdoMetDC_1; 1.
DR InterPro; IPR003826; AdoMetDC_fam_prok.
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..70
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /id="PRO_0000030151"
FT CHAIN 71..124
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /id="PRO_0000030152"
FT ACT_SITE 71
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT ACT_SITE 76
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 91
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 70..71
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT MOD_RES 71
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000269|PubMed:18650422"
SQ SEQUENCE 124 AA; 14044 MW; 002511155E18D68A CRC64;
MMMGVELAFP KVVGKQVYGS LYECDEDVLK DTKRLEQIIK EAADIGNMNI LDIKSWKIGE
GVSVVAIILE SHITIHTWPE YRFATVDVYS CGPHTSPLNA FRYIVEKLGA KRYTINEADR
SSEF
