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S-adenosylmethionine decarboxylase proenzyme (AdoMetDC) (SAMDC) (EC 4.1.1.50) [Cleaved into: S-adenosylmethionine decarboxylase beta chain; S-adenosylmethionine decarboxylase alpha chain]

 SPEH_SULSO              Reviewed;         124 AA.
Q9UWY8;
24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
07-JUN-2017, entry version 100.
RecName: Full=S-adenosylmethionine decarboxylase proenzyme;
Short=AdoMetDC;
Short=SAMDC;
EC=4.1.1.50;
Contains:
RecName: Full=S-adenosylmethionine decarboxylase beta chain;
Contains:
RecName: Full=S-adenosylmethionine decarboxylase alpha chain;
Flags: Precursor;
Name=speH; OrderedLocusNames=SSO0585; ORFNames=C21_014;
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 /
P2).
Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
Sulfolobus.
NCBI_TaxID=273057;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
PubMed=10701121; DOI=10.1139/g99-108;
Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D.,
Gaasterland T., Garrett R.A., Gordon P., Jeffries A.C., Kozera C.,
Kushwaha N., Lafleur E., Medina N., Peng X., Penny S.L., She Q.,
St Jean A., van der Oost J., Young F., Zivanovic Y., Doolittle W.F.,
Ragan M.A., Sensen C.W.;
"Gene content and organization of a 281-kbp contig from the genome of
the extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
Genome 43:116-136(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
PubMed=11427726; DOI=10.1073/pnas.141222098;
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G.,
Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A.,
De Moors A., Erauso G., Fletcher C., Gordon P.M.K.,
Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X.,
Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N.,
Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
"The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
[3]
CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, AND SCHIFF BASE FORMATION.
STRAIN=DSM 5833 / MT-4;
PubMed=1649051; DOI=10.1111/j.1432-1033.1991.tb16136.x;
Cacciapuoti G., Porcelli M., De Rosa M., Gambacorta A., Bertoldo C.,
Zappia V.;
"S-adenosylmethionine decarboxylase from the thermophilic
archaebacterium Sulfolobus solfataricus. Purification, molecular
properties and studies on the covalently bound pyruvate.";
Eur. J. Biochem. 199:395-400(1991).
[4]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ENZYME
REGULATION, SUBUNIT, MASS SPECTROMETRY, SELF-PROCESSING, AND CLEAVAGE
SITE.
STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
PubMed=18650422; DOI=10.1074/jbc.M802674200;
Giles T.N., Graham D.E.;
"Crenarchaeal arginine decarboxylase evolved from an S-
adenosylmethionine decarboxylase enzyme.";
J. Biol. Chem. 283:25829-25838(2008).
-!- FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to
S-adenosylmethioninamine (dcAdoMet), the propylamine donor
required for the synthesis of the polyamines spermine and
spermidine from the diamine putrescine. Has no arginine
decarboxylase (ArgDC) activity. {ECO:0000269|PubMed:18650422}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = S-adenosyl 3-
(methylthio)propylamine + CO(2). {ECO:0000269|PubMed:1649051,
ECO:0000269|PubMed:18650422}.
-!- COFACTOR:
Name=pyruvate; Xref=ChEBI:CHEBI:15361;
Evidence={ECO:0000269|PubMed:1649051,
ECO:0000269|PubMed:18650422};
Note=Binds 1 pyruvoyl group covalently per subunit.
{ECO:0000269|PubMed:1649051, ECO:0000269|PubMed:18650422};
-!- ENZYME REGULATION: Competitively inhibited by methylglyoxal bis-
guanylhydrazone. Irreversibly inhibited by NaBH(4) in vitro.
{ECO:0000269|PubMed:1649051, ECO:0000269|PubMed:18650422}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=96 uM for S-adenosyl-L-methionine
{ECO:0000269|PubMed:1649051};
pH dependence:
Optimum pH is 7.4. {ECO:0000269|PubMed:1649051};
Temperature dependence:
Optimum temperature is 75 degrees Celsius. Thermostable. Retains
20% activity after incubation at 100 degrees Celsius for 1 hour,
80% after 16 hours at 70 degrees Celsius, while no loss of
activity is observed after 16 hours at 50 degrees Celsius.
{ECO:0000269|PubMed:1649051};
-!- PATHWAY: Amine and polyamine biosynthesis; S-
adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from
S-adenosyl-L-methionine: step 1/1.
-!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged
as a dimer of alpha/beta heterodimers.
{ECO:0000269|PubMed:18650422}.
-!- PTM: Is synthesized initially as an inactive proenzyme. Formation
of the active enzyme involves a self-maturation process in which
the active site pyruvoyl group is generated from an internal
serine residue via an autocatalytic post-translational
modification. Two non-identical subunits are generated from the
proenzyme in this reaction, and the pyruvate is formed at the N-
terminus of the alpha chain, which is derived from the carboxyl
end of the proenzyme. The post-translation cleavage follows an
unusual pathway, termed non-hydrolytic serinolysis, in which the
side chain hydroxyl group of the serine supplies its oxygen atom
to form the C-terminus of the beta chain, while the remainder of
the serine residue undergoes an oxidative deamination to produce
ammonia and the pyruvoyl group blocking the N-terminus of the
alpha chain. {ECO:0000269|PubMed:18650422}.
-!- MASS SPECTROMETRY: Mass=6258; Method=Electrospray; Range=71-124;
Note=Pyruvoyl group-containing alpha subunit.;
Evidence={ECO:0000269|PubMed:18650422};
-!- MISCELLANEOUS: A chimeric protein containing the beta subunit of
SSO0536 and the alpha subunit of SSO0585 (SpeH) has ArgDC activity
and no AdoMetDC activity, implicating residues responsible for
substrate specificity in the beta subunit. But additional factors
in the alpha subunit are required for efficient cleavage and
turnover.
-!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y18930; CAB57715.1; -; Genomic_DNA.
EMBL; AE006641; AAK40898.1; -; Genomic_DNA.
PIR; C90205; C90205.
ProteinModelPortal; Q9UWY8; -.
SMR; Q9UWY8; -.
STRING; 273057.SSO0585; -.
EnsemblBacteria; AAK40898; AAK40898; SSO0585.
KEGG; sso:SSO0585; -.
PATRIC; fig|273057.12.peg.594; -.
eggNOG; arCOG00279; Archaea.
eggNOG; COG1586; LUCA.
HOGENOM; HOG000216579; -.
InParanoid; Q9UWY8; -.
KO; K01611; -.
OMA; LCVHQFS; -.
OrthoDB; POG093Z0GPL; -.
BRENDA; 4.1.1.50; 6163.
UniPathway; UPA00331; UER00451.
Proteomes; UP000001974; Chromosome.
GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IDA:UniProtKB.
GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008295; P:spermidine biosynthetic process; IDA:UniProtKB.
Gene3D; 3.60.90.10; -; 1.
HAMAP; MF_00464; AdoMetDC_1; 1.
InterPro; IPR003826; AdoMetDC_fam_prok.
InterPro; IPR016067; S-AdoMet_deCO2ase_core.
InterPro; IPR017716; S-AdoMet_deCOase_pro-enz.
Pfam; PF02675; AdoMet_dc; 1.
SUPFAM; SSF56276; SSF56276; 1.
TIGRFAMs; TIGR03330; SAM_DCase_Bsu; 1.
1: Evidence at protein level;
Autocatalytic cleavage; Complete proteome; Decarboxylase; Lyase;
Polyamine biosynthesis; Pyruvate; Reference proteome;
S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis;
Zymogen.
CHAIN 1 70 S-adenosylmethionine decarboxylase beta
chain.
/FTId=PRO_0000030151.
CHAIN 71 124 S-adenosylmethionine decarboxylase alpha
chain.
/FTId=PRO_0000030152.
ACT_SITE 71 71 Schiff-base intermediate with substrate;
via pyruvic acid.
ACT_SITE 76 76 Proton acceptor; for processing activity.
{ECO:0000250}.
ACT_SITE 91 91 Proton donor; for catalytic activity.
{ECO:0000250}.
SITE 70 71 Cleavage (non-hydrolytic); by autolysis.
MOD_RES 71 71 Pyruvic acid (Ser); by autocatalysis.
SEQUENCE 124 AA; 14044 MW; 002511155E18D68A CRC64;
MMMGVELAFP KVVGKQVYGS LYECDEDVLK DTKRLEQIIK EAADIGNMNI LDIKSWKIGE
GVSVVAIILE SHITIHTWPE YRFATVDVYS CGPHTSPLNA FRYIVEKLGA KRYTINEADR
SSEF


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