Sequence of SPEH_SACS2
EC Number:4.1.1.50
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
adenosylmethionine decarboxylase
Q9UWY8
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
124
14044
Reaction
S-adenosyl-L-methionine = S-adenosyl 3-(methylsulfanyl)propylamine + CO2
Other sequences found for EC No. 4.1.1.50
General information:
Sequence
0 MMMGVELAFP KVVGKQVYGS LYECDEDVLK DTKRLEQIIK EAADIGNMNI LDIKSWKIGE
60 GVSVVAIILE SHITIHTWPE YRFATVDVYS CGPHTSPLNA FRYIVEKLGA KRYTINEADR
120 SSEF
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
998889
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
998890
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
998891
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
998892
Giles T.N.,Graham D.E.
Crenarchaeal arginine decarboxylase evolved from an S-adenosylmethionine decarboxylase enzyme.
J. Biol. Chem.
283
25829-25838
2008
