HMM Summary Page: TIGR04350

Functionputative C-S lyase
Trusted Cutoff340.00
Domain Trusted Cutoff340.00
Noise Cutoff325.00
Domain Noise Cutoff325.00
Isology Typesubfamily
EC Number4.4.-.-
HMM Length384
AuthorHaft DH
Entry DateJul 3 2012 3:52PM
Last ModifiedJul 3 2012 3:52PM
CommentMembers of this subfamily are probable C-S lyases from a family of pyridoxal phosphate-dependent enzymes that tend to be (mis)annotated as probable aminotransferases. One member is PatB of Bacillus subtilis, a proven C-S-lyase. Another is the virulence factor cystalysin from Treponema denticola, whose hemolysin activity may stem from H2S production. Members of the seed alignment occur next to examples of the enzyme 5-histidylcysteine sulfoxide synthase, from ovothiol A biosynthesis, and would be expected to perform a C-S cleavage of 5-histidylcysteine sulfoxide to leave 1-methyl-4-mercaptohistidine (ovothiol A).
ReferencesRN [1] RM PMID:15760717 RT The PatB protein of Bacillus subtilis is a C-S-lyase. RA Auger S, Gomez MP, Danchin A, Martin-Verstraete I RL Biochimie. 2005 Feb;87(2):231-8. RN [2] RM PMID:10880431 RT Crystal structure of cystalysin from Treponema denticola: a pyridoxal 5'-phosphate-dependent protein acting as a haemolytic enzyme. RA Krupka HI, Huber R, Holt SC, Clausen T RL EMBO J. 2000 Jul 3;19(13):3168-78. RN [3] RM PMID:21247153 RT Identification and characterization of the first ovothiol biosynthetic enzyme. RA Braunshausen A, Seebeck FP RL J Am Chem Soc. 2011 Feb 16;133(6):1757-9.