Accession | TIGR04344 |
Name | ovoA_Nterm |
Function | 5-histidylcysteine sulfoxide synthase |
Gene Symbol | ovoA |
Trusted Cutoff | 400.00 |
Domain Trusted Cutoff | 400.00 |
Noise Cutoff | 325.00 |
Domain Noise Cutoff | 325.00 |
Isology Type | equivalog_domain |
HMM Length | 444 |
Author | Haft DH |
Entry Date | Jun 22 2012 3:01PM |
Last Modified | Aug 12 2012 6:56PM |
Comment | Ovothiol A is N1-methyl-4-mercaptohistidine. In the absence of S-adenosylmethione, a methyl donor, the intermediate produced is 4-mercaptohistidine. In both Erwinia tasmaniensis and Trypanosoma cruzi, a protein occurs with 5-histidylcysteine sulfoxide synthase activity, but these two enzymes and most homologs share an additional C-terminal methyltransferase domain. Thus OvoA may be a bifunctional enzyme with 5-histidylcysteine sulfoxide synthase and 4-mercaptohistidine N1-methyltranferase activity. This model describes the 5-histidylcysteine sulfoxide synthase domain, a homolog of the ergothioneine biosynthesis protein EgtB. |
References | RN [1]
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.
RN [2]
RM PMID:9022682
RT Studies on the biosynthesis of ovothiol A. Identification of 4-mercaptohistidine as an intermediate.
RA Steenkamp DJ, Weldrick D, Spies HS
RL Eur J Biochem. 1996 Dec 15;242(3):557-66. |
Genome Property | GenProp1064: ovothiol biosynthesis (HMM) |