| 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) |
