| Accession | TIGR03753 |
| Name | blh_monoox |
| Function | beta-carotene 15,15'-monooxygenase, Brp/Blh family |
| Trusted Cutoff | 95.25 |
| Domain Trusted Cutoff | 95.25 |
| Noise Cutoff | 58.05 |
| Domain Noise Cutoff | 58.05 |
| Isology Type | subfamily |
| EC Number | 1.14.99.36 |
| HMM Length | 260 |
| Author | Haft DH |
| Entry Date | May 21 2009 9:28AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This integral membrane protein family includes Brp (bacterio-opsin related protein) and Blh (Brp-like protein). Bacteriorhodopsin is a light-driven proton pump with a covalently bound retinal cofactor that appears to be derived beta-carotene. Blh has been shown to cleave beta-carotene to product two all-trans retinal molecules. Mammalian enzymes with similar enzymatic function are not multiple membrane spanning proteins and are not homologous. |
| References | RN [1]
RM PMID:19366683
RT In vitro characterization of a recombinant Blh protein from an uncultured marine bacterium as a beta-carotene 15,15-prime C-dioxygenase.
RA Kim YS, Kim NH, Yeom SJ, Kim SW, Oh DK
RL J Biol Chem. 2009 Apr 14. |
| Genome Property | GenProp0856: bacterio-opsin system (HMM) |
