| Primary Identifier | IPR019919 | Type | Family |
| Short Name | Lucif-like_OxRdtase_MSMEG_2256 |
| description | Bacterial luciferase is a flavin monooxygenase that catalyses the oxidation of long-chain aldehydes and releases energy in the form of visible light, and which uses flavin as a substrate rather than a cofactor []. Bacterial luciferase is an alpha/beta (LuxA/LuxB) heterodimer, where each individual subunit folds into a single TIM (beta/alpha)8-barrel domain. There are structural similarities between bacterial luciferase and nonfluorescent flavoproteins (LuxF, FP390), alkanesulphonate monooxygenase (SsuD), and coenzyme F420-dependent terahydromethanopterin reductase, which make up clearly related families with somewhat different folds [, , ].F420 is a flavin derivative that functions as a redox coenzyme in methanogenic archaea, Mycobacterium tuberculosis and related species, Colwellia psychrerythraea (strain 34H / ATCC BAA-681), Rhodopseudomonas palustris (strain HaA2), amongst others. A number of luciferase-like protein subfamilies appear only in F420-positive genomes and are likely to be F420-dependent oxidoreductases. This entry represents one such subfamily, exemplified by MSMEG_2256 from Mycobacterium smegmatis. |
