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ODP family beta lactamase
The ODP (Oxygen-binding Di-iron Protein) domain is a distinct member of the metallo-beta-lactamase superfamily recruited to various bacterial and archaeal signal transduction pathways, including chemotaxis, to function as oxygen and iron sensors (1). ODP was shown to act as a sensor for chemotactic responses to both iron and oxygen in the human pathogen Treponema denticola (Td). The ODP di-iron site binds oxygen at high affinity to reversibly form an unusually stable peroxo adduct. [1]. 31270241. A di-iron protein recruited as an Fe[II] and oxygen sensor for bacterial chemotaxis functions by stabilizing an iron-peroxy species. Muok AR, Deng Y, Gumerov VM, Chong JE, DeRosa JR, Kurniyati K, Coleman RE, Lancaster KM, Li C, Zhulin IB, Crane BR;. Proc Natl Acad Sci U S A. 2019;116:14955-14960. (from Pfam)
MBL fold metallo-hydrolase
flavodoxin domain-containing protein
rubredoxin
anaerobic nitric oxide reductase flavorubredoxin
anaerobic nitric oxide reductase flavorubredoxin is involved in nitric oxide detoxification as part of bacterial defense mechanisms against reactive nitrogen species; a FprA family A-type flavoprotein
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