Protein Family Models for Protein (Select 496664115) - Protein Family Models

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Links from Protein

Items: 8

Select item 4280551.

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)

Date:: 2024-10-16

Family Accession:: NF039346.4
Method:: HMM

Select item 4117912.

MBL fold metallo-hydrolase

Date:: 2024-08-14

Family Accession:: NF012955.5
Method:: HMM

Select item 4112563.

flavodoxin domain-containing protein

GO Terms:

Molecular Function:: FMN binding (GO:0010181)

Date:: 2024-08-14

Family Accession:: NF012481.5
Method:: HMM

Select item 4072054.

new record, indexing in progress

Family Accession:

Select item 3882625.

new record, indexing in progress

Family Accession:

Select item 3882236.

new record, indexing in progress

Family Accession:

Select item 3466957.

new record, indexing in progress

Family Accession:

Select item 919118.

FprA family A-type flavoprotein

FprA family A-type flavoprotein contains an MBL fold metallo-hydrolase domain having a binuclear iron center, and a flavodoxin-like domain containing one FMN moiety; similar to Desulfovibrio gigas rubredoxin-oxygen oxidoreductase, which catalyzes the four-electron reduction of one oxygen molecule to two water molecules