Protein Family Models

This family contains sequences that are similar to the fatty acid metabolism regulator protein (FadR, Swiss:P09371). This functions as a dimer, with each monomer being composed of an N-terminal DNA-binding domain and a regulatory C-terminal domain. A linker comprising two short alpha helices joins the two domains. In the C-terminal domain, an antiparallel array of six alpha helices forms a barrel-like structure, while a seventh alpha helix forms a 'lid' at the end closest to the N-terminal domain. This structure was found to be similar to that of the C-terminal domain of the Tet repressor. Long-chain acyl-CoA thioesters interact directly and reversibly with the C-terminal domain, and this interaction affects the structure and therefore the DNA binding properties of the N-terminal domain [1]. [1]. 11279025. The FadR.DNA complex. Transcriptional control of fatty acid metabolism in Escherichia coli. Xu Y, Heath RJ, Li Z, Rock CO, White SW;. J Biol Chem 2001;276:17373-17379. (from Pfam)

Date:

2024-10-16

This domain is the C-terminal ligand binding domain of many members of the GntR family. This domain binds to a range of effector molecules, including Lactate, Zn(II), Ni(II), Ca(II), Mg(II), citrate, sugar acids, sialic acid and N-acetylglucosamine-6-P, that regulate the transcription of genes through the action of the N-terminal DNA-binding domain Pfam:PF00392 (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). This domain is found in Swiss:P45427 and Swiss:P31460 that are regulators of sugar biosynthesis operons. It is also in the known structure of FadR where it binds to acyl-coA, the domain is alpha helical [1]. This family has been named as FCD for (FadR C-terminal Domain). [1]. 11013219. Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold. van Aalten DM, DiRusso CC, Knudsen J, Wierenga RK;. EMBO J 2000;19:5167-5177. (from Pfam)

Date:

2024-10-16

This family of regulatory proteins consists of the N-terminal HTH region of GntR-like bacterial transcription factors. At the C-terminus there is usually an effector-binding/oligomerisation domain. The GntR-like proteins include the following sub-families: MocR, YtrR, FadR, AraR, HutC and PlmA, DevA, DasR [1-2][4][5]. Many of these proteins have been shown experimentally to be autoregulatory, enabling the prediction of operator sites and the discovery of cis/trans relationships [3]. The DasR regulator has been shown to be a global regulator of primary metabolism and development in Streptomyces coelicolor [5]. [1]. 12867439. PlmA, a new member of the GntR family, has plasmid maintenance functions in Anabaena sp. strain PCC 7120. Lee MH, Scherer M, Rigali S, Golden JW;. J Bacteriol 2003;185:4315-4325. [2]. 11756427. Subdivision of the helix-turn-helix GntR family of bacterial regulators in the FadR, HutC, MocR, and YtrA subfamilies. Rigali S, Derouaux A, Giannotta F, Dusart J;. J Biol Chem 2002;277:12507-12515. [3]. 15247334. Extending the classification of bacterial transcription factors beyond the helix-turn-helix motif as an alternative approach to discover new cis/trans relationships. Rigali S, Schlicht M, Hoskisson P, Nothaft H, Merzbacher M, Joris B, Titgemeyer F;. Nucleic Acids Res 2004;32:3418-3426. [4]. 16936034. A new GntR family transcriptional regulator in streptomyces coelicolor is required for morphogenesis and antibiotic production and controls transcription of an ABC transporter in response to carbon source. Hillerich B, Westpheling J;. J Bacteriol. 2006;188:7477-7487. [5]. 16925557. The sugar phosphotransfer. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

fatty acid metabolism regulator is a dimeric acyl coenzyme A binding protein and GntR family transcription factor that regulates the expression of genes encoding fatty acid biosynthetic and degrading enzymes

Date:

2017-02-03

Multifunctional regulator of fatty acid metabolism

Gene:

fadR

Date:

2021-10-20

Members of this family are FadR, a transcriptional regulator of fatty acid metabolism, including both biosynthesis and beta-oxidation. It is found exclusively in a subset of Gammaproteobacteria, with strictly one copy per genome. It has an N-terminal DNA-binding domain and a less well conserved C-terminal long chain acyl-CoA-binding domain. FadR from this family heterologously expressed in Escherichia coli show differences in regulatory response and fatty acid binding profiles. The family is nevertheless designated equivalog, as all member proteins have at least nominally the same function.

Gene:

fadR

Date:

2024-05-13