Protein Family Models

Hydrogen gas-evolving membrane-bound hydrogenase (MBH) is a respiratory complex homologous to the quinone-reducing Complex I. Like Complex I, MBH has peripheral and membrane arms. MBH is made of 14 subunits (MbhA-N). MbhJ, K, L, N and M form the Membrane-anchored hydrogenase module. MbhJ, K, L, N are predicted to be exposed to the cytoplasm and form the peripheral arm. The remaining 10 subunits are predicted to be integral membrane proteins forming the membrane arm, made of 44 transmembrane helices (TMH) [2, 3]. MbhA, B, C and F form the Sodium translocation module. MbhD, E, G and H form the Proton translocation module. MbhI is the linker between the hydrogenase module and the proton-translocating membrane module. It anchors the discontinuous TMH7 of MbhH via its middle lateral helix and the C-terminal of TMH2, found in MbhE. MbhD and MbhE together are equivalent to Nqo10 of Complex I [1]. MbhE has two transmembrane helices: TMH1 and TMH2. Paper describing PDB structure 6cfw. [1]. 29754813. Structure of an Ancient Respiratory System. Yu H, Wu CH, Schut GJ, Haja DK, Zhao G, Peters JW, Adams MWW, Li H;. Cell. 2018;173:1636-1649. [2]. 22713092. The modular respiratory complexes involved in hydrogen and sulfur metabolism by heterotrophic hyperthermophilic archaea and their evolutionary implications. Schut GJ, Boyd ES, Peters JW, Adams MW;. FEMS Microbiol Rev. 2013;37:182-203. [3]. 26808919. The role of geochemistry and energetics in the evolution of modern respiratory complexes from a proton-reducing ancestor. Schut GJ, Zadvornyy O, Wu CH, Peters JW, Boyd ES, Adams MW;. Biochim Biophys Acta. 2016;1857:958-970. (from Pfam)

Gene:

mbhE

Date:

2024-10-16

Hydrogen gas-evolving membrane-bound hydrogenase (MBH) is a respiratory complex homologous to the quinone-reducing Complex I. Like Complex I, MBH has peripheral and membrane arms. MBH is made of 14 subunits (MbhA-N). MbhJ, K, L, N and M form the Membrane-anchored hydrogenase module. MbhJ, K, L, N are predicted to be exposed to the cytoplasm and form the peripheral arm. The remaining 10 subunits are predicted to be integral membrane proteins forming the membrane arm, made of 44 transmembrane helices (TMH) [2, 3]. MbhA, B, C and F form the Sodium translocation module. MbhD, E, G and H form the Proton translocation module. MbhI is the linker between the hydrogenase module and the proton-translocating membrane module. It anchors the discontinuous TMH7 of MbhH via its middle lateral helix and the C-terminal of TMH2, found in MbhE. MbhD and MbhE together are equivalent to Nqo10 of Complex I [1]. MbhD has three TM helices. Paper describing PDB structure 6cfw. [1]. 29754813. Structure of an Ancient Respiratory System. Yu H, Wu CH, Schut GJ, Haja DK, Zhao G, Peters JW, Adams MWW, Li H;. Cell. 2018;173:1636-1649. [2]. 33229520. Structure of the Dietzia Mrp complex reveals molecular mechanism of this giant bacterial sodium proton pump. Li B, Zhang K, Nie Y, Wang X, Zhao Y, Zhang XC, Wu XL;. Proc Natl Acad Sci U S A. 2020;117:31166-31176. [3]. 32735215. Structure and mechanism of the Mrp complex, an ancient cation/proton antiporter. Steiner J, Sazanov L;. Elife. 2020; [Epub ahead of print] (from Pfam)

Date:

2024-10-16

Possible subunit of Na+/H+ antiporter [1], [2]. Predicted integral membrane protein, usually four transmembrane regions in this domain. Often found in bacterial NADH dehydrogenase subunit. [1]. 9852009. A putative multisubunit Na+/H+ antiporter from Staphylococcus aureus. Hiramatsu T, Kodama K, Kuroda T, Mizushima T, Tsuchiya T;. J Bacteriol 1998;180:6642-6648. [2]. 11356194. Mrp-dependent Na(+)/H(+) antiporters of Bacillus exhibit characteristics that are unanticipated for completely secondary active transporters. Ito M, Guffanti AA, Krulwich TA;. FEBS Lett 2001;496:117-120. (from Pfam)

Date:

2024-10-16

Members of this family include multiple membrane-spanning proteins associated with proton translocation. These include NADH ubiquinone oxidoreductase subunits NuoL, NuoN, and NuoM, hydrogenase components HyfB, HyfD, and HyfF, as well as subunits of carbon monoxide dehydrogenase, F420 dehydrogenase, etc, as well as Na+/H+ antiporter subunits.

Date:

2024-10-16

This sub-family represents an amino terminal extension of Pfam:PF00361. Only NADH-Ubiquinone chain 5 and eubacterial chain L are in this family. This sub-family is part of complex I which catalyses the transfer of two electrons from NADH to ubiquinone in a reaction that is associated with proton translocation across the membrane. [1]. 1470679. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Walker JE;. Q Rev Biophys 1992;25:253-324. (from Pfam)

Date:

2024-10-16

monovalent cation/H+ antiporter subunit A similar to Sinorhizobium meliloti K(+)/H(+) antiporter subunit A/B, part of a K(+) efflux system which is required for the adaptation of R. meliloti to alkaline pH as well as for the infection process during symbiotic nodule development

Date:

2017-08-11

Part of an antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali

Date:

2022-12-21