F
IPR011305

Predicted [NiFe]-hydrogenase-3-type complex Eha, membrane protein EhaL

InterPro entry
Short namePrd_NiFe_hyd_3_EhaL
family relationships

Description

[NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions [NiFe] hydrogenases consist of two subunits, hydrogenase large and hydrogenase small. The large subunit contains the binuclear [NiFe] active site, while the small subunit binds at least one [4Fe-4S] cluster
[1]
.

Energy-converting [NiFe] hydrogenases (or [NiFe]-hydrogenase-3-type) form a distinct group within the [NiFe] hydrogenase family
[2, 3, 5]
. Members of this subgroup include:


 * Hydrogenase 3 and 4 (Hyc and Hyf) from Escherichia coli
 * CO-induced hydrogenase (Coo) from Rhodospirillum rubrum
 * Mbh hydrogenase from Pyrococcus furiosus
 * Eha and Ehb hydrogenases from Methanothermobacter species
 * Ech hydrogenase from Methanosarcina barkeri


Energy-converting [NiFe] hydrogenases are membrane-bound enzymes with a six-subunit core: the large and small hydrogenase subunits, plus two hydrophilic proteins and two integral membrane proteins. Their large and small subunits show little sequence similarity to other [NiFe] hydrogenases, except for key conserved residues coordinating the active site and [FeS] cluster. However, they show considerable sequence similarity to the six-subunit, energy-conserving NADH:quinone oxidoreductases (complex I), which are present in cytoplasmic membranes of many bacteria and in inner mitochondrial membranes. However, the reactions they catalyse differ significantly from complex I. Energy-converting [NiFe] hydrogenases function as ion pumps.

Eha and Ehb hydrogenases contain extra subunits in addition to those shared by other energy-converting [NiFe] hydrogenases (or [NiFe]-hydrogenase-3-type). Eha contains a 6[4Fe-4S] polyferredoxin, a 10[4F-4S] polyferredoxin, ten other predicted integral membrane proteins (EhaA
IPR011306
, EhaB
IPR011314
, EhaC
IPR011316
, EhaD
IPR011308
, EhaE
IPR011317
, EhaF
IPR011313
, EhaG
IPR011311
, EhaI
IPR011318
, EhaK
IPR011319
, EhaL
IPR019211
and
IPR011305
) and four hydrophilic subunits (EhaM, EhaR, EhS, EhT)
[4, 5]
. The ten predicted integral membrane proteins are absent from Ech, Coo, Hyc and Hyf complexes, which may have simpler membrane components than Eha. Eha and Ehb catalyse the reduction of low-potential redox carriers (e.g. ferredoxins or polyferredoxins), which then might function as electron donors to oxidoreductases.

Based on sequence similarity and genome context analysis, other organisms such as Methanopyrus kandleri, Methanocaldococcus jannaschii, and Methanothermobacter marburgensis also encode Eha-like [NiFe]-hydrogenase-3-type complexes and have very similarehaoperon structure.

This entry represents small membrane proteins that are predicted to be the EhaL transmembrane subunits of multisubunit membrane-bound [NiFe]-hydrogenase Eha complexes.

References

1.Molecular biology of microbial hydrogenases. Vignais PM, Colbeau A. 6, 159-88, (2004). PMID: 15119826

2.Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I. Hedderich R. J. Bioenerg. Biomembr. 36, 65-75, (2004). View articlePMID: 15168611

3.Energy-converting [NiFe] hydrogenases: more than just H2 activation. Hedderich R, Forzi L. J. Mol. Microbiol. Biotechnol. 10, 92-104, (2005). View articlePMID: 16645307

4.Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins. Tersteegen A, Hedderich R. Eur. J. Biochem. 264, 930-43, (1999). View articlePMID: 10491142

5.Essential anaplerotic role for the energy-converting hydrogenase Eha in hydrogenotrophic methanogenesis. Lie TJ, Costa KC, Lupa B, Korpole S, Whitman WB, Leigh JA. Proc Natl Acad Sci U S A 109, 15473-8, (2012). PMID: 22872868

Contributing Member Database Entry
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.