v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | This group contains membrane proteins that are predicted to be transmembrane subunits (EhaH) of multisubunit membrane-bound [NiFe]-hydrogenase Eha complexes.The energy-converting hydrogenase A ( eha) operon encodes a putative multisubunit membrane-bound [NiFe]-hydrogenase Eha in Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133). Sequence analysis of the ehaoperon indicates that it encodes at least 20 proteins, including the [NiFe]-hydrogenase large subunit, the [NiFe]-hydrogenase small subunit, and two broadly conserved integral membrane proteins (one this entry). These four proteins show high sequence similarity to subunits of the Ech hydrogenase from Methanosarcina barkeri, Escherichia coli hydrogenases 3 and 4 (Hyc and Hyf), and CO-induced hydrogenase from Rhodospirillum rubrum (Coo), all of which form a distinct group of multisubunit membrane-bound [NiFe]-hydrogenases (together called hydrogenase-3-type hydrogenases). In addition to these four subunits, the ehaoperon encodes a 6[4Fe-4S] polyferredoxin, a 10[4Fe-4S]polyferredoxin, ten other predicted integral membrane proteins ( , , , , , , , , , ), and four hydrophilic subunits ( , , ) (the latter hydrophilic subunits is a member of well-characterised enzyme family but lack the essential amino acids assumed to form the active site [ ]). All of these proteins are expressed and therefore thought to be functional subunits of the Eha hydrogenase complex []. Note, however, that the ten additional predicted integral membrane proteins are absent from Ech, Coo, Hyc, and Hyf complexes (and therefore from corresponding organisms), indicating that those complexes have a simpler membrane component than Eha [].Members of this group are homologous to the N-terminal domain of EhbF, HyfF of E. coli hydrogenase 4, amongst others. Therefore, this type of membrane subunit of Eha complex is conserved across the various hydrogenase-3-type hydrogenases (that is, they are not limited to the Eha subgroup). A protein with sequence similarity to the C-terminal part of EhbF is not present in the Eha complex (not encoded by the ehaoperon). Based on sequence similarity and genome context analysis, other organisms such as Methanopyrus kandleri,Methanocaldococcus jannaschii, and M. thermoautotrophicum also encode Eha-like [NiFe]-hydrogenase-3-type complexes and have very similar ehaoperon structure. |
| Short Name | NiFe-hyd_3_EhaH_prd |