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3.D.1.4.2
[Ni2+-4Fe-4S] H+ translocating, quinone-independent ferredoxin:H+ oxidoreductase, EchA-F (Hedderich and Forzi, 2005; Künkel et al., 1998; Welte and Deppenmeier 2013) The Ech hydrogenases of M. mazei and M. barkeri have been characterized and were shown to pump protons (Welte et al., 2010).  The EchC and EcnF subunits include [Fe4S4] centers, and that in the EchC subunit exhibits a pH dependency to suggest that it plays a role in proton pumping (Forzi et al. 2005).  EchE has the NiFe center that converts 2H+ to H2.  The transmembrane subuits are EchA and EchB (Welte and Deppenmeier 2013) The Ech hydrogenases of M. mazei and M. barkeri have been characterized and were shown to pump protons (Welte et al., 2010).  The EchC and EcnF subunits include [Fe4S4] centers, and that in the EchC subunit exhibits a pH dependency to suggest that it plays a role in proton pumping (Forzi et al. 2005).  EchE has the NiFe center that converts 2H+ to H2.  The transmembrane subuits are EchA and EchB (Welte and Deppenmeier 2013).

Accession Number:O59655
Protein Name:EchD
Length:113
Molecular Weight:12981.00
Species:Methanosarcina barkeri [2208]
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate hydron

Cross database links:

Pfam: PF00329   
BioCyc: MetaCyc:MONOMER-12660   

Gene Ontology

GO:0008137 F:NADH dehydrogenase (ubiquinone) activity
GO:0055114 P:oxidation reduction

References (1)

[1] “An Escherichia coli hydrogenase-3-type hydrogenase in methanogenic archaea.”  Kunkel A.et.al.   9546662

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MLENEVEIKN SDELLKTVEG LKNDGYRNVT MICLKANEGH EFIYVFEKDY QLKNLRYFLK 
61:	PGEKPKSISG IYLCALLIEN EYQDLFGLTF EGLAIDYKGH LYLTPNSPKA PLA