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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:O59657
Protein Name:EchF
Length:122
Molecular Weight:13542.00
Species:Methanosarcina barkeri [2208]
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate hydron

Cross database links:

Pfam: PF00037   
BioCyc: MetaCyc:MONOMER-12662   

Gene Ontology

GO:0009055 F:electron carrier activity
GO:0051536 F:iron-sulfur cluster binding
GO:0016491 F:oxidoreductase activity
GO:0055114 P:oxidation reduction

References (1)

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

External Searches:

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MGMLNLVLTN ISRKPATRLY PFEIREPFKE FKGRIVFDPE NCILCGLCQK KCPPDAITVT 
61:	KADKTWELNL FRCIMCTECV NGCPKGCLSI SNERAKTGAE EVIKIAVPIV DKPKAPKAAP 
121:	SK