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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:O59653
Protein Name:EchB
Length:285
Molecular Weight:31692.00
Species:Methanosarcina barkeri [2208]
Number of TMSs:8
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate hydron

Cross database links:

Pfam: PF00146   
BioCyc: MetaCyc:MONOMER-12658   

Gene Ontology

GO:0016020 C:membrane
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:	MNDILTIILV LIGAPIIGCL ASGIDRKITA RLQGRVGPPL LQPYYDVKKL LSKDNMVVNP 
61:	SQNFYVVVYL AFIILSLFML VFKQDFLMII FVYTVASVAL VVGGMSTGSP YARIGSSREI 
121:	MAILSYEPVL ILYALAIYLL TGTFKLSALL DASSPLLMYT PLIFIAMIVV LNIKLKKSPF 
181:	DYSTSHHGHQ ELIKGMTTEY GGPGFATIEI AHFYEYVFLT GLIFLFWAST PVIGVLIGII 
241:	AYLLVIVIDN ITARVYWQWM LKLSWTILLV ISLVNIDTCT LVESN