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).
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Accession Number: | O59652 |
Protein Name: | EchA |
Length: | 639 |
Molecular Weight: | 68696.00 |
Species: | Methanosarcina barkeri [2208] |
Number of TMSs: | 19 |
Location1 / Topology2 / Orientation3: |
Membrane1 / Multi-pass membrane protein2 |
Substrate |
hydron |
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1: MIENTVMLLI IVPLLFSLLF VALPKSLYRY LAWAFFIIGV ALSVSLVLGG TGVVPVEGPN
61: FAMYENIVLL LEVLVILYIL AVSAKYKNWP TLGLGIISAA LFAYTYANVP GAEGASFNID
121: PLAQLMILIV NIVGTAIILF ATGYMDQYEE HRHLNRQKIF YFTMSFFLAA MNGLVMSDTL
181: GWLYLFWELT TLCSFVLISY NMDEEGINNG FRALSLNLVG GVAMSIGIIL LATNYNISSL
241: TGIATYAGTD AVALAALALP VALLCIGGFA KSAQMPFHSW LLGAMVAPTP VSALLHSSTM
301: VNAGVFLVVK LVPAYANTSL GTAIAVYGSF TFVICSALAL SQRNAKRVLA YSTIANLGLI
361: IASAGIGTPL AVAASMMLIL FHAISKGLLF LCTGEIEHTI GSRDIEDMSG LIKKAPLLTS
421: IAALGMVSML LPPFGVLLTK WVSMEAASNN PVVIIFIVLG SALTTVYYSK WLGTILSTSM
481: DKNAVPHKKL ETYFPLSVLG LSIIGTSIFI FSIYDYFIRP QVEILLKVAP AVTGQAGQFT
541: SEIGAFAYAA IFAVLALAIL IYLATKNMFT PRTAGYYMCG ENNLEKDRLM FRNGLCSYEK
601: CSVSNIYLQN IFGESKLTTF GYAISIILIV IALAGGVGL