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3.D.1.4.3
Carbon monoxide-induced, H+ translocating, quinone-independent, polyferredoxin (CooF):H+ oxidoreductase, H2ase (Fox et al., 1996a,b; Hedderich and Forzi, 2005) [oxidation of CO to CO2 by CO dehydrogenase results in transfer of electrons to polyferredoxin which reduces H2ase] (Soboh et al., 2002, 2004).

Accession Number:P31895
Protein Name:CooH
Length:361
Molecular Weight:40280.00
Species:Rhodospirillum rubrum [1085]
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate hydron

Cross database links:

Pfam: PF00346    PF00374   

Gene Ontology

GO:0008901 F:ferredoxin hydrogenase activity
GO:0051287 F:NAD or NADH binding
GO:0016151 F:nickel ion binding
GO:0016651 F:oxidoreductase activity, acting on NADH or ...
GO:0048038 F:quinone binding
GO:0055114 P:oxidation reduction

References (2)

[1] “Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme.”  Fox J.D.et.al.   8626276
[2] “Genetic and physiological characterization of the Rhodospirillum rubrum carbon monoxide dehydrogenase system.”  Kerby R.L.et.al.   1644755

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSTYTIPVGP LHVALEEPMY FRIEVDGEKV VSVDITAGHV HRGIEYLATK RNIYQNIVLT 
61:	ERVCSLCSNS HPQTYCMALE SITGMVVPPR AQYLRVIADE TKRVASHMFN VAILAHIVGF 
121:	DSLFMHVMEA REIMQDTKEA VFGNRMDIAA MAIGGVKYDL DKDGRDYFIG QLDKLEPTLR 
181:	DEIIPLYQTN PSIVDRTRGI GVLSAADCVD YGLMGPVARG SGHAYDVRKQ APYAVYDRLD 
241:	FEMALGEHGD VWSRAMVRWQ EALTSIGLIR QCLRDMPDGP TKAGPVPPIP AGEAVAKTEA 
301:	PRGELIYYLK TNGTDRPERL KWRVPTYMNW DALNVMMAGA RISDIPLIVN SIDPCISCTE 
361:	R