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5.A.3.5.1
Thiosulfate reductase, PhsABC (Heinzinger et al., 1995) (Clark and Barrett 1987). Menaquinone is the sole electron donor. The endoergonic reduction reaction is driven by the pmf by a reverse loop mechanism (Stoffels et al. 2012). The enzyme can catalyze oxidation of sulfide to sulfite and sulfite to thiosulfate in an exergonic reaction that is pmf-independent (Stoffels et al. 2012). Because the endoergonic reaction is dependent on the pmf, there may be a proton channels in the complex, (possibly subunit C) that allows proton flux into the cell, coupled to the reduction reaction.

Accession Number:P0A1I1
Protein Name:Thiosulfate reductase electron transport protein PhsB
Length:192
Molecular Weight:21320.00
Species:Salmonella typhimurium [90371]
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate electron

Cross database links:

RefSeq: NP_461009.1   
Entrez Gene ID: 1253585   
Pfam: PF00037   
BioCyc: MetaCyc:MONOMER-12542    STYP99287:STM2064-MONOMER   
KEGG: stm:STM2064   

Gene Ontology

GO:0051539 F:4 iron, 4 sulfur cluster binding
GO:0009055 F:electron carrier activity
GO:0046872 F:metal ion binding
GO:0022900 P:electron transport chain
GO:0006810 P:transport

References (3)

[1] “Sequence analysis of the phs operon in Salmonella typhimurium and the contribution of thiosulfate reduction to anaerobic energy metabolism.”  Heinzinger N.K.et.al.   7751291
[2] “Cloning and characterization of a gene cluster, phsBCDEF, necessary for the production of hydrogen sulfide from thiosulfate by Salmonella typhimurium.”  Alami N.et.al.   7737516
[3] “Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.”  McClelland M.et.al.   11677609

External Searches:

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FASTA formatted sequence
1:	MNHLTNQYVM LHDEKRCIGC QACTVACKVL NDVPEGFSRV QVQIRAPEQA SNALTHFQFV 
61:	RVSCQHCENA PCVSVCPTGA SYRDENGIVQ VDKSRCIGCD YCVAACPFHV RYLNPQTGVA 
121:	DKCNFCADTR LAAGQSPACV SVCPTDALKF GRLDESEIQR WVGQKEVYRQ QEARSGAVSL 
181:	YRRKEVHQEG KA