[FeFe] Group C3-hydrogenase Putative
This entry was last updated at: Feb. 9, 2018, 6:15 a.m.
Properties
| Group | [FeFe]-hydrogenases |
| Subgroup | [FeFe] Group C3: Phosphatase-linked |
| Function | Unconfirmed role. May serve as H2-sensors in regulatory cascades. Enzyme predicted to transfer H2-liberated electrons to PAS domain. Associated redox change may modulate activity of associated serine/threonine phosphatase or AAA-type ATPase domains. Members of this class are co-transcribed with fermentative hydrogenases and appear to regulate their transcription. |
| Activity | H2-sensing? |
| Oxygen tolerance | O2-labile |
| Localisation | Cytosolic |
Distribution
| Ecosystem distribution | Gastrointestinal tracts, anoxic soils and sediments |
| Taxonomic distribution | Widespread in anaerobic bacteria, including Firmicutes, Deltaproteobacteria, and Spirochaete |
Genetic Organisation
Organisation 1: Ruminococcus albus (WP_002849014.1):
Organisation 2: Geobacter sulfurreducens (WP_014552161.1):
Architecture
| Structures |
|
| Subunits | 1 or 3 |
| Subunit description | Organisation 1: HydS (catalytic subunit with PAS domain), HydP (serine/threonine phosphatase), HydT (thioredoxin) Organisation 2: HydS fusion (catalytic subunit with PAS domain fused to AAA-type ATPase domain) |
| Catalytic site | [FeFe]-centre |
| FeS clusters | 2 [4Fe4S] clusters |
Sequences in this class
| NCBI Accession | Organism | Hydrogenase Class | Phylum | Order | Activity (Predicted) | Oxygen Tolerance (Predicted) | Subunits (Predicted) | Metal Centres (Predicted) | Accessory Subunits (Predicted) |
|---|---|---|---|---|---|---|---|---|---|
| WP_029460054.1 | Desulfovibrio alcoholivorans | [FeFe] Group C3 | Deltaproteobacteria | Desulfovibrionales | Sensory | Labile | 3 | [FeFe]-centre, 2 x [4Fe4S] clusters, PAS domain | Phosphatase, thioredoxin |
| WP_029502581.1 | Lachnoclostridium phytofermentans | [FeFe] Group C3 | Firmicutes | Clostridiales | Sensory | Labile | 3 | [FeFe]-centre, 2 x [4Fe4S] clusters, PAS domain | Phosphatase, thioredoxin |
| WP_029918197.1 | Pelobacter seleniigenes | [FeFe] Group C3 | Deltaproteobacteria | Desulfuromonadales | Sensory | Labile | 1 | [FeFe]-centre, 2 x [4Fe4S] clusters, PAS domain | Fusion with transcriptional activator |
Literature
Genetics:
- Calusinska, M., Happe, T., Joris, B., and Wilmotte, A. (2010) The surprising diversity of clostridial hydrogenases: a comparative genomic perspective. Microbiol. 156: 1575-1588.
- Greening, C., Biswas, A., Carere, C.R., Jackson, C.J., Taylor, M.C., Stott, M.B., Cook, G.M., and Morales, S.E. (2016) Genomic and metagenomic surveys of hydrogenase distribution indicate H2 is a widely utilised energy source for microbial growth and survival. ISME J. 10: 761-777.
- Poudel, S., Tokmina-Lukaszewska, M., Colman, D.R., Refai, M., Schut, G.J., King, P.W., Maness, P.C., Adams, M.W., Peters, J.W., Bothner, B., and Boyd, E.S. (2016) Unification of [FeFe]-hydrogenases into three structural and functional groups. BBA Gen. Subj. 1860: 1910-1921.
- Wolf, P.G., Biswas, A., Morales, S.E., Greening, C., and Gaskins, H.R. (2016) H2 metabolism is widespread and diverse among human colonic microbes. Gut Microb. 7: 235-245.
- Søndergaard, D., Petersen, C.N.S., and Greening, C. (2017) HydDB: a web tool for hydrogenase classification and analysis. Sci. Rep. 6: 34212.
- Zheng, Y., Kahnt, J., Kwon, I.H., Mackie, R.I., and Thauer, R.K. (2014) Hydrogen formation and its regulation in Ruminococcus albus: involvement of an electron-bifurcating [FeFe]-hydrogenase, of a non-electron-bifurcating [FeFe]-hydrogenase, and of a putative hydrogen-sensing [FeFe]-hydrogenase. J. Bacteriol. 196: 3840-3852.
Physiology:
- Shaw, A.J., Hogsett, D.A., and Lynd, L.R. (2009) Identification of the [FeFe]-hydrogenase responsible for hydrogen generation in Thermoanaerobacterium saccharolyticum and demonstration of increased ethanol yield via hydrogenase knockout. J. Bacteriol. 191: 6457-6464.
Biochemistry:
- Chongdar, N., Birrell, J.A., Pawlak, K., Sommer, C., Reijerse, E.J., Rüdiger, O., Lubitz, W., and Ogata, H. (2018). Unique spectroscopic properties of the H-cluster in a putative sensory [FeFe] hydrogenase. J. Am. Chem. Soc. 140: 1057-1068.