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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
1998-2-10
|
| pubmed:databankReference | |
| pubmed:abstractText |
The nucleotide sequence has been determined for a twelve-gene operon of Escherichia coli designated the hyf operon (hyfABCDEFGHIR-focB). The hyf operon is located at 55.8-56.0 min and encodes a putative nine-subunit hydrogenase complex (hydrogenase four or Hyf), a potential formate- and sigma 54-dependent transcriptional activator, HyfR (related to FhlA), and a possible formate transporter, FocB (related to FocA). Five of the nine Hyf-complex subunits are related to subunits of both the E. coli hydrogenase-3 complex (Hyc) and the proton-translocating NADH:quinone oxidoreductases (complex I and Nuo), whereas two Hyf subunits are related solely to NADH:quinone oxidoreductase subunits. The Hyf components include a predicted 523 residue [Ni-Fe] hydrogenase (large subunit) with an N-terminus (residues 1-170) homologous to the 30 kDa or NuoC subunit of complex I. It is proposed that Hyf, in conjunction with formate dehydrogenase H (Fdh-H), forms a hitherto unrecognized respiration-linked proton-translocating formate hydrogenlyase (FHL-2). It is likely that HyfR acts as a formate-dependent regulator of the hyf operon and that FocB provides the Hyf complex with external formate as substrate.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Formate Dehydrogenases,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Protons,
http://linkedlifedata.com/resource/pubmed/chemical/formate hydrogenlyase
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| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
1350-0872
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
143 ( Pt 11)
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
3633-47
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| pubmed:dateRevised |
2010-8-25
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| pubmed:meshHeading |
pubmed-meshheading:9387241-Amino Acid Sequence,
pubmed-meshheading:9387241-Bacterial Proteins,
pubmed-meshheading:9387241-Escherichia coli,
pubmed-meshheading:9387241-Formate Dehydrogenases,
pubmed-meshheading:9387241-Genes, Bacterial,
pubmed-meshheading:9387241-Hydrogenase,
pubmed-meshheading:9387241-Membrane Proteins,
pubmed-meshheading:9387241-Models, Chemical,
pubmed-meshheading:9387241-Molecular Sequence Data,
pubmed-meshheading:9387241-Multienzyme Complexes,
pubmed-meshheading:9387241-Open Reading Frames,
pubmed-meshheading:9387241-Operon,
pubmed-meshheading:9387241-Protein Structure, Secondary,
pubmed-meshheading:9387241-Protons,
pubmed-meshheading:9387241-Restriction Mapping,
pubmed-meshheading:9387241-Sequence Alignment,
pubmed-meshheading:9387241-Sequence Analysis, DNA,
pubmed-meshheading:9387241-Sequence Homology, Amino Acid
|
| pubmed:year |
1997
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| pubmed:articleTitle |
A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system.
|
| pubmed:affiliation |
Krebs Institute, Department of Molecular Biology & Biotechnology, University of Sheffield, UK. s.andrews@sheffield.ac.uk
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|