| http://purl.uniprot.org/citations/9387241 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9387241 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9387241 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.org/dc/terms/identifier | "doi:10.1099/00221287-143-11-3633"xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.org/dc/terms/identifier | "doi:10.1099/00221287-143-11-3633"xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/author | "Golby P."xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/author | "Golby P."xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/author | "Quail M.A."xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/author | "Quail M.A."xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/author | "Andrews S.C."xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/author | "Andrews S.C."xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/author | "Guest J.R."xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/author | "Guest J.R."xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/author | "Berks B.C."xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/author | "Berks B.C."xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/author | "Ambler A."xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/author | "Ambler A."xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/author | "McClay J."xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/author | "McClay J."xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/name | "Microbiology"xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/name | "Microbiology"xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/pages | "3633-3647"xsd:string |
| http://purl.uniprot.org/citations/9387241 | http://purl.uniprot.org/core/pages | "3633-3647"xsd:string |