Summary: Formate dehydrogenase N, transmembrane
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Formate dehydrogenase Edit Wikipedia article
|Formate dehydrogenase N, transmembrane|
Formate dehydrogenases are a set of enzymes that catalyse the oxidation of formate to carbon dioxide, donating the electrons to a second substrate, such as NAD+ in formate:NAD+ oxidoreductase (EC 220.127.116.11) or to a cytochrome in formate:ferricytochrome-b1 oxidoreductase (EC 18.104.22.168).
NAD-dependent formate dehydrogenases are important in methylotrophic yeast and bacteria and are vital in the catabolism of C1 compounds such as methanol. The cytochrome-dependent enzymes are more important in anaerobic metabolism in prokaryotes. For example, in E. coli, the formate:ferricytochrome-b1 oxidoreductase is an intrinsic membrane protein with two subunits and is involved in anaerobic nitrate respiration.
Formate + NAD+ â†” CO2 + NADH + H+
Formate + 2 ferricytochrome b1 â†” CO2 + 2 ferrocytochrome b1 + 2 H+
Molybdopterin, molybdenum and selenium dependence
The transmembrane domain of the beta subunit of formate dehydrogenase consists of a single transmembrane helix. This domain acts as a transmembrane anchor, allowing the conduction of electrons within the protein.
- Formate dehydrogenase (cytochrome)
- Formate dehydrogenase (cytochrome-c-553)
- Formate dehydrogenase (NADP+)
- Microbial metabolism
- Ferry JG (1990). "Formate dehydrogenase". FEMS Microbiol. Rev. 7 (3â€“4): 377â€“82. PMID 2094290.
- Popov VO, Lamzin VS (1994). "NAD(+)-dependent formate dehydrogenase". Biochem. J. 301 (3): 625â€“43. PMC 1137035. PMID 8053888.
- Jormakka M, Byrne B, Iwata S (2003). "Formate dehydrogenase--a versatile enzyme in changing environments". Curr. Opin. Struct. Biol. 13 (4): 418â€“23. doi:10.1016/S0959-440X(03)00098-8. PMID 12948771.
- Graham A, Boxer DH (1981). "The organization of formate dehydrogenase in the cytoplasmic membrane of Escherichia coli". Biochem. J. 195 (3): 627â€“37. PMC 1162934. PMID 7032506.
- Ruiz-Herrera J, DeMoss JA (1969). "Nitrate reductase complex of Escherichia coli K-12: participation of specific formate dehydrogenase and cytochrome b1 components in nitrate reduction". J. Bacteriol. 99 (3): 720â€“9. PMC 250087. PMID 4905536.
- Khangulov SV, Gladyshev VN, Dismukes GC, Stadtman TC (1998). "Selenium-Containing Formate Dehydrogenase H from Escherichia coli: A Molybdopterin Enzyme That Catalyzes Formate Oxidation without Oxygen Transfer". Biochemistry 37 (10): 3518â€“3528. doi:10.1021/bi972177k. PMID 9521673.
- Jormakka M, TÃ¶rnroth S, Byrne B, Iwata S (2002). "Molecular basis of proton motive force generation: structure of formate dehydrogenase-N". Science 295 (5561): 1863â€“1868. doi:10.1126/science.1068186. PMID 11884747.
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Formate dehydrogenase N, transmembrane Provide feedback
Members of this family are predominantly found in the beta subunit of formate dehydrogenase, and consist of a single transmembrane helix. They act as a transmembrane anchor, and allow for conduction of electrons within the protein .
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This tab holds annotation information from the InterPro database.
InterPro entry IPR015246
The transmembrane domain of the beta subunit of formate dehydrogenase consists of a single transmembrane helix. This domain acts as a transmembrane anchor, allowing the conduction of electrons within the protein [PUBMED:11884747].
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|Number in seed:||62|
|Number in full:||6893|
|Average length of the domain:||44.00 aa|
|Average identity of full alignment:||67 %|
|Average coverage of the sequence by the domain:||14.79 %|
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build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Form-deh_trans domain has been found. There are 2 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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