Summary: Oxidoreductase NAD-binding domain
This is the Wikipedia entry entitled "Oxidoreductase NAD-binding domain". More...
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Oxidoreductase NAD-binding domain Edit Wikipedia article
Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.
Bacterial ferredoxin-NADP+ reductase may be bound to the thylakoid membrane or anchored to the thylakoid-bound phycobilisomes. Chloroplast ferredoxin-NADP+ reductase (EC 188.8.131.52) may play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power. It is involved in the final step in the linear photosynthetic electron transport chain and has also been implicated in cyclic electron flow around photosystem I where its role would be to return electrons from ferredoxin to the cytochrome B-F complex.
This domain is present in a variety of proteins that include, bacterial flavohemoprotein, mammalian NADH-cytochrome b5 reductase, eukaryotic NADPH-cytochrome P450 reductase, nitrate reductase from plants, nitric-oxide synthase, bacterial vanillate demethylase and others.
Human genes encoding proteins containing this domain include:
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Oxidoreductase NAD-binding domain Provide feedback
Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.
Hyde GE, Crawford NM, Campbell W; , J Biol Chem 1991;266:23542-23547.: The sequence of squash NADH:nitrate reductase and its relationship to the sequences of other flavoprotein oxidoreductases. A family of flavoprotein pyridine nucleotide cytochrome reductases. PUBMED:1748631 EPMC:1748631
Internal database links
|Similarity to PfamA using HHSearch:||NAD_binding_6|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001433
Bacterial ferredoxin-NADP+ reductase may be bound to the thylakoid membrane or anchored to the thylakoid-bound phycobilisomes. Chloroplast ferredoxin-NADP+ reductase (EC) may play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power. It is involved in the final step in the linear photosynthetic electron transport chain and has also been implicated in cyclic electron flow around photosystem I where its role would be to return electrons from ferredoxin to the cytochrome B-F complex.
This domain is present in a variety of proteins that include, bacterial flavohemoprotein, mammalian NADH-cytochrome b5 reductase, eukaryotic NADPH-cytochrome P450 reductase, nitrate reductase from plants, nitric-oxide synthase, bacterial vanillate demethylase, as well as others.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||oxidoreductase activity (GO:0016491)|
|Biological process||oxidation-reduction process (GO:0055114)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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We make a range of alignments for each Pfam-A family:
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Key: available, not generated, — not available.
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Curation and family details
|Previous IDs:||oxidored_fad; NAD_binding;|
|Number in seed:||72|
|Number in full:||19747|
|Average length of the domain:||105.10 aa|
|Average identity of full alignment:||20 %|
|Average coverage of the sequence by the domain:||24.44 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||16|
|Download:||download the raw HMM for this family|
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There are 7 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 NAD_binding_1 domain has been found. There are 191 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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