Summary: FAD binding domain
This is the Wikipedia entry entitled "Flavoprotein pyridine nucleotide cytochrome reductases". More...
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Flavoprotein pyridine nucleotide cytochrome reductases Edit Wikipedia article
|FAD binding domain|
Flavoprotein pyridine nucleotide cytochrome reductases catalyse the interchange of reducing equivalents between one-electron carriers and the two-electron-carrying nicotinamide dinucleotides. The enzymes include ferredoxin-NADP+ reductases, plant and fungal NAD(P)H:nitrate reductases, cytochrome b5 reductases, cytochrome P450 reductases, sulphite reductases, nitric oxide synthases, phthalate dioxygenase reductase, and various other flavoproteins.
 Human proteins containing this domain
- Hyde GE, Crawford NM, Campbell WH (1991). "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". J. Biol. Chem. 266 (35): 23542–23547. PMID 1748631.
- Karplus PA, Bruns CM (1994). "Structure-function relations for ferredoxin reductase". J. Bioenerg. Biomembr. 26 (1): 89–99. doi:10.1007/BF00763221. PMID 8027025.
- Siverio JM (2002). "Assimilation of nitrate by yeasts". FEMS Microbiol. Rev. 26 (3): 277–284. doi:10.1111/j.1574-6976.2002.tb00615.x. PMID 12165428.
- Iwanaga S, Miyata T, Yubisui T, Tamura M, Takeshita M (1986). "Complete amino acid sequence of NADH-cytochrome b5 reductase purified from human erythrocytes". J. Biochem. 99 (2): 407–422. PMID 3700359.
- Porter TD (1991). "An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals". Trends Biochem. Sci. 16 (4): 154–158. doi:10.1016/0968-0004(91)90059-5. PMID 1908607.
- Siegel LM, Ostrowski J, Rueger DC, Miller BE, Kredich NM, Barber MJ (1989). "Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cytochrome P-450 reductase". J. Biol. Chem. 264 (27): 15796–15808. PMID 2550423.
- Snyder SH, Reed RR, Bredt DS, Hwang PM, Glatt CE, Lowenstein C (1991). "Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase". Nature 351 (6329): 714–718. doi:10.1038/351714a0. PMID 1712077.
- Karplus PA, Bruns CM, Correll CC, Ludwig ML (1993). "Structural prototypes for an extended family of flavoprotein reductases: comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin". Protein Sci. 2 (12): 2112–2133. doi:10.1002/pro.5560021212. PMC 2142325. PMID 8298460. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2142325/.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
FAD binding domain Provide feedback
This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, Nitric oxide synthase and methionine synthase reductase.
Eschenbrenner M, Coves J, Fontecave M; , J Biol Chem 1995;270:20550-20555.: The flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure. PUBMED:7657631 EPMC:7657631
Eschenbrenner M, Coves J, Fontecave M; , FEBS Lett 1995;374:82-84.: NADPH-sulfite reductase flavoprotein from Escherichia coli: contribution to the flavin content and subunit interaction. PUBMED:7589518 EPMC:7589518
Wang M, Roberts DL, Paschke R, Shea TM, Masters BS, Kim JJ; , Proc Natl Acad Sci U S A 1997;94:8411-8416.: Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes. PUBMED:9237990 EPMC:9237990
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003097
This domain is found in sulphite reductase, NADPH cytochrome P450 reductase, nitric oxide synthase and methionine synthase reductase. Flavoprotein pyridine nucleotide cytochrome reductases [PUBMED:1748631] (FPNCR) catalyse the interchange of reducing equivalents between one-electron carriers and the two-electron-carrying nicotinamide dinucleotides. The enzymes include ferredoxin:NADP+reductases (FNR) [PUBMED:8027025], plant and fungal NAD(P)H:nitrate reductases [PUBMED:1748631, PUBMED:12165428], NADH:cytochrome b5 reductases [PUBMED:3700359], NADPH:P450 reductases [PUBMED:1908607], NADPH:sulphite reductases [PUBMED:2550423], nitric oxide synthases [PUBMED:1712077], phthalate dioxygenase reductase [PUBMED:8298460], and various other flavoproteins.
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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Curation and family details
|Seed source:||Pfam-B_180 (release 2.1)|
|Number in seed:||15|
|Number in full:||3726|
|Average length of the domain:||195.00 aa|
|Average identity of full alignment:||27 %|
|Average coverage of the sequence by the domain:||27.25 %|
|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:||15|
|Download:||download the raw HMM for this family|
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There are 3 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 FAD_binding_1 domain has been found. There are 39 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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