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InterPro: IPR016168 FAD-linked oxidase, FAD-binding, subdomain 2
Protein matches
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UniProtKB Matches: 3340 proteins |
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Accession
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IPR016168 FAD-linked_Oxase_FAD-bd_sub2 |
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Type
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Domain |
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Signatures
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InterPro Relationships
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Found in
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IPR004490 Glycolate oxidase subunit GlcD
IPR006094 FAD linked oxidase, N-terminal
IPR010031 Sugar 1,4-lactone oxidase
IPR010032 FAD-linked oxidoreductase
IPR012256 D-lactate dehydrogenase
IPR016166 FAD-binding, type 2
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GO Term annotation
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Function
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GO:0003824 catalytic activity
GO:0050660 FAD binding
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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These FAD-binding domains consist of two alpha+beta subdomains. This entry represents the second (C-terminal) 2-layer alpha/beta subdomain, which is found in several FAD-linked oxidases as an N-terminal FAD-binding domain, including vanillyl-alochol oxidase (EC:1.1.3.38) [1], flavoprotein subunit of p-cresol methylhydroxylase (EC:1.17.99.1) [2], D-lactate dehydrogenases (EC:1.1.1.28, EC:1.1.2.4 -cytochrome) [3], Cholesterol oxidases (EC:1.1.3.6) [4], Cytokinin dehydrogenase 1 (EC:1.5.99.12) [5].
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Structural links
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Example proteins
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O00116 Alkyldihydroxyacetonephosphate synthase, peroxisomal
O17397 Diminuto-like protein
P32891 D-lactate dehydrogenase [cytochrome] 1, mitochondrial
P58710 L-gulonolactone oxidase
Q9V778 Alkyldihydroxyacetonephosphate synthase
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR007173 |
D-arabinono-1,4-lactone oxidase |
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| IPR006093 |
Oxygen oxidoreductase covalent FAD-binding site |
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| IPR016168 |
FAD-linked oxidase, FAD-binding, subdomain 2 |
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| IPR016167 |
FAD-binding, type 2, subdomain 1 |
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| IPR004113 |
FAD-linked oxidase, C-terminal |
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| IPR016166 |
FAD-binding, type 2 |
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| IPR006094 |
FAD linked oxidase, N-terminal |
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| IPR016164 |
FAD-linked oxidase-like, C-terminal |
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| IPR010031 |
Sugar 1,4-lactone oxidase |
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SWISS-MODEL |
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ModBase |
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Publications
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1.
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Fraaije MW, van den Heuvel RH, van Berkel WJ, Mattevi A.
Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase.
J. Biol. Chem. 274 35514-20 1999
[PubMed: 10585424]
http://dx.doi.org/10.1074/jbc.274.50.35514
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2.
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Cunane LM, Chen ZW, McIntire WS, Mathews FS.
p-Cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit.
Biochemistry 44 2963-73 2005
[PubMed: 15723539]
http://dx.doi.org/10.1021/bi048020r
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3.
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Dym O, Pratt EA, Ho C, Eisenberg D.
The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme.
Proc. Natl. Acad. Sci. U.S.A. 97 9413-8 2000
[PubMed: 10944213]
http://dx.doi.org/10.1073/pnas.97.17.9413
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4.
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Coulombe R, Yue KQ, Ghisla S, Vrielink A.
Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair.
J. Biol. Chem. 276 30435-41 2001
[PubMed: 11397813]
http://dx.doi.org/10.1074/jbc.M104103200
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5.
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Malito E, Coda A, Bilyeu KD, Fraaije MW, Mattevi A.
Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis.
J. Mol. Biol. 341 1237-49 2004
[PubMed: 15321719]
http://dx.doi.org/10.1016/j.jmb.2004.06.083
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Additional Reading
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Lim L, Molla G, Guinn N, Ghisla S, Pollegioni L, Vrielink A.
Structural and kinetic analyses of the H121A mutant of cholesterol oxidase.
Biochem. J. 400 2006 13-22
[PubMed: 16856877]
http://dx.doi.org/10.1042/BJ20060664
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Fraaije MW, van Den Heuvel RH, van Berkel WJ, Mattevi A.
Structural analysis of flavinylation in vanillyl-alcohol oxidase.
J. Biol. Chem. 275 2000 38654-8
[PubMed: 10984479]
http://dx.doi.org/10.1074/jbc.M004753200
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van den Heuvel RH, van den Berg WA, Rovida S, van Berkel WJ.
Laboratory-evolved vanillyl-alcohol oxidase produces natural vanillin.
J. Biol. Chem. 279 2004 33492-500
[PubMed: 15169773]
http://dx.doi.org/10.1074/jbc.M312968200
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InterPro 23.1
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