Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyQuinone reductase 8031712 4003674 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyFlavoproteins 8044090 3001217 SCOP2 (2022-06-29)
BSCOP2B SuperfamilyFlavoproteins 8044090 3001217 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyFlavoproteins 8044090 3001217 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyFlavoproteins 8044090 3001217 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AFMN_rede1d4aA1 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Flavoproteins/Phosphotyrosine protein phosphatases-likeT: FlavoproteinsF: FMN_redECOD (1.6)
BFMN_rede1d4aB1 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Flavoproteins/Phosphotyrosine protein phosphatases-likeT: FlavoproteinsF: FMN_redECOD (1.6)
CFMN_rede1d4aC1 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Flavoproteins/Phosphotyrosine protein phosphatases-likeT: FlavoproteinsF: FMN_redECOD (1.6)
DFMN_rede1d4aD1 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Flavoproteins/Phosphotyrosine protein phosphatases-likeT: FlavoproteinsF: FMN_redECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.40.50.360 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold Flavodoxin domainCATH (4.3.0)
B3.40.50.360 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold Flavodoxin domainCATH (4.3.0)
C3.40.50.360 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold Flavodoxin domainCATH (4.3.0)
D3.40.50.360 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold Flavodoxin domainCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D
PF02525Flavodoxin-like fold (Flavodoxin_2)Flavodoxin-like foldThis family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyse the NAD(P)H-dependent two-electron reductions of quinones and protect cell ...This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyse the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species [1]. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy [1]. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP [2]. This family is related to Pfam:PF03358 and Pfam:PF00258.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B, C, D
QUINONE REDUCTASE

InterPro: Protein Family Classification InterPro Database Homepage

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
A, B, C, D
PharosP15559

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
NAD(P)H dehydrogenase (quinone)  M-CSA #3

Quinone reductase exists as a dimer of identical subunits, each comprising of 273 amino acids with two identical catalytic sites at equivalent positions. The enzyme catalyses the FAD dependent reduction of quinones. The dimer binds two FAD cofactors which remain non-covalently bound during catalysis. NAD(P)H and NAD(P)+ cycle in and out of the catalytic site. The catalytic domain has the characteristic twisted central parallel beta sheet surrounded on both sides by connecting helices, as found in other flavoproteins.

Defined by 3 residues: GLY:A-149TYR:A-155HIS:A-161
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