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NAD(P)-linked oxidoreductase superfamily
SCOP classification
Superfamily statistics
Functional annotation
General category | Metabolism |
Detailed category | Redox |
Document: Function annotation of SCOP domain superfamilies
Enzyme Commission (EC) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: EC annotation of SCOP domains
Disease Ontology (DO) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: DO annotation of SCOP domains
Human Phenotype (HP) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: HP annotation of SCOP domains
Worm Phenotype (WP) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: WP annotation of SCOP domains
Fly Phenotype (FP) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: FP annotation of SCOP domains
Xenopus Anatomy (XA) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: XA annotation of SCOP domains
Arabidopsis Plant Ontology (AP) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: AP annotation of SCOP domains
Enzyme Commission (EC) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: EC annotation of SCOP domains
UniProtKB KeyWords (KW) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: KW annotation of SCOP domains
InterPro annotation
Cross references | IPR001395 SSF51430 Protein matches |
Abstract | The aldo-keto reductase family includes a number of related monomeric
NADPH-dependent oxidoreductases, such as aldehyde reductase, aldose
reductase, prostaglandin F synthase, xylose reductase, rho crystallin, and
many others [ 2498333]. All possess a similar structure, with a beta-alpha-beta fold
characteristic of nucleotide binding proteins [ 2105951].
The fold comprises a parallel beta-8/alpha-8-barrel, which contains a
novel NADP-binding motif. The binding site is located in a large,
deep, elliptical pocket in the C-terminal end of the beta sheet, the
substrate being bound in an extended conformation. The hydrophobic
nature of the pocket favours aromatic and apolar substrates over highly
polar ones [ 1621098]. Binding of the NADPH coenzyme causes a massive
conformational change, reorienting a loop, effectively locking the
coenzyme in place. This binding is more similar to FAD- than to
NAD(P)-binding oxidoreductases [ 1447221].
Some proteins of this entry contain a K+ ion channel beta chain regulatory domain; these are reported to have oxidoreductase activity [ 10884227]. |
InterPro database
PDBeMotif information about ligands, sequence and structure motifs
PDBeMotif resource
Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Disease Ontology (DO) · Human Phenotype (HP) · Worm Phenotype (WP) · Fly Phenotype (FP) · Xenopus Anatomy (XA) · Arabidopsis Plant Ontology (AP) · Enzyme Commission (EC) · UniProtKB KeyWords (KW) ]
Internal database links
Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry
out SCOP domain assignments to all genomes at the superfamily level.
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Alignments of sequences to 62 models
in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical
are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.
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Browse and view proteins in genomes which have
different domain combinations including a NAD(P)-linked oxidoreductase domain.
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Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.
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Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.
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There are 62 hidden Markov models representing the NAD(P)-linked oxidoreductase superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.
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Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Disease Ontology (DO) · Human Phenotype (HP) · Worm Phenotype (WP) · Fly Phenotype (FP) · Xenopus Anatomy (XA) · Arabidopsis Plant Ontology (AP) · Enzyme Commission (EC) · UniProtKB KeyWords (KW) · Internal database links ]
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