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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
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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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