NAD(P)-linked oxidoreductase superfamily

SCOP classification

Root:	SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:	Alpha and beta proteins (a/b) [ 51349] (147)
Fold:	TIM beta/alpha-barrel [ 51350] (33)
Superfamily:	NAD(P)-linked oxidoreductase [ 51430]
Families:	Aldo-keto reductases (NADP) [ 51431] (15)

Superfamily statistics

	Genomes (2,708)	Uniprot 2018_03 genome	PDB chains (SCOP 1.75)
Domains	25,569	165,419	47
Proteins	25,361	164,813	47

Functional annotation

General category	Metabolism
Detailed category	Redox

Document: Function annotation of SCOP domain superfamilies

Enzyme Commission (EC)

(show details)

	EC term	FDR (all)	SDEO level	Annotation (direct or inherited)
Enzyme Commission (EC)	Oxidoreductases	0	Least Informative	Direct
Enzyme Commission (EC)	With NAD(+) or NADP(+) as acceptor	0	Moderately Informative	Direct
Enzyme Commission (EC)	Acting on the CH-CH group of donors	0.4925	Moderately Informative	Inherited

Document: EC annotation of SCOP domains

Disease Ontology (DO)

(show details) Document: DO annotation of SCOP domains

Human Phenotype (HP)

(show details) Document: HP annotation of SCOP domains

Worm Phenotype (WP)

(show details)

	WP term	FDR (all)	SDWP level	Annotation (direct or inherited)
Worm Phenotype (WP)	organism behavior variant	0.003039	Least Informative	Inherited
Worm Phenotype (WP)	defecation variant	0.0000001717	Informative	Direct
Worm Phenotype (WP)	defecation cycle variant	0.0000000001725	Highly Informative	Direct

Document: WP annotation of SCOP domains

Fly Phenotype (FP)

(show details)

	FP term	FDR (all)	SDFP level	Annotation (direct or inherited)
Fly Phenotype (FP)	viable	0	Least Informative	Direct

Document: FP annotation of SCOP domains

Xenopus Anatomy (XA)

(show details) Document: XA annotation of SCOP domains

Arabidopsis Plant Ontology (AP)

(show details)

	AP term	FDR (all)	SDAP level	Annotation (direct or inherited)
Plant structure DEvelopment stage (PDE)	LP.04 four leaves visible stage	0	Least Informative	Direct

Document: AP annotation of SCOP domains

Enzyme Commission (EC)

(show details)

	EC term	FDR (all)	SDEC level	Annotation (direct or inherited)
Enzyme Commission (EC)	Oxidoreductases	0	Least Informative	Direct
Enzyme Commission (EC)	Acting on the CH-OH group of donors	0	Moderately Informative	Direct
Enzyme Commission (EC)	With NAD(+) or NADP(+) as acceptor	0	Informative	Direct
Enzyme Commission (EC)	With NAD(+) or NADP(+) as acceptor	0.0000001388	Informative	Direct

Document: EC annotation of SCOP domains

UniProtKB KeyWords (KW)

(show details)

	KW term	FDR (all)	SDKW level	Annotation (direct or inherited)
Post-translational modification	Oxidoreductase	0	Moderately Informative	Direct

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 [ PubMed 2498333]. All possess a similar structure, with a beta-alpha-beta fold characteristic of nucleotide binding proteins [ PubMed 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 [ PubMed 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 [ PubMed 1447221].

Some proteins of this entry contain a K+ ion channel beta chain regulatory domain; these are reported to have oxidoreductase activity [ PubMed 10884227].

InterPro database

PDBeMotif information about ligands, sequence and structure motifs

Cross references

PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural 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.

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.

Browse and view proteins in genomes which have different domain combinations including a NAD(P)-linked oxidoreductase domain.

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.

Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

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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NAD(P)-linked oxidoreductase superfamily