SUPERFAMILY 1.73 HMM library and genome assignments server


LDH C-terminal domain-like superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   Alpha and beta proteins (a+b) [ 53931] (334)
  Mainly antiparallel beta sheets (segregated alpha and beta regions)
Fold:   LDH C-terminal domain-like [ 56326]
  unusual fold, defines family
Superfamily:   LDH C-terminal domain-like [ 56327] (2)
Families:   Lactate & malate dehydrogenases, C-terminal domain [ 56328] (4)
  N-terminal domain is NAD-binding module (alpha/beta Rossmann-fold domain)
  AglA-like glucosidase [ 90050] (4)
  family 4 glycosyl hydrolase


Superfamily statistics
Genomes (1,099) UniProt 15.0 PDB chains (SCOP 1.73)
Domains 2,985 4,516 56
Proteins 2,983 4,516 56


Functional annotation
General category Metabolism
Detailed category Redox

Function annotation of SCOP domain superfamilies
InterPro annotation
Cross references IPR015955 SSF56327 Protein matches
Abstract

This entry represents a structural motif found at the C-terminal of lactate dehydrogenase and malate dehydrogenases , as well as at the C-terminal of family 4 glycoside hydrolases . These domains have an unusual fold consisting of segregated alpha-helical and beta-sheet regions, although they contain predominantly anti-parallel beta-sheets [PubMed11276087, PubMed8117664, PubMed12588867].

L-lactate dehydrogenases are metabolic enzymes that catalyse the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis. L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes. Malate dehydrogenases catalyse the interconversion of malate to oxaloacetate. The enzyme participates in the citric acid cycle.

O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [PubMed7624375, PubMed8535779]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in 'clans'. Glycoside hydrolase family 4 comprises enzymes with several known activities; 6-phospho-beta-glucosidase ; 6-phospho-alpha-glucosidase ; alpha-galactosidase .


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

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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 33 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 LDH C-terminal domain-like 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 33 hidden Markov models representing the LDH C-terminal domain-like superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.


Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Internal database links ]