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LuxS/MPP-like metallohydrolase 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:   LuxS/MPP-like metallohydrolase [ 63410]
  core: beta-alpha-beta(2)-alpha(2); 2 layers: alpha/beta
Superfamily:   LuxS/MPP-like metallohydrolase [ 63411] (2)
Families:   Autoinducer-2 production protein LuxS [ 64294]
  contains additional N-terminal strand; possible relationships to the putative editing domain of ThrRS (d.67.1)
  MPP-like [ 63412] (6)
  Common fold elaborated with many additional structures; duplication: each family member consists of two similar domains of beta(2)-alpha(2)-beta(2)-alpha(5)-beta structure, but only the N-terminal domain of MPP beta chain binds the catalytic metal

 Superfamily statistics
Genomes (1,097) UniProt 15.0 PDB chains (SCOP 1.73)
Domains 12,040 10,956 44
Proteins 4,835 4,710 23

 Functional annotation
General category Processes_IC
Detailed category Proteases

Function annotation of SCOP domain superfamilies
InterPro annotation
Cross references IPR011249 SSF63411 Protein matches
Abstract

This entry represents domains with a two-layer alpha/beta structure found in metalloenzymes such as LuxS (S-ribosylhomocysteinase) and metallopeptidases belonging to MEROPS peptidase family M16. These domains share the same active site motif of HxxEH located in the first core helix, but differ in one of the metal-binding residues. LuxS, the AI-2 (autoinducer-2) producing enzyme for quorum sensing in bacteria, is a homodimeric iron-dependent metalloenzyme containing two identical tetrahedral metal-binding sites similar to those found in peptidases and amidases, although it contains an extra N-terminal strand [PubMed15751951, PubMed11553770]. Some M16 family metallopeptidases, such as mitochondrial processing peptidase (MPP), share the same common fold elaborated with many extra additional structures [PubMed11470436]. These peptidases usually contain a duplication of this domain, although only the N-terminal domain binds the catalytic metal.


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 28 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 LuxS/MPP-like metallohydrolase 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 28 hidden Markov models representing the LuxS/MPP-like metallohydrolase 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 ]
Please cite: Gough, J., Karplus, K., Hughey, R. and Chothia, C. (2001). "Assignment of Homology to Genome Sequences using a Library of Hidden Markov Models that Represent all Proteins of Known Structure." J. Mol. Biol., 313(4), 903-919.

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© Copyright 2001-2010 The Medical Research Council and the SUPERFAMILY authors; Derek Wilson, Martin Madera and Julian Gough.