SUPERFAMILY 1.73 HMM library and genome assignments server


S-adenosylmethionine synthetase 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:   S-adenosylmethionine synthetase [ 55972]
  duplication: consists of 3 similar intertwined domains
structural repeat: beta-alpha-beta(2)-alpha-beta; two layers, alpha/beta
Superfamily:   S-adenosylmethionine synthetase [ 55973]
Families:   S-adenosylmethionine synthetase [ 55974]


Superfamily statistics
Genomes (1,128) UniProt 15.0 PDB chains (SCOP 1.73)
Domains 4,290 4,959 6
Proteins 1,471 1,724 2


Functional annotation
General category Metabolism
Detailed category Coenzyme metabolism and transport

Function annotation of SCOP domain superfamilies
InterPro annotation
Cross references IPR002133 SSF55973 Protein matches
Abstract

S-adenosylmethionine synthetase (MAT, ) is the enzyme that catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP [PubMed1696256]. AdoMet is an important methyl donor for transmethylation and is also the propylamino donor in polyamine biosynthesis.

In bacteria there is a single isoform of AdoMet synthetase (gene metK), there are two in budding yeast (genes SAM1 and SAM2) and in mammals while in plants there is generally a multigene family.

The sequence of AdoMet synthetase is highly conserved throughout isozymes and species. The active sites of both the Escherichia coli and rat liver MAT reside between two subunits, with contributions from side chains of residues from both subunits, resulting in a dimer as the minimal catalytic entity. The side chains that contribute to the ligand binding sites are conserved between the two proteins. In the structures of complexes with the E. coli enzyme, the phosphate groups have the same positions in the (PPi plus Pi) complex and the (ADP plus Pi) complex, and are located at the bottom of a deep cavity with the adenosyl group nearer the entrance [PubMed1213535].


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 6 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 S-adenosylmethionine synthetase 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 6 hidden Markov models representing the S-adenosylmethionine synthetase 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 ]