SUPERFAMILY 1.75 HMM library and genome assignments server

SUPERFAMILY 2 can be accessed from supfam.org. Please contact us if you experience any problems.

  Home > SCOP hierarchy > Methenyltetrahydromethanopterin cyclohydrolase superfamily


Methenyltetrahydromethanopterin cyclohydrolase superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   Alpha and beta proteins (a+b) [ 53931] (376)
Fold:   Methenyltetrahydromethanopterin cyclohydrolase [ 56198]
Superfamily:   Methenyltetrahydromethanopterin cyclohydrolase [ 56199]
Families:   Methenyltetrahydromethanopterin cyclohydrolase [ 56200]

 Superfamily statistics
Genomes (145) Uniprot 2018_03 genome PDB chains (SCOP 1.75)
Domains 153 1,191 1
Proteins 153 1,191 1

 Functional annotation
General category Metabolism
Detailed category Other enzymes

Document: Function annotation of SCOP domain superfamilies

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEO levelAnnotation (direct or inherited)
Enzyme Commission (EC)In cyclic amidines0InformativeDirect

Document: EC annotation of SCOP domains

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEC levelAnnotation (direct or inherited)
Enzyme Commission (EC)Hydrolases0Least InformativeDirect
Enzyme Commission (EC)Acting on carbon-nitrogen bonds, other than peptide bonds0Moderately InformativeDirect
Enzyme Commission (EC)In cyclic amidines0InformativeDirect

Document: EC annotation of SCOP domains

InterPro annotation
Cross references IPR003209 SSF56199 Protein matches
Abstract

Methenyltetrahydromethanopterin cyclohydrolase catalyses the interconversion of methenyltetrahydromethanopterin and N(5)formyltetrahydromethanopterin, and is found in both archaea and bacteria. In methanogenic archaea, such as Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133), this enzyme is involved in the production of methane from carbon dioxide [PubMed8617278]. In the sulphate-reducer Archaeoglobus fulgidus, this enzyme is involved in the tetrahydromethanopterin-dependent oxidation of lactate [PubMed8481088]. In Gram-negative methylotrophic bacteria this enzyme is involved in the tetrahydromethanopterin-dependent oxidation of formaldehyde to formate [PubMed10482517].


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) · Enzyme Commission (EC) ]

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 3 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 Methenyltetrahydromethanopterin cyclohydrolase 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 3 hidden Markov models representing the Methenyltetrahydromethanopterin cyclohydrolase 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 · Enzyme Commission (EC) · Enzyme Commission (EC) · 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.

Please send feedback, comments or questions to superfamily@cs.bris.ac.uk or use the feedback form.

© Copyright 2013 The SUPERFAMILY authors and Julian Gough.