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Methenyltetrahydrofolate cyclohydrolase-like superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   All alpha proteins [ 46456] (284)
Fold:   Methenyltetrahydrofolate cyclohydrolase-like [ 101261]
Superfamily:   Methenyltetrahydrofolate cyclohydrolase-like [ 101262]
Families:   Methenyltetrahydrofolate cyclohydrolase-like [ 101263]


Superfamily statistics
Genomes (384) Uniprot 2014_06 PDB chains (SCOP 1.75)
Domains 450 1,658 1
Proteins 447 1,656 1


Functional annotation
General category Metabolism
Detailed category Other enzymes

Document:
Function annotation of SCOP domain superfamilies

Gene Ontology (high-coverage)

(show details) Document: GO annotation of SCOP domains

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEO levelAnnotation (direct or inherited)
Enzyme Commission (EC)Transferring one-carbon groups0.00000002056Least InformativeDirect
Enzyme Commission (EC)Lyases0.0000001589Least InformativeDirect
Enzyme Commission (EC)Carbon-nitrogen lyases7.054e-16InformativeDirect
Enzyme Commission (EC)Hydroxymethyl-, formyl- and related transferases0.0000000000003583InformativeDirect

Document: EC annotation of SCOP domains

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEC levelAnnotation (direct or inherited)
Enzyme Commission (EC)Lyases0.0000001961Least InformativeDirect
Enzyme Commission (EC)Transferring one-carbon groups0.00000002159Moderately InformativeDirect
Enzyme Commission (EC)Carbon-nitrogen lyases0.000000000000008715InformativeDirect
Enzyme Commission (EC)Hydroxymethyl-, formyl- and related transferases0.0000000000002665InformativeDirect
Enzyme Commission (EC)Ammonia-lyases0Highly InformativeDirect

Document: EC annotation of SCOP domains

UniProtKB KeyWords (KW)

(show details)
KW termFDR (all)SDKW levelAnnotation (direct or inherited)
Biological processHistidine metabolism0Highly InformativeDirect
Cellular componentCytoplasm0.02068Least InformativeInherited
Cellular componentGolgi apparatus0.0000000000002345Moderately InformativeDirect
Cellular componentCytoskeleton0.000000006726Moderately InformativeDirect
Molecular functionPyridoxal phosphate0.0000000000007026Highly InformativeDirect
Post-translational modificationTransferase0.0001045Least InformativeDirect
Post-translational modificationLyase0.0000000103Moderately InformativeDirect

Document: KW annotation of SCOP domains

InterPro annotation
Cross references IPR007044 SSF101262 Protein matches
Abstract

Enzymes containing the cyclodeaminase domain function in channeling one-carbon units to the folate pool. In most cases, this domain catalyses the cyclisation of formimidoyltetrahydrofolate to methenyltetrahydrofolate as shown in reaction (1). In the methylotrophic bacterium Methylobacterium extorquens, however, it catalyses the interconversion of formyltetrahydrofolate and methylenetetrahydrofolate [PubMed10215859],as shown in reaction (2)

(1) 5-formimidoyltetrahydrofolate = 5,10-methenyltetrahydrofolate + NH(3) (2) 10- formyltetrahydrofolate = 5,10-methenyltetrahydrofolate + H(2)O

In prokaryotes, this domain mostly occurs on its own, while in eukaryotes it is fused to a glutamate formiminotransferase domain (which catalyses the previous step in the pathway) to form the bifunctional enzyme formiminotransferase-cyclodeaminase [PubMed7654689]. The eukaryotic enzyme is a circular tetramer of homodimers [PubMed7410436], while the prokaryotic enzyme is a dimer [PubMed10215859, PubMed15651027].

The crystal structure of the cyclodeaminase enzyme from Thermaotogoa maritima has been studied [PubMed15651027]. It is a homodimer, where each monomer is composed of six alpha helices arranged in an up and down helical bundle, forming a novel fold. The location of the active site is not known, but sequence alignments revealed two clusters of conserved residues located in a deep pocket within the dimmer interface. This pocket was large enough to accommodate the reaction product and it was postulated that this is the active site.


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 · Gene Ontology (high-coverage) · Enzyme Commission (EC) · 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 1 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 Methenyltetrahydrofolate cyclohydrolase-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 1 hidden Markov models representing the Methenyltetrahydrofolate cyclohydrolase-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 · Gene Ontology (high-coverage) · Enzyme Commission (EC) · Enzyme Commission (EC) · UniProtKB KeyWords (KW) · Internal database links ]