About: Cyclodeaminase domain

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In molecular biology, enzymes containing the cyclodeaminase domain function in channeling one-carbon units to the folate pool. In most cases, this domain acts as a formimidoyltetrahydrofolate cyclodeaminase, which catalyses the cyclisation of formimidoyltetrahydrofolate to methenyltetrahydrofolate as shown in reaction (1). In the methylotrophic bacterium Methylobacterium extorquens, however, it acts as a methenyltetrahydrofolate cyclohydrolase, which catalyses the interconversion of formyltetrahydrofolate and methylenetetrahydrofolate, as shown in reaction (2).

Attributes	Values
rdf:type	Thing Biomolecule Biomolecule Protein yago:Abstraction100002137 yago:Family108078020 yago:Group100031264 yago:Organization108008335 yago:YagoLegalActor yago:YagoLegalActorGeo yago:YagoPermanentlyLocatedEntity protein yago:SocialGroup107950920 yago:Unit108189659 yago:WikicatProteinFamilies
rdfs:label	Cyclodeaminase domain (en)
rdfs:comment	In molecular biology, enzymes containing the cyclodeaminase domain function in channeling one-carbon units to the folate pool. In most cases, this domain acts as a formimidoyltetrahydrofolate cyclodeaminase, which catalyses the cyclisation of formimidoyltetrahydrofolate to methenyltetrahydrofolate as shown in reaction (1). In the methylotrophic bacterium Methylobacterium extorquens, however, it acts as a methenyltetrahydrofolate cyclohydrolase, which catalyses the interconversion of formyltetrahydrofolate and methylenetetrahydrofolate, as shown in reaction (2). (en)
name	FTCD_C (en)
foaf:depiction
dct:subject	Protein families
Wikipage page ID	32840658 (xsd:integer)
Wikipage revision ID	997180646 (xsd:integer)
Link from a Wikipage to another Wikipage	Carbon Prokaryotes Prokaryotic Methenyltetrahydrofolate cyclohydrolase Monomer Sequence alignment Protein families Enzyme Conserved sequence Crystal structure Bacterium Active site Catalyse Helix Alpha helix Eukaryotes Eukaryotic dbr:Folate Formimidoyltetrahydrofolate cyclodeaminase Dimer (chemistry) Protein domain Protein folding Product (chemistry) Residue (chemistry) Biocatalysis Methylotrophic Methylobacterium extorquens Catalysis Formiminotransferase cyclodeaminase Tetramer Glutamate formiminotransferase Homodimer
sameAs	Cyclodeaminase domain Cyclodeaminase domain Cyclodeaminase domain Cyclodeaminase domain
dbp:wikiPageUsesTemplate	dbt:Infobox_protein_family dbt:InterPro_content dbt:Reflist
thumbnail	wiki-commons:Special:FilePath/PDB_1o5h_EBI.jpg?width=300
SCOP	18000.0 (second)
caption	crystal structure of formiminotetrahydrofolate cyclodeaminase from thermotoga maritima at 2.80 a resolution (en)
InterPro	IPR007044 (en)
Pfam	PF04961 (en)
symbol	FTCD_C (en)
has abstract	In molecular biology, enzymes containing the cyclodeaminase domain function in channeling one-carbon units to the folate pool. In most cases, this domain acts as a formimidoyltetrahydrofolate cyclodeaminase, which catalyses the cyclisation of formimidoyltetrahydrofolate to methenyltetrahydrofolate as shown in reaction (1). In the methylotrophic bacterium Methylobacterium extorquens, however, it acts as a methenyltetrahydrofolate cyclohydrolase, which catalyses the interconversion of formyltetrahydrofolate and methylenetetrahydrofolate, 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. The eukaryotic enzyme is a circular tetramer of homodimers, while the prokaryotic enzyme is a dimer. The crystal structure of the cyclodeaminase enzyme from Thermaotogoa maritima has been studied. 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. (en)
prov:wasDerivedFrom	wikipedia-en:Cyclodeaminase_domain?oldid=997180646&ns=0
page length (characters) of wiki page	4324 (xsd:nonNegativeInteger)
Symbol	FTCD_C
foaf:isPrimaryTopicOf	wikipedia-en:Cyclodeaminase_domain
is foaf:primaryTopic of	wikipedia-en:Cyclodeaminase_domain

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