Summary: IMP cyclohydrolase-like protein
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This is the Wikipedia entry entitled "IMP cyclohydrolase". More...
IMP cyclohydrolase Edit Wikipedia article
| IMP cyclohydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.4.10 | ||||||||
| CAS number | 9013-81-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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| IMP cyclohydrolase-like protein | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| crystal structure of puro from methanothermobacter thermoautotrophicus | |||||||||
| Identifiers | |||||||||
| Symbol | IMP_cyclohyd | ||||||||
| Pfam | PF07826 | ||||||||
| InterPro | IPR020600 | ||||||||
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In enzymology, an IMP cyclohydrolase (EC 3.5.4.10) is an enzyme that catalyzes the chemical reaction
- IMP + H2O
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Thus, the two substrates of this enzyme are IMP and H2O, whereas its product is 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is IMP 1,2-hydrolase (decyclizing). Other names in common use include inosinicase, and inosinate cyclohydrolase. This enzyme catalyses the cyclisation of 5-formylamidoimidazole-4-carboxamide ribonucleotide to IMP, a reaction which is important in de novo purine biosynthesis in archaeal species.[1]
[edit] Structural studies
In most cases this single-domain protein is arranged to form an overall fold that consists of a four-layered alpha-beta-beta-alpha core structure. The two antiparallel beta-sheets pack against each other and are covered by alpha-helices on one face of the molecule. The protein is structurally similar to members of the N-terminal nucleophile (NTN) hydrolase superfamily. A deep pocket was in fact found on the surface of IMP cyclohydrolase in a position equivalent to that of active sites of NTN-hydrolases, but an N-terminal nucleophile could not be found. Therefore, it is thought that this enzyme is structurally but not functionally similar to members of the NTN-hydrolase family.[2]
As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes 1G8M, 1M9N, 1OZ0, 1P4R, 1PKX, 1PL0, 1THZ, 2B1G, 2B1I, 2IU0, 2IU3, 2NTK, 2NTL, and 2NTM.
[edit] References
- ^ Graupner M, Xu H, White RH (March 2002). "New class of IMP cyclohydrolases in Methanococcus jannaschii". J. Bacteriol. 184 (5): 14713. PMC 134845. PMID 11844782. //www.ncbi.nlm.nih.gov/pmc/articles/PMC134845/.
- ^ Saridakis V, Christendat D, Thygesen A, Arrowsmith CH, Edwards AM, Pai EF (July 2002). "Crystal structure of Methanobacterium thermoautotrophicum conserved protein MTH1020 reveals an NTN-hydrolase fold". Proteins 48 (1): 1413. doi:10.1002/prot.10147. PMID 12012346.
[edit] Further reading
- FLAKS JG, ERWIN MJ, BUCHANAN JM (1957). "Biosynthesis of the purines. XVIII 5-Amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase and inosinicase". J. Biol. Chem. 229 (2): 60312. PMID 13502325.
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This article incorporates text from the public domain Pfam and InterPro IPR020600
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IMP cyclohydrolase-like protein Provide feedback
This enzyme (O27099) is may catalyse the cyclization of 5-formylamidoimidazole-4-carboxamide ribonucleotide to inosine monophosphate (IMP), a reaction which is important in de novo purine biosynthesis in archaeal species. This single domain protein is arranged to form an overall fold that consists of a four-layered alpha-beta-beta-alpha core structure. The two antiparallel beta-sheets pack against each other and are covered by alpha-helices on one face of the molecule. The protein is structurally similar to members of the N-terminal nucleophile (NTN) hydrolase superfamily. A deep pocket was in fact found on the surface of IMP cyclohydrolase in a position equivalent to that of active sites of NTN-hydrolases, but an N-terminal nucleophile could not be found. Therefore, it is thought that this enzyme is structurally but not functionally similar to members of the NTN-hydrolase family [1].
Literature references
-
Saridakis V, Christendat D, Thygesen A, Arrowsmith CH, Edwards AM, Pai EF; , Proteins 2002;48:141-143.: Crystal structure of Methanobacterium thermoautotrophicum conserved protein MTH1020 reveals an NTN-hydrolase fold. PUBMED:12012346 EPMC:12012346
External database links
| PANDIT: | PF07826 |
| Pseudofam: | PF07826 |
| SYSTERS: | IMP_cyclohyd |
This tab holds annotation information from the InterPro database.
InterPro entry IPR020600
This entry represents inosine monophosphate (IMP) cyclohydrolase, found in archaeal species, as well as some bacterial proteins of unknown function.
IMP cyclohydrolase catalyses the cyclisation of 5-formylamidoimidazole-4-carboxamide ribonucleotide to IMP, a reaction which is important in de novo purine biosynthesis in archaeal species [PUBMED:11844782]. This single domain protein is arranged to form an overall fold that consists of a four-layered alpha-beta-beta-alpha core structure. The two antiparallel beta-sheets pack against each other and are covered by alpha-helices on one face of the molecule. The protein is structurally similar to members of the N-terminal nucleophile (NTN) hydrolase superfamily. A deep pocket was in fact found on the surface of IMP cyclohydrolase in a position equivalent to that of active sites of NTN-hydrolases, but an N-terminal nucleophile could not be found. Therefore, it is thought that this enzyme is structurally but not functionally similar to members of the NTN-hydrolase family [PUBMED:12012346].
In bacteria this step is catalysed by a bifunctional enzyme (purH).
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | IMP cyclohydrolase activity (GO:0003937) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
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| Seed (6) |
Full (187) |
Representative proteomes | NCBI (183) |
Meta (27) |
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| RP15 (22) |
RP35 (44) |
RP55 (57) |
RP75 (63) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
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| Seed (6) |
Full (187) |
Representative proteomes | NCBI (183) |
Meta (27) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (22) |
RP35 (44) |
RP55 (57) |
RP75 (63) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
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Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_50235 (release 14.0) |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Fenech M |
| Number in seed: | 6 |
| Number in full: | 187 |
| Average length of the domain: | 212.30 aa |
| Average identity of full alignment: | 40 % |
| Average coverage of the sequence by the domain: | 92.54 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 200 | ||||||||||||
| Family (HMM) version: | 6 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
IMP_cyclohydStructures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the IMP_cyclohyd domain has been found. There are 13 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence