Summary: Imidazoleglycerol-phosphate dehydratase
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This is the Wikipedia entry entitled "Imidazoleglycerol-phosphate dehydratase". More...
Imidazoleglycerol-phosphate dehydratase Edit Wikipedia article
| imidazoleglycerol-phosphate dehydratase | |||||||||
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| Identifiers | |||||||||
| EC number | 4.2.1.19 | ||||||||
| CAS number | 9024-35-5 | ||||||||
| 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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| Imidazoleglycerol-phosphate dehydratase | |||||||||
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| crystal structure of imidazole glycerol phosphate dehydratase | |||||||||
| Identifiers | |||||||||
| Symbol | IGPD | ||||||||
| Pfam | PF00475 | ||||||||
| Pfam clan | CL0329 | ||||||||
| InterPro | IPR000807 | ||||||||
| PROSITE | PDOC00738 | ||||||||
| SCOP | 1rhy | ||||||||
| SUPERFAMILY | 1rhy | ||||||||
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In enzymology, an imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) is an enzyme that catalyzes the chemical reaction
- D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Hence, this enzyme has one substrate, D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate, and two products, 3-(imidazol-4-yl)-2-oxopropyl phosphate and H2O. This reaction is the seventh step in the biosynthesis of histidine in bacteria, fungi and plants.
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-erythro-1-(imidazol-4-yl)glycerol-3-phosphate hydro-lyase [3-(imidazol-4-yl)-2-oxopropyl-phosphate-forming]. Other names in common use include IGP dehydratase, and D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate hydro-lyase. This enzyme participates in histidine metabolism as it is involved in the 6th step of histidine biosynthesis as part of a nine step cyclical pathway.
IGPD is a recognised novel herbicide target as animals do not have an IGPD
There are two isoforms of IGPD; IGPD1 and IGPD2. The different isoforms are highly conserved with only 8 amino acids differing between them. These subtle differences however affect their activity but as yet it is unknown how.
In most organisms IGPD is a monofunctional protein of about 22 to 29 kD. In some bacteria such as Escherichia coli, it is the C-terminal domain of a bifunctional protein that include a histidinol-phosphatase domain.[1] In E. coli, this is the protein encoded by the hisB gene.[2]
[edit] Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1RHY, 2AE8, and 2F1D.
[edit] References
- ^ Carlomagno MS, Chiariotti L, Alifano P, Nappo AG, Bruni CB (October 1988). "Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons". J. Mol. Biol. 203 (3): 585–606. doi:10.1016/0022-2836(88)90194-5. PMID 3062174.
- ^ Brilli, M.; Fani, R. (2004). "Molecular Evolution of hisB Genes". Journal of Molecular Evolution 58 (2): 225–237. doi:10.1007/s00239-003-2547-x. PMID 15042344.
[edit] Further reading
- AMES BN (1957). "The biosynthesis of histidine; D-erythro-imidazoleglycerol phosphate dehydrase". J. Biol. Chem. 228 (1): 131–43. PMID 13475302.
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No Pfam abstract.
External database links
| PANDIT: | PF00475 |
| PROSITE: | PDOC00738 |
| Pseudofam: | PF00475 |
| SCOP: | 1rhy |
| SYSTERS: | IGPD |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000807
Imidazoleglycerol-phosphate dehydratase is the enzyme that catalyses the seventh step in the biosynthesis of histidine in bacteria, fungi and plants. In most organisms it is a monofunctional protein of about 22 to 29 kD. In some bacteria such as Escherichia coli, it is the C-terminal domain of a bifunctional protein that include a histidinol-phosphatase domain [PUBMED:3062174].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | imidazoleglycerol-phosphate dehydratase activity (GO:0004424) |
| Biological process | histidine biosynthetic process (GO:0000105) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan S5 (CL0329), which contains the following 14 members:
ChlI DNA_mis_repair EFG_IV Fae GHMP_kinases_N IGPD Lon_C LpxC Ribonuclease_P Ribosomal_S5_C RNase_PH Topo-VIb_trans UPF0029 Xol-1_NAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (146) |
Full (3695) |
Representative proteomes | NCBI (2611) |
Meta (2275) |
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| RP15 (330) |
RP35 (666) |
RP55 (867) |
RP75 (1011) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (146) |
Full (3695) |
Representative proteomes | NCBI (2611) |
Meta (2275) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (330) |
RP35 (666) |
RP55 (867) |
RP75 (1011) |
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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
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
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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: | Prosite |
| Previous IDs: | none |
| Type: | Family |
| Author: | Finn RD |
| Number in seed: | 146 |
| Number in full: | 3695 |
| Average length of the domain: | 144.30 aa |
| Average identity of full alignment: | 51 % |
| Average coverage of the sequence by the domain: | 57.73 % |
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: | 145 | ||||||||||||
| Family (HMM) version: | 13 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
IGPDStructures
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 IGPD domain has been found. There are 24 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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3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence