Summary: Imidazoleglycerol-phosphate dehydratase
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Imidazoleglycerol-phosphate dehydratase Edit Wikipedia article
In enzymology, an imidazoleglycerol-phosphate dehydratase (EC 126.96.36.199) 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 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 of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1RHY, 2AE8, and 2F1D.
- AMES BN (1957). "The biosynthesis of histidine; D-erythro-imidazoleglycerol phosphate dehydrase". J. Biol. Chem. 228: 131â€“43. PMIDÂ 13475302.
- The CAS registry number for this enzyme class is Template:CAS registry.
Gene Ontology (GO) codes
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Imidazoleglycerol-phosphate dehydratase Provide feedback
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External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000807
Imidazoleglycerol-phosphate dehydratase (IGPD; EC ) catalyzes the dehydration of imidazole glycerol phosphate to imidazole acetol phosphate, the sixth step of histidine biosynthesis in plants and microorganisms where the histidine is synthesized de novo. There is an internal repeat in the protein domain that is related by pseudo-dyad symmetry, perhaps as a result of an ancient gene duplication. The apo-form of IGPD exists as a catalytically inactive trimer which, in the presence of specific divalent metal cations such as manganese (Mn2+), cobalt (Co2+), cadmium (Cd2+), nickel (Ni2+), iron (Fe2+) and zinc (Zn2+), assembles to form a biologically active high molecular weight metalloenzyme; a 24-mer with 4-3-2 symmetry. Each 24-mer has 24 active sites, and contains around 1.5 metal ions per monomer, each monomer contributing residues to three separate active sites.
IGPD enzymes are monofunctional in fungi, plants, archaea and some eubacteria while they are encoded as bifunctional enzymes in other eubacteria, such that the enzyme is fused to histidinol-phosphate phosphatase, the penultimate enzyme of the histidine biosynthesis pathway. The histidine biosynthesis pathway is a potential target for development of herbicides, and IGPD is a target for the triazole phosphonate herbicides [ PUBMED:16338409 , PUBMED:14724278 , PUBMED:15042344 , PUBMED:10885480 , PUBMED:16511155 , PUBMED:10450980 , PUBMED:8066131 , PUBMED:3001645 , PUBMED:9767718 , PUBMED:8511965 , PUBMED:2664449 , PUBMED:3007936 ].
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)|
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This family is a member of clan S5 (CL0329), which has the following description:
This superfamily contains a wide range of families that possess a structure similar to the second domain of ribosomal S5 protein.
The clan contains the following 18 members:ChlI DNA_gyraseB DNA_mis_repair EFG_IV Fae GalKase_gal_bdg GHMP_kinases_N IGPD Lon_C LpxC Morc6_S5 Ribonuclease_P Ribosomal_S5_C Ribosomal_S9 RNase_PH Topo-VIb_trans UPF0029 Xol-1_N
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|Number in seed:||487|
|Number in full:||8422|
|Average length of the domain:||143 aa|
|Average identity of full alignment:||49 %|
|Average coverage of the sequence by the domain:||61.05 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||21|
|Download:||download the raw HMM for this family|
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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 135 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 sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.