Summary: Myo-inositol-1-phosphate synthase
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This is the Wikipedia entry entitled "Inositol-3-phosphate synthase". More...
Inositol-3-phosphate synthase Edit Wikipedia article
| inositol-3-phosphate synthase | |||||||||
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| Identifiers | |||||||||
| EC number | 5.5.1.4 | ||||||||
| CAS number | 9032-95-5 | ||||||||
| 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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| Myo-inositol-1-phosphate synthase | |||||||||
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| myo-inositol phosphate synthase mips from a. fulgidus | |||||||||
| Identifiers | |||||||||
| Symbol | Inos-1-P_synth | ||||||||
| Pfam | PF01658 | ||||||||
| InterPro | IPR013021 | ||||||||
| SCOP | 1gr0 | ||||||||
| SUPERFAMILY | 1gr0 | ||||||||
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In enzymology, an inositol-3-phosphate synthase (EC 5.5.1.4) is an enzyme that catalyzes the chemical reaction
- D-glucose 6-phosphate
1D-myo-inositol 3-phosphate
Hence, this enzyme has one substrate, D-glucose 6-phosphate, and one product, 1D-myo-inositol 3-phosphate.
This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is 1D-myo-inositol-3-phosphate lyase (isomerizing). Other names in common use include myo-inositol-1-phosphate synthase, D-glucose 6-phosphate cycloaldolase, inositol 1-phosphate synthatase, glucose 6-phosphate cyclase, inositol 1-phosphate synthetase, glucose-6-phosphate inositol monophosphate cycloaldolase, glucocycloaldolase, and 1L-myo-inositol-1-phosphate lyase (isomerizing).
This enzyme participates in streptomycin biosynthesis and inositol phosphate metabolism. It employs one cofactor, NAD+. The reaction this enzyme catalyses represents the first committed step in the production of all inositol-containing compounds, including phospholipids, either directly or by salvage. The enzyme exists in a cytoplasmic form in a wide range of plants, animals, and fungi. It has also been detected in several bacteria and a chloroplast form is observed in alga and higher plants. Inositol phosphates play an important role in signal transduction.
In Saccharomyces cerevisiae (Baker's yeast), the transcriptional regulation of the INO1 gene encoding inositol-3-phosphate synthase has been studied in detail and its expression is sensitive to the availability of phospholipid precursors as well as growth phase.[1] The regulation of the structural gene encoding 1L-myo-inositol-1-phosphate synthase has also been analyzed at the transcriptional level in the aquatic angiosperm, Spirodela polyrrhiza (Giant duckweed) and the halophyte, Mesembryanthemum crystallinum (Common ice plant).[2]
[edit] Structural studies
As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1GR0, 1JKF, 1JKI, 1LA2, 1P1F, 1P1H, 1P1I, 1P1J, 1P1K, 1RM0, 1VJP, and 1VKO.
[edit] References
- ^ Klig LS, Zobel PA, Devry CG, Losberger C (June 1994). "Comparison of INO1 gene sequences and products in Candida albicans and Saccharomyces cerevisiae". Yeast 10 (6): 789â800. doi:10.1002/yea.320100609. PMID 7975896.
- ^ Majumder AL, Johnson MD, Henry SA (September 1997). "1L-myo-inositol-1-phosphate synthase". Biochim. Biophys. Acta 1348 (1-2): 245â56. PMID 9370339.
[edit] Further reading
- Eisenberg F Jr (1967). "D-myoinositol 1-phosphate as product of cyclization of glucose 6-phosphate and substrate for a specific phosphatase in rat testis". J. Biol. Chem. 242 (7): 1375â82. PMID 4290245.
- Sherman WR, Stewart MA, Zinbo M (1969). "Mass spectrometric study on the mechanism of D-glucose 6-phosphate-L-myo-inositol 1-phosphate cyclase". J. Biol. Chem. 244 (20): 5703â8. PMID 4310603.
- Barnett JE, Corina DL (1968). "The mechanism of glucose 6-phosphate-D-myo-inositol 1-phosphate cyclase of rat testis. The involvement of hydrogen atoms". Biochem. J. 108 (1): 125â9. PMC 1198777. PMID 4297937. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1198777/.
- Barnett JE, Rasheed A, Corina DL (1973). "Partial reactions of D-glucose 6-phosphate-1L-myoinositiol 1-phosphate cyclase". Biochem. J. 131 (1): 21â30. PMC 1177435. PMID 4352864. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1177435/.
This article incorporates text from the public domain Pfam and InterPro IPR013021
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Myo-inositol-1-phosphate synthase Provide feedback
This is a family of myo-inositol-1-phosphate synthases. Inositol-1-phosphate catalyses the conversion of glucose-6- phosphate to inositol-1-phosphate, which is then dephosphorylated to inositol [1]. Inositol phosphates play an important role in signal transduction.
Literature references
-
Klig LS, Zobel PA, Devry CG, Losberger C; , Yeast 1994;10:789-800.: Comparison of INO1 gene sequences and products in Candida albicans and Saccharomyces cerevisiae. PUBMED:7975896 EPMC:7975896
External database links
| PANDIT: | PF01658 |
| Pseudofam: | PF01658 |
| SCOP: | 1gr0 |
| SYSTERS: | Inos-1-P_synth |
This tab holds annotation information from the InterPro database.
InterPro entry IPR013021
This is a region of myo-inositol-1-phosphate synthases that is related to the glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain.
1L-myo-Inositol-1-phosphate synthase (EC) catalyzes the conversion of D-glucose 6-phosphate to 1L-myo-inositol-1-phosphate, the first committed step in the production of all inositol-containing compounds, including phospholipids, either directly or by salvage. The enzyme exists in a cytoplasmic form in a wide range of plants, animals, and fungi. It has also been detected in several bacteria and a chloroplast form is observed in alga and higher plants. Inositol phosphates play an important role in signal transduction.
In Saccharomyces cerevisiae (Baker's yeast), the transcriptional regulation of the INO1 gene has been studied in detail [PUBMED:7975896] and its expression is sensitive to the availability of phospholipid precursors as well as growth phase. The regulation of the structural gene encoding 1L-myo-inositol-1-phosphate synthase has also been analyzed at the transcriptional level in the aquatic angiosperm, Spirodela polyrrhiza (Giant duckweed) and the halophyte, Mesembryanthemum crystallinum (Common ice plant) [PUBMED:9370339].
Domain organisation
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Alignments
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| Seed (60) |
Full (1141) |
Representative proteomes | NCBI (1086) |
Meta (280) |
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| RP15 (186) |
RP35 (341) |
RP55 (459) |
RP75 (533) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
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| Seed (60) |
Full (1141) |
Representative proteomes | NCBI (1086) |
Meta (280) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (186) |
RP35 (341) |
RP55 (459) |
RP75 (533) |
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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.
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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
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_959 (release 4.1) |
| Previous IDs: | none |
| Type: | Family |
| Author: | Bashton M, Bateman A |
| Number in seed: | 60 |
| Number in full: | 1141 |
| Average length of the domain: | 110.30 aa |
| Average identity of full alignment: | 40 % |
| Average coverage of the sequence by the domain: | 26.16 % |
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: | 112 | ||||||||||||
| Family (HMM) version: | 12 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
Structures
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 Inos-1-P_synth domain has been found. There are 36 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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1D-myo-inositol 3-phosphate
Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence