Entry: Q7AQG7 Genes: ML0662 Length: 255 aa

Histidinol-phosphatase

Q7AQG7_MYCLE • Mycobacterium leprae (strain TN)
Navigate Overview Model Scores RCSB 1D Mol* Pockets B-Cell Epitopes Function and interactions Ontology and localisation Evidence and cross-references

Summary

Download FASTA UniProt: Q7AQG7 ML Locus: ML0662
Entry Q7AQG7
Reviewed unreviewed
Entry Name Q7AQG7_MYCLE
Gene Names ML0662
ML locus tag ML0662
Organism Mycobacterium leprae (strain TN)
Length 255 aa
Mass 27041 Da
Annotation 2.0
Annotation Summary

Evidence and cross-references

PubMed ID 11234002
DOI ID 10.1038/35059006
STRING 272631.gene:17574485;
KEGG mle:ML0662;
eggNOG COG0483;
OrthoDB 9772456at2;
InterPro IPR011809;IPR020583;IPR000760;

Oligomer Models

Best Boltz2 oligomer and local AlphaFold‑3 homooligomer structure models matched to ML0662, with the same model switching, Mol*, Nightingale, pLDDT, PAE, and download functionality as monomers.
Count: 2
Assembly Method Template / Source Overall Rank Download
Homo 2-mer Boltz2 5ZON 0.939099 Download Model
homo 2-mer AlphaFold‑3 — — Download Model

Ligands

Curated ligands imported from the selected oligomer template/YAML rows. The displayed ligand code is the original template CCD code; predicted-model placeholders such as LIG1/LIG2 are not shown. Click a ligand code to focus the ligand in Mol*.
Ligands: 0
Ligand Code Ligand Name PubChem ID
No curated ligand rows were found for this oligomer in the database.

Monomer Models

Monomer structure models for ML0662, retaining all existing model selection, Mol*, Nightingale, pLDDT, PAE, and download functionality.
Count: 4
Assembly Method Model Overall Rank Download
Monomer Boltz2 0 0.941091 Download Model
Monomer AlphaFold‑3 2 0.946191 Download Model
Monomer Boltz 0 0.944694 Download Model
Monomer CHAI 1 0.192626 Download Model

Sequence & Feature Viewer

Residue-level feature tracks for the loaded model — pLDDT confidence colouring, mapped annotations, and interactive PAE selection ranges. Drag a region on the heatmap to highlight it here and in Mol*.
RCSB 1D
Sequence viewer will initialise once a structure model is loaded.
Mol* — ML0662

Mol* Structure Viewer

Local mmCIF model display for ML0662 with Mol* controls hidden.
Default: Homo 2-mer • Boltz2
Preparing Homo 2-mer • Boltz2 model 0 for ML0662…
Residue focus: none
Heterooligomer ML IDs / chain selection

PAE Map Panel

Predicted aligned error heatmap for the currently loaded model, when pairwise confidence data are available in the local mmCIF.
PAE • Waiting for Model
PAE Heatmap
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Scored residue
Aligned residue
Hover over the heatmap to inspect residue-pair PAE values.
Click a cell or drag across the heatmap to select residue blocks and mirror them in the sequence viewer.

B-cell Epitope Propensity

Per-residue conformational B-cell epitope predictions from DiscoTope-3.0.
Epitope · Loading
Low
Epitope
Residue number Residue type DiscoTope-3.0 score Focus
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Click a residue to focus it in Mol*.
Annotation Summary

Function and interactions

EC number 3.1.3.15
Pathway PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9. {ECO:0000256|ARBA:ARBA00004970}.
Catalytic activity CATALYTIC ACTIVITY: Reaction=L-histidinol phosphate + H2O = L-histidinol + phosphate; Xref=Rhea:RHEA:14465, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57699, ChEBI:CHEBI:57980; EC=3.1.3.15; Evidence={ECO:0000256|ARBA:ARBA00049158};
Binding site BINDING 61; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR600760-2"; BINDING 77; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR600760-2"; BINDING 79; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR600760-2"; BINDING 80; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR600760-2"; BINDING 206; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /ligand_label="1"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR600760-2"
Cofactor COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|PIRSR:PIRSR600760-2};
Annotation Summary

Ontology and localisation

Gene Ontology (biological process) inositol metabolic process [GO:0006020]; L-histidine biosynthetic process [GO:0000105]; signal transduction [GO:0007165]
Gene Ontology (GO) histidinol-phosphatase activity [GO:0004401]; inositol monophosphate 1-phosphatase activity [GO:0008934]; metal ion binding [GO:0046872]; inositol metabolic process [GO:0006020]; L-histidine biosynthetic process [GO:0000105]; signal transduction [GO:0007165]
Gene Ontology (molecular function) histidinol-phosphatase activity [GO:0004401]; inositol monophosphate 1-phosphatase activity [GO:0008934]; metal ion binding [GO:0046872]
Gene Ontology IDs GO:0000105; GO:0004401; GO:0006020; GO:0007165; GO:0008934; GO:0046872
Protein families Inositol monophosphatase superfamily
Sequence similarities SIMILARITY: Belongs to the inositol monophosphatase superfamily. {ECO:0000256|ARBA:ARBA00009759}.