Entry: Q9CCP9 Genes: rpe ML0554 Length: 224 aa

Ribulose-phosphate 3-epimerase

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

Summary

Download FASTA UniProt: Q9CCP9 ML Locus: ML0554
Entry Q9CCP9
Reviewed reviewed
Entry Name RPE_MYCLE
Gene Names rpe ML0554
ML locus tag ML0554
Organism Mycobacterium leprae (strain TN)
Length 224 aa
Mass 23408 Da
Annotation 3.0
Annotation Summary

Evidence and cross-references

PubMed ID 11234002
DOI ID 10.1038/35059006
STRING 272631.gene:17574375;
KEGG mle:ML0554;
eggNOG COG0036;
OrthoDB 1645589at2;
InterPro IPR013785;IPR026019;IPR000056;IPR011060;

Oligomer Models

Best Boltz2 oligomer and local AlphaFold‑3 homooligomer structure models matched to ML0554, with the same model switching, Mol*, Nightingale, pLDDT, PAE, and download functionality as monomers.
Count: 1
Assembly Method Template / Source Overall Rank Download
Homo 3-mer Boltz2 7SBJ 0.768574 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 ML0554, retaining all existing model selection, Mol*, Nightingale, pLDDT, PAE, and download functionality.
Count: 4
Assembly Method Model Overall Rank Download
Monomer Boltz2 0 0.963187 Download Model
Monomer AlphaFold‑3 2 0.965270 Download Model
Monomer Boltz 0 0.962347 Download Model
Monomer CHAI 2 0.193517 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* — ML0554

Mol* Structure Viewer

Local mmCIF model display for ML0554 with Mol* controls hidden.
Default: Homo 3-mer • Boltz2
Preparing Homo 3-mer • Boltz2 model 0 for ML0554…
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
Loading pairwise confidence data for the selected model…
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
Loading epitope predictions…
Click a residue to focus it in Mol*.
Annotation Summary

Function and interactions

EC number 5.1.3.1
Pathway PATHWAY: Carbohydrate degradation. {ECO:0000255|HAMAP-Rule:MF_02227}.
Catalytic activity CATALYTIC ACTIVITY: Reaction=D-ribulose 5-phosphate = D-xylulose 5-phosphate; Xref=Rhea:RHEA:13677, ChEBI:CHEBI:57737, ChEBI:CHEBI:58121; EC=5.1.3.1; Evidence={ECO:0000255|HAMAP-Rule:MF_02227};
Binding site BINDING 8; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_02227"; BINDING 31; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000255|HAMAP-Rule:MF_02227"; BINDING 33; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000255|HAMAP-Rule:MF_02227"; BINDING 64; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000255|HAMAP-Rule:MF_02227"; BINDING 64; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_02227"; BINDING 140..143; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_02227"; BINDING 173..175; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_02227"; BINDING 173; /ligand="a divalent metal cation"; /ligand_id="ChEBI:CHEBI:60240"; /evidence="ECO:0000255|HAMAP-Rule:MF_02227"; BINDING 195..196; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
Cofactor COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_02227}; Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-Rule:MF_02227};
Active site ACT_SITE 33; /note="Proton acceptor"; /evidence="ECO:0000255|HAMAP-Rule:MF_02227"; ACT_SITE 173; /note="Proton donor"; /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
Annotation Summary

Ontology and localisation

Gene Ontology (biological process) pentose catabolic process [GO:0019323]; pentose-phosphate shunt [GO:0006098]
Gene Ontology (cellular component) cytoplasm [GO:0005737]
Gene Ontology (GO) cytoplasm [GO:0005737]; D-ribulose-phosphate 3-epimerase activity [GO:0004750]; metal ion binding [GO:0046872]; pentose catabolic process [GO:0019323]; pentose-phosphate shunt [GO:0006098]
Gene Ontology (molecular function) D-ribulose-phosphate 3-epimerase activity [GO:0004750]; metal ion binding [GO:0046872]
Gene Ontology IDs GO:0004750; GO:0005737; GO:0006098; GO:0019323; GO:0046872
Protein families Ribulose-phosphate 3-epimerase family
Sequence similarities SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family. {ECO:0000255|HAMAP-Rule:MF_02227}.
Annotation Summary

Sequence features and PTMs

Chain CHAIN 1..224; /note="Ribulose-phosphate 3-epimerase"; /id="PRO_0000171576"