Entry: Q9CCP8 Genes: ribG ML0555 Length: 339 aa

Riboflavin biosynthesis protein RibD

Q9CCP8_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: Q9CCP8 ML Locus: ML0555
Entry Q9CCP8
Reviewed unreviewed
Entry Name Q9CCP8_MYCLE
Gene Names ribG ML0555
ML locus tag ML0555
Organism Mycobacterium leprae (strain TN)
Length 339 aa
Mass 35147 Da
Annotation 3.0
Annotation Summary

Evidence and cross-references

PubMed ID 11234002
DOI ID 10.1038/35059006
STRING 272631.gene:17574376;
KEGG mle:ML0555;
eggNOG COG0117;COG1985;
OrthoDB 9800865at2;
InterPro IPR016192;IPR002125;IPR016193;IPR024072;IPR004794;IPR002734;IPR050765;

Oligomer Models

Best Boltz2 oligomer and local AlphaFold‑3 homooligomer structure models matched to ML0555, with the same model switching, Mol*, Nightingale, pLDDT, PAE, and download functionality as monomers.
Count: 1
Assembly Method Template / Source Overall Rank Download
Homo 4-mer Boltz2 4G3M 0.766332 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 ML0555, retaining all existing model selection, Mol*, Nightingale, pLDDT, PAE, and download functionality.
Count: 4
Assembly Method Model Overall Rank Download
Monomer Boltz2 0 0.934252 Download Model
Monomer AlphaFold‑3 0 0.906709 Download Model
Monomer Boltz 0 0.934892 Download Model
Monomer CHAI 1 0.188654 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* — ML0555

Mol* Structure Viewer

Local mmCIF model display for ML0555 with Mol* controls hidden.
Default: Homo 4-mer • Boltz2
Preparing Homo 4-mer • Boltz2 model 0 for ML0555…
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.
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PAE Heatmap
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Scored residue
Aligned residue
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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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Annotation Summary

Function and interactions

EC number 1.1.1.193; 3.5.4.26
Pathway PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4. {ECO:0000256|ARBA:ARBA00004882, ECO:0000256|PIRNR:PIRNR006769}.; PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 3/4. {ECO:0000256|ARBA:ARBA00004910, ECO:0000256|PIRNR:PIRNR006769}.
Catalytic activity CATALYTIC ACTIVITY: Reaction=2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H2O + H(+) = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+); Xref=Rhea:RHEA:21868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:58453, ChEBI:CHEBI:58614; EC=3.5.4.26; Evidence={ECO:0000256|ARBA:ARBA00049886, ECO:0000256|PIRNR:PIRNR006769}; CATALYTIC ACTIVITY: Reaction=5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP(+) = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NADPH + H(+); Xref=Rhea:RHEA:17845, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58421, ChEBI:CHEBI:58453; EC=1.1.1.193; Evidence={ECO:0000256|ARBA:ARBA00049861, ECO:0000256|PIRNR:PIRNR006769};
Binding site BINDING 57; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR006769-3"; BINDING 82; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR006769-3"; BINDING 91; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000256|PIRSR:PIRSR006769-3"; BINDING 161; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000256|PIRSR:PIRSR006769-2"; BINDING 175; /ligand="substrate"; /evidence="ECO:0000256|PIRSR:PIRSR006769-2"; BINDING 177; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000256|PIRSR:PIRSR006769-2"; BINDING 191; /ligand="substrate"; /evidence="ECO:0000256|PIRSR:PIRSR006769-2"; BINDING 203; /ligand="substrate"; /evidence="ECO:0000256|PIRSR:PIRSR006769-2"; BINDING 207; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000256|PIRSR:PIRSR006769-2"; BINDING 211; /ligand="substrate"; /evidence="ECO:0000256|PIRSR:PIRSR006769-2"; BINDING 214; /ligand="substrate"; /evidence="ECO:0000256|PIRSR:PIRSR006769-2"; BINDING 272; /ligand="substrate"; /evidence="ECO:0000256|PIRSR:PIRSR006769-2"; BINDING 274..280; /ligand="NADP(+)"; /ligand_id="ChEBI:CHEBI:58349"; /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
Cofactor COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|PIRNR:PIRNR006769, ECO:0000256|PIRSR:PIRSR006769-3}; Note=Binds 1 zinc ion. {ECO:0000256|PIRNR:PIRNR006769, ECO:0000256|PIRSR:PIRSR006769-3};
Active site ACT_SITE 59; /note="Proton donor"; /evidence="ECO:0000256|PIRSR:PIRSR006769-1"
Annotation Summary

Ontology and localisation

Gene Ontology (biological process) riboflavin biosynthetic process [GO:0009231]
Gene Ontology (GO) 5-amino-6-(5-phosphoribosylamino)uracil reductase activity [GO:0008703]; diaminohydroxyphosphoribosylaminopyrimidine deaminase activity [GO:0008835]; zinc ion binding [GO:0008270]; riboflavin biosynthetic process [GO:0009231]
Gene Ontology (molecular function) 5-amino-6-(5-phosphoribosylamino)uracil reductase activity [GO:0008703]; diaminohydroxyphosphoribosylaminopyrimidine deaminase activity [GO:0008835]; zinc ion binding [GO:0008270]
Gene Ontology IDs GO:0008270; GO:0008703; GO:0008835; GO:0009231
Protein families HTP reductase family; Cytidine and deoxycytidylate deaminase family
Sequence similarities SIMILARITY: In the C-terminal section; belongs to the HTP reductase family. {ECO:0000256|ARBA:ARBA00007417, ECO:0000256|PIRNR:PIRNR006769}.; SIMILARITY: In the N-terminal section; belongs to the cytidine and deoxycytidylate deaminase family. {ECO:0000256|ARBA:ARBA00005259, ECO:0000256|PIRNR:PIRNR006769}.
Annotation Summary

Sequence features and PTMs

Domain [FT] DOMAIN 7..129; /note="CMP/dCMP-type deaminase"; /evidence="ECO:0000259|PROSITE:PS51747"