Entry: P37969 Genes: tsaD gcp ML0379 B1620_C3_226 B229_C3_246 u1620c u229e Length: 351 aa

tRNA N6-adenosine threonylcarbamoyltransferase

TSAD_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: P37969 ML Locus: ML0379
Entry P37969
Reviewed reviewed
Entry Name TSAD_MYCLE
Gene Names tsaD gcp ML0379 B1620_C3_226 B229_C3_246 u1620c u229e
ML locus tag ML0379
Organism Mycobacterium leprae (strain TN)
Length 351 aa
Mass 35406 Da
Annotation 3.0
Annotation Summary

Evidence and cross-references

PubMed ID 11234002; 1354834
DOI ID 10.1038/35059006; 10.1111/j.1365-2958.1992.tb01372.x
STRING 272631.gene:17574198;
KEGG mle:ML0379;
eggNOG COG0533;
OrthoDB 9806197at2;
InterPro IPR043129;IPR000905;IPR017861;IPR017860;IPR022450;

Oligomer Models

Best Boltz2 oligomer and local AlphaFold‑3 homooligomer structure models matched to ML0379, with the same model switching, Mol*, Nightingale, pLDDT, PAE, and download functionality as monomers.
Count: 1
Assembly Method Template / Source Overall Rank Download
Hetero 2-mer Boltz2 3ZEU 0.907004 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 ML0379, retaining all existing model selection, Mol*, Nightingale, pLDDT, PAE, and download functionality.
Count: 4
Assembly Method Model Overall Rank Download
Monomer Boltz2 0 0.925025 Download Model
Monomer AlphaFold‑3 4 0.951034 Download Model
Monomer Boltz 0 0.923803 Download Model
Monomer CHAI 2 0.190988 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* — ML0379

Mol* Structure Viewer

Local mmCIF model display for ML0379 with Mol* controls hidden.
Default: Hetero 2-mer • Boltz2
Preparing Hetero 2-mer • Boltz2 model 0 for ML0379…
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 2.3.1.234
Catalytic activity CATALYTIC ACTIVITY: Reaction=L-threonylcarbamoyladenylate + adenosine(37) in tRNA = N(6)-L-threonylcarbamoyladenosine(37) in tRNA + AMP + H(+); Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163, ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411, ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234; Evidence={ECO:0000255|HAMAP-Rule:MF_01445};
Binding site BINDING 124; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000255|HAMAP-Rule:MF_01445"; BINDING 128; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000255|HAMAP-Rule:MF_01445"; BINDING 146..150; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_01445"; BINDING 180; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_01445"; BINDING 193; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_01445"; BINDING 197; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_01445"; BINDING 285; /ligand="substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_01445"; BINDING 313; /ligand="Fe cation"; /ligand_id="ChEBI:CHEBI:24875"; /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
Cofactor COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-Rule:MF_01445}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01445};
Annotation Summary

Ontology and localisation

Gene Ontology (biological process) tRNA threonylcarbamoyladenosine modification [GO:0002949]
Gene Ontology (cellular component) cytoplasm [GO:0005737]
Gene Ontology (GO) cytoplasm [GO:0005737]; iron ion binding [GO:0005506]; tRNA N(6)-L-threonylcarbamoyladenine synthase activity [GO:0061711]; tRNA threonylcarbamoyladenosine modification [GO:0002949]
Gene Ontology (molecular function) iron ion binding [GO:0005506]; tRNA N(6)-L-threonylcarbamoyladenine synthase activity [GO:0061711]
Gene Ontology IDs GO:0002949; GO:0005506; GO:0005737; GO:0061711
Subcellular location [CC] SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01445}.
Protein families KAE1 / TsaD family
Sequence similarities SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-Rule:MF_01445}.
Annotation Summary

Sequence features and PTMs

Chain CHAIN 1..351; /note="tRNA N6-adenosine threonylcarbamoyltransferase"; /id="PRO_0000096969"