Entry: Q7APW5 Genes: gatD ML2327 Length: 230 aa

Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD

Q7APW5_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: Q7APW5 ML Locus: ML2327
Entry Q7APW5
Reviewed unreviewed
Entry Name Q7APW5_MYCLE
Gene Names gatD ML2327
ML locus tag ML2327
Organism Mycobacterium leprae (strain TN)
Length 230 aa
Mass 24474 Da
Annotation 3.0
Annotation Summary

Evidence and cross-references

PubMed ID 11234002
DOI ID 10.1038/35059006
STRING 272631.gene:17576188;
KEGG mle:ML2327;
eggNOG COG3442;
OrthoDB 9782045at2;
InterPro IPR029062;IPR033949;IPR011698;IPR043702;

Oligomer Models

Best Boltz2 oligomer and local AlphaFold‑3 homooligomer structure models matched to ML2327, 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 7Q8E 0.929372 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 ML2327, retaining all existing model selection, Mol*, Nightingale, pLDDT, PAE, and download functionality.
Count: 4
Assembly Method Model Overall Rank Download
Monomer Boltz2 0 0.950436 Download Model
Monomer AlphaFold‑3 4 0.949535 Download Model
Monomer Boltz 0 0.952482 Download Model
Monomer CHAI 4 0.192187 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* — ML2327

Mol* Structure Viewer

Local mmCIF model display for ML2327 with Mol* controls hidden.
Default: Hetero 2-mer • Boltz2
Preparing Hetero 2-mer • Boltz2 model 0 for ML2327…
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 3.5.1.2; 6.3.5.13
Pathway PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02213}.
Catalytic activity CATALYTIC ACTIVITY: Reaction=L-glutamine + H2O = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; Evidence={ECO:0000256|HAMAP-Rule:MF_02213}; CATALYTIC ACTIVITY: Reaction=beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + L-glutamine + ATP + H2O = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + L-glutamate + ADP + phosphate + H(+); Xref=Rhea:RHEA:57928, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:60033, ChEBI:CHEBI:62233, ChEBI:CHEBI:456216; EC=6.3.5.13; Evidence={ECO:0000256|HAMAP-Rule:MF_02213};
Binding site BINDING 123; /ligand="substrate"; /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
Active site ACT_SITE 89; /note="Nucleophile"; /evidence="ECO:0000256|HAMAP-Rule:MF_02213"; ACT_SITE 189; /evidence="ECO:0000256|HAMAP-Rule:MF_02213"
Subunit structure SUBUNIT: Forms a heterodimer with MurT. {ECO:0000256|HAMAP-Rule:MF_02213}.
Annotation Summary

Ontology and localisation

Gene Ontology (biological process) cell wall organization [GO:0071555]; cobalamin biosynthetic process [GO:0009236]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360]
Gene Ontology (GO) carbon-nitrogen ligase activity on lipid II [GO:0140282]; glutaminase activity [GO:0004359]; cell wall organization [GO:0071555]; cobalamin biosynthetic process [GO:0009236]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360]
Gene Ontology (molecular function) carbon-nitrogen ligase activity on lipid II [GO:0140282]; glutaminase activity [GO:0004359]
Gene Ontology IDs GO:0004359; GO:0008360; GO:0009236; GO:0009252; GO:0071555; GO:0140282
Protein families CobB/CobQ family, GatD subfamily
Sequence similarities SIMILARITY: Belongs to the CobB/CobQ family. GatD subfamily. {ECO:0000256|HAMAP-Rule:MF_02213}.
Annotation Summary

Sequence features and PTMs

Domain [FT] DOMAIN 2..196; /note="CobB/CobQ-like glutamine amidotransferase"; /evidence="ECO:0000259|Pfam:PF07685"