| IED ID | IndEnz0010000141 |
| Enzyme Type ID | esterase000141 |
| Protein Name |
Diacylglycerol acyltransferase/mycolyltransferase Ag85C DGAT EC 2.3.1.122 EC 2.3.1.20 Acyl-CoA:diacylglycerol acyltransferase Antigen 85 complex C 85C Ag85C Fibronectin-binding protein C Fbps C |
| Gene Name | fbpC fbpC2 ML2655 |
| Organism | Mycobacterium leprae (strain TN) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium leprae Mycobacterium leprae (strain TN) |
| Enzyme Sequence | MKFLQQMRKLFGLAAKFPARLTIAVIGTALLAGLVGVVGDTAIAVAFSKPGLPVEYLQVPSPSMGHDIKIQFQGGGQHAVYLLDGLRAQEDYNGWDINTPAFEEYYHSGLSVIMPVGGQSSFYSNWYQPSQGNGQHYTYKWETFLTQEMPSWLQANKNVLPTGNAAVGLSMSGSSALILASYYPQQFPYAASLSGFLNPSEGWWPTMIGLAMNDSGGYNANSMWGPSTDPAWKRNDPMVQIPRLVANNTRIWVYCGNGAPNELGGDNIPAKFLESLTLSTNEIFQNTYAASGGRNGVFNFPPNGTHSWPYWNQQLVAMKPDIQQILNGSNNNA |
| Enzyme Length | 333 |
| Uniprot Accession Number | Q05862 |
| Absorption | |
| Active Site | ACT_SITE 170; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 274; /evidence=ECO:0000250; ACT_SITE 306; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 170; /note=Substrate; /evidence=ECO:0000250; BINDING 198; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; CATALYTIC ACTIVITY: Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose 6,6'-bismycolate + alpha,alpha-trehalose; Xref=Rhea:RHEA:23472, ChEBI:CHEBI:16551, ChEBI:CHEBI:18195, ChEBI:CHEBI:18234; EC=2.3.1.122; |
| DNA Binding | |
| EC Number | 2.3.1.122; 2.3.1.20 |
| Enzyme Function | FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria to fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (2); Chain (1); Region (4); Signal peptide (1) |
| Keywords | Acyltransferase;Reference proteome;Secreted;Signal;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..44; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 36,392 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:10868; RHEA:23472 |
| Cross Reference Brenda |