Detail Information for IndEnz0010000262
IED ID IndEnz0010000262
Enzyme Type ID esterase000262
Protein Name Diacylglycerol acyltransferase/mycolyltransferase Ag85B
DGAT
EC 2.3.1.122
EC 2.3.1.20
30 kDa extracellular protein
Acyl-CoA:diacylglycerol acyltransferase
Antigen 85 complex B
85B
Ag85B
Extracellular alpha-antigen
Fibronectin-binding protein B
Fbps B
Gene Name fbpB MRA_1897
Organism Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Enzyme Sequence MTDVSRKIRAWGRRLMIGTAAAVVLPGLVGLAGGAATAGAFSRPGLPVEYLQVPSPSMGRDIKVQFQSGGNNSPAVYLLDGLRAQDDYNGWDINTPAFEWYYQSGLSIVMPVGGQSSFYSDWYSPACGKAGCQTYKWETFLTSELPQWLSANRAVKPTGSAAIGLSMAGSSAMILAAYHPQQFIYAGSLSALLDPSQGMGPSLIGLAMGDAGGYKAADMWGPSSDPAWERNDPTQQIPKLVANNTRLWVYCGNGTPNELGGANIPAEFLENFVRSSNLKFQDAYNAAGGHNAVFNFPPNGTHSWEYWGAQLNAMKGDLQSSLGAG
Enzyme Length 325
Uniprot Accession Number A5U3Q3
Absorption
Active Site ACT_SITE 166; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 270; /evidence=ECO:0000250; ACT_SITE 302; /evidence=ECO:0000250
Activity Regulation
Binding Site BINDING 166; /note=Substrate; /evidence=ECO:0000250; BINDING 194; /note=Substrate; /evidence=ECO:0000250; BINDING 279; /note=Substrate; /evidence=ECO:0000250
Calcium Binding
catalytic Activity 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; 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;
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 for 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 (3); Chain (1); Disulfide bond (1); Region (4); Signal peptide (1)
Keywords Acyltransferase;Disulfide bond;Secreted;Signal;Transferase
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..40; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 34,581
Kinetics
Metal Binding
Rhea ID RHEA:23472; RHEA:10868
Cross Reference Brenda