Detail Information for IndEnz0010001109
IED ID IndEnz0010001109
Enzyme Type ID esterase001109
Protein Name Ferri-bacillibactin esterase BesA
EC 3.1.-.-
Bacillibactin trilactone hydrolase
Gene Name besA yuiI BSU32010
Organism Bacillus subtilis (strain 168)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168)
Enzyme Sequence MKEQTTDRTNGGTSNAFTIPGTEVRMMSSRNENRTYHIFISKPSTPPPPAGYPVIYLLDANSVFGTMTEAVRIQGRRPEKTGVIPAVIVGIGYETAEPFSSARHRDFTMPTAQSKLPERPDGREWPEHGGAEGFFRFIEEDLKPEIERDYQIDKKRQTIFGHSLGGLFVLQVLLTKPDAFQTYIAGSPSIHWNKPFILKKTDHFVSLTKKNNQPINILLAAGELEQHHKSRMNDNARELYERLAVLSEQGIRAEFCEFSGEGHISVLPVLVSRALRFALHPDGPHLSMG
Enzyme Length 289
Uniprot Accession Number O32102
Absorption
Active Site ACT_SITE 163; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 225; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 263; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.1.-.-
Enzyme Function FUNCTION: Catalyzes the hydrolysis of the trilactone cycle of ferri-bacillibactin (ferri-BB) complex, leading to the formation of bacillibactin monomers and to cytosolic iron release, thus making iron available for metabolic use. Can also hydrolyze bacillibactin (BB), however the catalytic efficiency for ferri-BB hydrolysis is much higher than for BB. {ECO:0000269|PubMed:16889643}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1)
Keywords Cytoplasm;Hydrolase;Reference proteome;Serine esterase
Interact With
Induction INDUCTION: Repressed by fur in the presence of iron. {ECO:0000269|PubMed:12354229}.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:16889643}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 32,439
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.54 uM for ferri-bacillibactin complex {ECO:0000269|PubMed:16889643}; KM=24.4 uM for bacillibactin {ECO:0000269|PubMed:16889643}; KM=221 uM for enterobactin {ECO:0000269|PubMed:16889643};
Metal Binding
Rhea ID
Cross Reference Brenda