Detail Information for IndEnz0010000148
IED ID IndEnz0010000148
Enzyme Type ID esterase000148
Protein Name Pimeloyl-
acyl-carrier protein methyl ester esterase
EC 3.1.1.85
Biotin synthesis protein BioH
Carboxylesterase BioH
Gene Name bioH SF3435 S4329
Organism Shigella flexneri
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Shigella Shigella flexneri
Enzyme Sequence MNNIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPDKAIWLGWSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARALKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFISHPVEFCHLLVALKQRVLVVSES
Enzyme Length 262
Uniprot Accession Number Q83PW0
Absorption
Active Site ACT_SITE 82; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_01260; ACT_SITE 207; /evidence=ECO:0000255|HAMAP-Rule:MF_01260; ACT_SITE 235; /evidence=ECO:0000255|HAMAP-Rule:MF_01260
Activity Regulation
Binding Site BINDING 22; /note=Substrate; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000255|HAMAP-Rule:MF_01260; BINDING 235; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_01260
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=6-carboxyhexanoyl-[ACP] methyl ester + H2O = 6-carboxyhexanoyl-[ACP] + H(+) + methanol; Xref=Rhea:RHEA:42700, Rhea:RHEA-COMP:9955, Rhea:RHEA-COMP:10186, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:78846, ChEBI:CHEBI:82735; EC=3.1.1.85; Evidence={ECO:0000255|HAMAP-Rule:MF_01260};
DNA Binding
EC Number 3.1.1.85
Enzyme Function FUNCTION: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. {ECO:0000255|HAMAP-Rule:MF_01260}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Cofactor biosynthesis; biotin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01260}.
nucleotide Binding
Features Active site (3); Beta strand (8); Binding site (2); Chain (1); Domain (1); Helix (13); Region (2)
Keywords 3D-structure;Biotin biosynthesis;Cytoplasm;Hydrolase;Reference proteome;Serine esterase
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01260}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 4ETW;
Mapped Pubmed ID 23045647;
Motif
Gene Encoded By
Mass 29,148
Kinetics
Metal Binding
Rhea ID RHEA:42700
Cross Reference Brenda 3.1.1.85;