IED ID | IndEnz0010000714 |
Enzyme Type ID | esterase000714 |
Protein Name |
Deacetylase EF_0837 EC 3.1.1.- |
Gene Name | EF_0837 I574_01240 OO5_02741 |
Organism | Enterococcus faecalis (strain ATCC 700802 / V583) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Enterococcaceae Enterococcus Enterococcus faecalis (Streptococcus faecalis) Enterococcus faecalis (strain ATCC 700802 / V583) |
Enzyme Sequence | MDYDLLIKNGQTVNGMPVEIAIKEKKIAAVAATISGSAKETIHLEPGTYVSAGWIDDHVHCFEKMALYYDYPDEIGVKKGVTTVIDAGTTGAENIHEFYDLAQQAKTNVFGLVNISKWGIVAQDELADLSKVQASLVKKAIQELPDFVVGIKARMSRTVIGDNGITPLELAKQIQQENQEIPLMVHIGSAPPHLDEILALMEKGDVLTHCFNGKENGILDQATDKIKDFAWQAYNKGVVFDIGHGTDSFNFHVAETALREGMKAASISTDIYIRNRENGPVYDLATTMEKLRVVGYDWPEIIEKVTKAPAENFHLTQKGTLEIGKDADLTIFTIQAEEKTLTDSNGLTRVAKEQIRPIKTIIGGQIYDN |
Enzyme Length | 369 |
Uniprot Accession Number | Q837K0 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.1.1.- |
Enzyme Function | FUNCTION: Esterase that can catalyze the deacetylation of acetyl-(R)-mandelate, but with very low efficiency (in vitro). {ECO:0000269|PubMed:23214420}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Beta strand (21); Chain (1); Helix (14); Metal binding (7); Modified residue (1); Site (1); Turn (7) |
Keywords | 3D-structure;Hydrolase;Metal-binding;Reference proteome;Zinc |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | MOD_RES 152; /note=N6-carboxylysine; /evidence=ECO:0000269|PubMed:23214420 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 2ICS; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 40,658 |
Kinetics | |
Metal Binding | METAL 58; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000269|PubMed:23214420; METAL 60; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000269|PubMed:23214420; METAL 152; /note=Zinc 1; via carbamate group; /evidence=ECO:0000269|PubMed:23214420; METAL 152; /note=Zinc 2; via carbamate group; /evidence=ECO:0000269|PubMed:23214420; METAL 186; /note=Zinc 2; via pros nitrogen; /evidence=ECO:0000269|PubMed:23214420; METAL 209; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000269|PubMed:23214420; METAL 270; /note=Zinc 1; /evidence=ECO:0000269|PubMed:23214420 |
Rhea ID | |
Cross Reference Brenda |