| IED ID | IndEnz0010000713 |
| Enzyme Type ID | esterase000713 |
| Protein Name |
Deacetylase Oant_2987 EC 3.1.1.- |
| Gene Name | Oant_2987 |
| Organism | Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Hyphomicrobiales Brucellaceae Brucella/Ochrobactrum group Brucella Brucella anthropi (Ochrobactrum anthropi) Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi) |
| Enzyme Sequence | MISGEQAKPLLITNVKPVAFGVEHSDATTDILVGKDGSISAIGKSLNAPADVERVDGKGAWISPGWVDLHVHIWHGGTDISIRPSECGAERGVTTLVDAGSAGEANFHGFREYIIEPSKERIKAFLNLGSIGLVACNRVPELRDIKDIDLDRILECYAANSEHIVGIKVRASHVITGSWGVTPVKLGKKIAKILKVPMMVHVGEPPALYDEVLEILGPGDVVTHCFNGKSGSSIMEDEDLFNLAERCSGEGIRLDIGHGGASFSFKVAEAAIERGLLPFSISTDLHGHSMNFPVWDLATTMSKLLSVNMPFENVIEAVTHNPASVIKLSMENRLSVGQRADFTIFDLVDADLEATDSNGDVSRLNRLFEPRYAVIGAEAITASRYIPRARKLVRHSHGYSWR |
| Enzyme Length | 402 |
| Uniprot Accession Number | A6X391 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Esterase that catalyzes the deacetylation of acetyl-(R)-mandelate (in vitro). Can also hydrolyze acetyl glycolate, but with lower efficiency. Has very low N-acetyl-D-amino acid deacetylase activity with N-acetyl-D-serine and N-acetyl-D-threonine (in vitro). Theoretical substrate docking studies suggest that other N-acetylated amino acids may optimally occupy the active site and may in fact be the physiological substrates. {ECO:0000269|PubMed:23214420}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (7); Modified residue (1); Site (1) |
| Keywords | Hydrolase;Metal-binding;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 168; /note=N6-carboxylysine; /evidence=ECO:0000250 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 43,606 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 mM for acetyl-(R)-mandelate {ECO:0000269|PubMed:23214420}; |
| Metal Binding | METAL 70; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000250; METAL 72; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000250; METAL 168; /note=Zinc 1; via carbamate group; /evidence=ECO:0000250; METAL 168; /note=Zinc 2; via carbamate group; /evidence=ECO:0000250; METAL 201; /note=Zinc 2; via pros nitrogen; /evidence=ECO:0000250; METAL 224; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000250; METAL 284; /note=Zinc 1; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |