| IED ID | IndEnz0010000396 |
| Enzyme Type ID | esterase000396 |
| Protein Name |
Deacetylase Atu3266 EC 3.1.1.- |
| Gene Name | Atu3266 |
| Organism | Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58)) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Hyphomicrobiales Rhizobiaceae Rhizobium/Agrobacterium group Agrobacterium Agrobacterium tumefaciens complex Agrobacterium fabrum Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58)) |
| Enzyme Sequence | MTSGEQAKTPLQAPILLTNVKPVGFGKGASQSSTDILIGGDGKIAAVGSALQAPADTQRIDAKGAFISPGWVDLHVHIWHGGTDISIRPSECGAERGVTTLVDAGSAGEANFHGFREYIIEPSRERIKAFLNLGSIGLVACNRVPELRDIKDIDLDRILECYAENSEHIVGLKVRASHVITGSWGVTPVKLGKKIAKILKVPMMVHVGEPPALYDEVLEILGPGDVVTHCFNGKSGSSIMEDEDLFNLAERCAGEGIRLDIGHGGASFSFKVAEAAIARGLLPFSISTDLHGHSMNFPVWDLATTMSKLLSVDMPFENVVEAVTRNPASVIRLDMENRLDVGQRADFTVFDLVDADLEATDSNGDVSRLKRLFEPRYAVIGAEAIAASRYIPRARKLVRHSHGYSWR |
| Enzyme Length | 407 |
| Uniprot Accession Number | Q7CS13 |
| 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 | Beta strand (18); Chain (1); Helix (13); 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 173; /note=N6-carboxylysine; /evidence=ECO:0000269|PubMed:23214420 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2OGJ; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 43,969 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.0 mM for acetyl-(R)-mandelate {ECO:0000269|PubMed:23214420}; |
| Metal Binding | METAL 75; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000269|PubMed:23214420; METAL 77; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000269|PubMed:23214420; METAL 173; /note=Zinc 1; via carbamate group; /evidence=ECO:0000269|PubMed:23214420; METAL 173; /note=Zinc 2; via carbamate group; /evidence=ECO:0000269|PubMed:23214420; METAL 206; /note=Zinc 2; via pros nitrogen; /evidence=ECO:0000269|PubMed:23214420; METAL 229; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000269|PubMed:23214420; METAL 289; /note=Zinc 1; /evidence=ECO:0000269|PubMed:23214420 |
| Rhea ID | |
| Cross Reference Brenda |