| IED ID | IndEnz0002007811 |
| Enzyme Type ID | protease007811 |
| Protein Name |
Murein peptide amidase A EC 3.4.17.- Gamma-D-Glu-Dap amidase Zinc metallocarboxypeptidase MpaA |
| Gene Name | mpaA VIBHAR_07057 |
| Organism | Vibrio campbellii (strain ATCC BAA-1116 / BB120) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio Vibrio harveyi group Vibrio campbellii Vibrio campbellii (strain ATCC BAA-1116 / BB120) |
| Enzyme Sequence | MNRYYSNNQEITVSLIPRTERAAFLITPTSYGKSVLGAPLLYFPAQVESNSRGLILAGTHGDETASIAGLSCALRSLPAECLKHDVILSMNPDANQLGTRANANQVDLNRAFPTQNWTEHGTVYRWSSHTPVRDVKVKTGDKEQLEPEVDALISLIELRRPKFVVSFHEPLAFVDDPAHSDLAKWLGKQFNLPIVDDVDYETPGSFGTWCNERQLPCITVELPPISADLTIEKHLDAFIALLQHDPDL |
| Enzyme Length | 248 |
| Uniprot Accession Number | A7N805 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate = L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate; Xref=Rhea:RHEA:28398, ChEBI:CHEBI:15377, ChEBI:CHEBI:57791, ChEBI:CHEBI:61395, ChEBI:CHEBI:61401; Evidence={ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000269|PubMed:22970852}; |
| DNA Binding | |
| EC Number | 3.4.17.- |
| Enzyme Function | FUNCTION: Involved in muropeptide degradation. Catalyzes the hydrolysis of the gamma-D-glutamyl-diaminopimelic acid (gamma-D-Glu-Dap) amide bond in the murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid, leading to the formation of L-Ala-gamma-D-Glu and Dap. Has weak activity with L-Ala-gamma-D-Glu-L-Lys, MurNAc-tripeptide and gamma-D-Glu-meso-Dap. Cannot hydrolyze murein tetrapeptide. {ECO:0000269|PubMed:22970852}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall degradation; peptidoglycan degradation. {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000305|PubMed:22970852}. |
| nucleotide Binding | |
| Features | Beta strand (11); Chain (1); Helix (9); Metal binding (3) |
| Keywords | 3D-structure;Carboxypeptidase;Cell wall biogenesis/degradation;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Protease;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02211}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4AXV; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 27,573 |
| Kinetics | |
| Metal Binding | METAL 60; /note="Zinc; via pros nitrogen"; /evidence="ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000269|PubMed:22970852, ECO:0007744|PDB:4AXV"; METAL 63; /note="Zinc"; /evidence="ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000269|PubMed:22970852, ECO:0007744|PDB:4AXV"; METAL 168; /note="Zinc; via pros nitrogen"; /evidence="ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000269|PubMed:22970852, ECO:0007744|PDB:4AXV" |
| Rhea ID | RHEA:28398 |
| Cross Reference Brenda |