| IED ID | IndEnz0002009144 |
| Enzyme Type ID | protease009144 |
| Protein Name |
Aminopyrimidine aminohydrolase EC 3.5.99.2 Thiaminase II |
| Gene Name | tenA SAR2183 |
| Organism | Staphylococcus aureus (strain MRSA252) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus aureus Staphylococcus aureus (strain MRSA252) |
| Enzyme Sequence | MEFSQKLYQAAKPIINDIYEDDFIQKMLLGNIQADALRHYLQADAAYLKEFTNLYALLIPKMNSMNDVKFLVEQIEFMVEGEVLAHDILAQIVGESYEEIIKTKVWPPSGDHYIKHMYFQAHSRENAIYTIAAMAPCPYIYAELAKRSQSDHKLNREKDTAKWFDFYSTEMDDIINVFESLMNKLAESMSDKELEQVKQVFLESCIHERRFFNMAMTLEQWEFGGKVND |
| Enzyme Length | 229 |
| Uniprot Accession Number | Q6GEY1 |
| Absorption | |
| Active Site | ACT_SITE 137; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P25052; ACT_SITE 208; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P25052 |
| Activity Regulation | |
| Binding Site | BINDING 44; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P25052; BINDING 141; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P25052; BINDING 167; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P25052 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + NH4(+); Xref=Rhea:RHEA:31799, ChEBI:CHEBI:15377, ChEBI:CHEBI:16892, ChEBI:CHEBI:28938, ChEBI:CHEBI:63416; EC=3.5.99.2; Evidence={ECO:0000250|UniProtKB:P25052}; CATALYTIC ACTIVITY: Reaction=H2O + thiamine = 4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole + H(+); Xref=Rhea:RHEA:17509, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892, ChEBI:CHEBI:17957, ChEBI:CHEBI:18385; EC=3.5.99.2; Evidence={ECO:0000269|PubMed:24311574}; |
| DNA Binding | |
| EC Number | 3.5.99.2 |
| Enzyme Function | FUNCTION: Catalyzes an amino-pyrimidine hydrolysis reaction at the C5' of the pyrimidine moiety of thiamine compounds, a reaction that is part of a thiamine salvage pathway. Thus, catalyzes the conversion of 4-amino-5-aminomethyl-2-methylpyrimidine to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) (By similarity). Is also able to catalyze the hydrolytic cleavage of thiamine; however, this thiaminase activity may not be physiologically relevant. Therefore, is probably involved in the regeneration of the thiamine pyrimidine from thiamine degraded products present in the environment, rather than in thiamine degradation. {ECO:0000250|UniProtKB:P25052, ECO:0000269|PubMed:24311574, ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. {ECO:0000250|UniProtKB:P25052}. |
| nucleotide Binding | |
| Features | Active site (2); Binding site (3); Chain (1); Helix (13); Mutagenesis (2); Site (1); Turn (1) |
| Keywords | 3D-structure;Hydrolase;Thiamine biosynthesis |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4FN6; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 26,841 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.40 mM for thiamine {ECO:0000269|PubMed:24311574}; Note=kcat is 4.07 msec(-1) for the hydrolysis of thiamine. {ECO:0000269|PubMed:24311574}; |
| Metal Binding | |
| Rhea ID | RHEA:31799; RHEA:17509 |
| Cross Reference Brenda |