| IED ID | IndEnz0010000479 |
| Enzyme Type ID | esterase000479 |
| Protein Name |
Aclacinomycin 10-hydroxylase RdmB EC 4.1.1.- 15-demethoxy-epsilon-rhodomycin 10-hydroxylase 15-demethoxyaclacinomycin T |
| Gene Name | rdmB |
| Organism | Streptomyces purpurascens |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces purpurascens |
| Enzyme Sequence | MSSSSPGEPLEPTDQDLDVLLKNLGNLVTPMALRVAATLRLVDHLLAGADTLAGLADRTDTHPQALSRLVRHLTVVGVLEGGEKQGRPLRPTRLGMLLADGHPAQQRAWLDLNGAVSHADLAFTGLLDVVRTGRPAYAGRYGRPFWEDLSADVALADSFDALMSCDEDLAYEAPADAYDWSAVRHVLDVGGGNGGMLAAIALRAPHLRGTLVELAGPAERARRRFADAGLADRVTVAEGDFFKPLPVTADVVLLSFVLLNWSDEDALTILRGCVRALEPGGRLLVLDRADVEGDGADRFFSTLLDLRMLTFMGGRVRTRDEVVDLAGSAGLALASERTSGSTTLPFDFSILEFTAVSEEAAPAAQASEALPAQE |
| Enzyme Length | 374 |
| Uniprot Accession Number | Q54527 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by sinefungin and S-adenosyl-L-homocysteine. {ECO:0000269|PubMed:15548527}. |
| Binding Site | BINDING 171; /note="S-adenosyl-L-methionine"; /evidence="ECO:0000269|PubMed:14607118, ECO:0000269|PubMed:15548527"; BINDING 190; /note="S-adenosyl-L-methionine; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:14607118, ECO:0000269|PubMed:15548527"; BINDING 213; /note="S-adenosyl-L-methionine"; /evidence="ECO:0000269|PubMed:14607118, ECO:0000269|PubMed:15548527"; BINDING 255; /note="S-adenosyl-L-methionine"; /evidence="ECO:0000269|PubMed:14607118, ECO:0000269|PubMed:15548527"; BINDING 260; /note="Substrate"; /evidence="ECO:0000269|PubMed:15548527" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=15-demethylaclacinomycin T + AH2 + O2 = 10-decarboxymethylaclacinomycin T + A + CO2 + H2O; Xref=Rhea:RHEA:45800, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:17499, ChEBI:CHEBI:74354, ChEBI:CHEBI:85430; Evidence={ECO:0000269|PubMed:11004563, ECO:0000269|PubMed:15548527}; |
| DNA Binding | |
| EC Number | 4.1.1.- |
| Enzyme Function | FUNCTION: Involved in the biosynthesis of the anthracycline aclacinomycin which is an aromatic polyketide antibiotic that exhibits high cytotoxicity and is widely applied in the chemotherapy of a variety of cancers. In vivo and in vitro, RdmB catalyzes the removal of the carboxylic group from the C-10 position of 15-demethoxyaclacinomycin T coupled to hydroxylation at the same C-10 position. It could also catalyze the removal of the carboxylic group at the C-10 position of 15-demethoxy-epsilon-rhodomycin coupled to hydroxylation at the same C-10 position to yield rhodomycin B. The reaction catalyzes by RdmB is intriguing, since the enzyme does not use any of the cofactors usually associated with hydroxylases such as flavins and/or metal ions to activate molecular oxygen. {ECO:0000269|PubMed:11004563, ECO:0000269|PubMed:15548527}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Antibiotic biosynthesis; aclacinomycin biosynthesis.; PATHWAY: Antibiotic biosynthesis; rhodomycin biosynthesis. |
| nucleotide Binding | |
| Features | Beta strand (9); Binding site (5); Chain (1); Helix (21); Mutagenesis (1); Region (1); Turn (4) |
| Keywords | 3D-structure;Antibiotic biosynthesis;Direct protein sequencing;Lyase;S-adenosyl-L-methionine |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1QZZ; 1R00; 1XDS; 1XDU; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 39,797 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:45800 |
| Cross Reference Brenda |