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Information on EC 1.14.13.211 - rifampicin monooxygenase
for references in articles please use BRENDA:EC1.14.13.211
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
1.14.13.211 rifampicin monooxygenase
IUBMB Comments
The enzyme has been found in the Corynebacteria Rhodococcus equi and Nocardia farcinica. It confers increased resistance to the antibiotic rifampicin by initiating its degradation.
The enzyme appears in viruses and cellular organisms
showSynonyms
rifmo, rifampicin monooxygenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
RIF-O
-
-
-
-
rifampicin monooxygenase
RifMO
rox
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
rifampicin + NAD(P)H + O2 = 2'-N-hydroxyrifampicin + NAD(P)+ + H2O
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-
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SYSTEMATIC NAME
IUBMB Comments
rifampicin:NAD(P)H:oxygen oxidoreductase (2'-N-hydroxyrifampicin-forming)
The enzyme has been found in the Corynebacteria Rhodococcus equi and Nocardia farcinica. It confers increased resistance to the antibiotic rifampicin by initiating its degradation.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
16-demethylrifamycin W + NAD(P)H + O2
? + NAD(P)+ + H2O
-
Substrates: -
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16-demethylrifamycin W + NAD(P)H + O2
? + NAD(P)+ + H2O
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Substrates: -
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16-demethylrifamycin W + NAD(P)H + O2
? + NAD(P)+ + H2O
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Substrates: -
Products: -
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rifampicin + NAD(P)H + O2
2'-N-hydroxyrifampicin + NAD(P)+ + H2O
-
Substrates: -
Products: -
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?
rifampicin + NAD(P)H + O2
2'-N-hydroxyrifampicin + NAD(P)+ + H2O
Substrates: -
Products: -
Products: -
?
rifampicin + NAD(P)H + O2
2'-N-hydroxyrifampicin + NAD(P)+ + H2O
-
Substrates: -
Products: -
Products: -
?
rifampicin + NAD(P)H + O2
2'-N-hydroxyrifampicin + NAD(P)+ + H2O
Substrates: -
Products: -
Products: -
?
rifamycin SV + NAD(P)H + O2
? + NAD(P)+ + H2O
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Substrates: -
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rifamycin SV + NAD(P)H + O2
? + NAD(P)+ + H2O
-
Substrates: -
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?
rifamycin SV + NAD(P)H + O2
? + NAD(P)+ + H2O
-
Substrates: -
Products: -
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rifamycin SV + NAD(P)H + O2
? + NAD(P)+ + H2O
-
Substrates: -
Products: -
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rifamycin SV + NAD(P)H + O2
? + NAD(P)+ + H2O
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Substrates: -
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additional information
?
-
Substrates: the enzyme from Rhodococcus equi has the ability to inactivate the antibiotic rifampicin via its decomposition and confers low-level rifampin resistance
Products: -
Products: -
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additional information
?
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Rhodococcus equi ATCC 14887
Substrates: the enzyme from Rhodococcus equi has the ability to inactivate the antibiotic rifampicin via its decomposition and confers low-level rifampin resistance
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
rifampicin + NAD(P)H + O2
2'-N-hydroxyrifampicin + NAD(P)+ + H2O
-
Substrates: -
Products: -
Products: -
?
rifampicin + NAD(P)H + O2
2'-N-hydroxyrifampicin + NAD(P)+ + H2O
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme from Rhodococcus equi has the ability to inactivate the antibiotic rifampicin via its decomposition and confers low-level rifampin resistance
Products: -
Products: -
?
additional information
?
-
Rhodococcus equi ATCC 14887
Substrates: the enzyme from Rhodococcus equi has the ability to inactivate the antibiotic rifampicin via its decomposition and confers low-level rifampin resistance
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
NADPH efficiently reduces the FAD only when rifampicin is present, implying that rifampicin binds before NADPH in the catalytic scheme
FAD
-
enzyme Rox is a probable FAD-dependent monooxygenase because it contains the FAD-binding domain (Pfam accession number PF01494)
FAD
NADPH efficiently reduces the FAD only when rifampicin is present, implying that rifampicin binds before NADPH in the catalytic scheme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
RIFMO catalyzes the hydroxylation of rifampicin at the C2 atom followed by cleavage of the ansa linkage, which leads to inactivation of the antibiotic by preventing key contacts with the RNA polymerase target
metabolism
-
RIFMO catalyzes the hydroxylation of rifampicin at the C2 atom followed by cleavage of the ansa linkage, which leads to inactivation of the antibiotic by preventing key contacts with the RNA polymerase target
-
physiological function
the enzyme from Rhodococcus equi has the ability to inactivate the antibiotic rifampicin via its decomposition and confers low-level rifampin resistance
physiological function
-
the rox gene is capable of initiating rifampicin degradation with another metabolite formation at the first step and having a role as the secondary rifampicin resistance factor in Nocardia farcinica
physiological function
-
the rox gene is capable of initiating rifampicin degradation with another metabolite formation at the first step and having a role as the secondary rifampicin resistance factor in Nocardia farcinica
-
physiological function
Rhodococcus equi ATCC 14887
-
the enzyme from Rhodococcus equi has the ability to inactivate the antibiotic rifampicin via its decomposition and confers low-level rifampin resistance
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ROX_NOCFA
Nocardia farcinica (strain IFM 10152)
473
0
51364
Swiss-Prot
Secretory Pathway (Reliability: 1)
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with rifampicin, to 1.8 A resolution. RifMO is a class A flavoprotein monooxygenase and is similar in fold and quaternary structure to MtmOIV and OxyS, in the mithramycin and oxytetracycline biosynthetic pathways, respectively. RifMO dimerizes via the FAD-binding domain to form a bell-shaped homodimer in solution with a maximal dimension of 110 A. The rifampicin naphthoquinone blocks access to the FAD N5 atom
structure of RIFMO in complex with the hydroxylated rifampicin product, to 2.10 A resolution. Structure shows a breach of the ansa aliphatic chain of rifampicin between naphthoquinone C2 and amide N1
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the rox gene deletion mutation DELTArox gives no significant influence to the rifampicin resistance of Nocardia farcinica. Transformation with plasmid pKNL027_N05 overexpressing the rox gene markedly raises the rifampicin resistance in the strain with the deletion mutation of the rpoB2 gene as the principal rifampicin resistance determinant. Rifampicin is degraded by the wild-type strain, whereas it remains intact when incubated with the DELTArox strain
additional information
-
the rox gene deletion mutation DELTArox gives no significant influence to the rifampicin resistance of Nocardia farcinica. Transformation with plasmid pKNL027_N05 overexpressing the rox gene markedly raises the rifampicin resistance in the strain with the deletion mutation of the rpoB2 gene as the principal rifampicin resistance determinant. Rifampicin is degraded by the wild-type strain, whereas it remains intact when incubated with the DELTArox strain
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene iri, DNA and amino acid sequence determination and analysis, recombinant expression, the gene cloned from the Rhodococcus equi strain ATCC 14887 confers a 10fold increase in resistance to rifampin in Escherichia coli as well as a 25fold increase in Rhodococcus
gene rox, cloning and expression of wild-type and mutant enzymes in Escherichia coli strains JM109 and BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hoshino, Y.;, Fujii, S., Shinonaga, H.; Arai, K.; Saito, F.; Fukai, T.; Satoh, H.; Miyazaki, Y.; Ishikawa, J.
Monooxygenation of rifampicin catalyzed by the rox gene product of Nocardia farcinica: structure elucidation, gene identification and role in drug resistance
J. Antibiot.
63
23-28
2010
Nocardia farcinica, Nocardia farcinica IFM 10152
brenda
Andersen, S.; Quan, S.; Gowan, B.; Dabbs, E.
Monooxygenase-like sequence of a Rhodococcus equi gene conferring increased resistance to rifampin by inactivating this antibiotic
Antimicrob. Agents Chemother.
41
218-221
1997
Rhodococcus equi (P95598), Rhodococcus equi ATCC 14887 (P95598)
brenda
Liu, L.K.; Abdelwahab, H.; Martin Del Campo, J.S.; Mehra-Chaudhary, R.; Sobrado, P.; Tanner, J.J.
The structure of the antibiotic deactivating, N-hydroxylating rifampicin monooxygenase
J. Biol. Chem.
291
21553-21562
2016
Nocardia farcinica (Q5YTV5), Nocardia farcinica, Nocardia farcinica IFM 10152 (Q5YTV5)
brenda
Liu, L.K.; Dai, Y.; Abdelwahab, H.; Sobrado, P.; Tanner, J.J.
Structural evidence for rifampicin monooxygenase inactivating rifampicin by cleaving its ansa-bridge
Biochemistry
57
2065-2068
2018
Nocardia farcinica (Q5YTV5), Nocardia farcinica IFM 10152 (Q5YTV5)
brenda
Zheng, X.; Liu, X.; Peng, S.; Zhou, Q.; Xu, B.; Yuan, H.; Tang, G.
Characterization of the rifamycin-degrading monooxygenase from rifamycin producers implicating its involvement in saliniketal biosynthesis
Front. Microbiol.
11
971
2020
Amycolatopsis mediterranei, Micromonospora sp. TP-A0468, Nocardioides dokdonensis, Salinispora arenicola, Streptomyces sp. TP-A0356
brenda
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Release 2023.1 (January 2023)
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