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Information on EC 1.14.13.166 - 4-nitrocatechol 4-monooxygenase and Organism(s) Rhodococcus opacus and UniProt Accession Q6F4M8

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IUBMB Comments
Contains FAD. The enzyme catalyses the oxidation of 4-nitrocatechol with the concomitant removal of the nitro group as nitrite. Forms a two-component system with a flavoprotein reductase . The enzymes from the bacteria Lysinibacillus sphaericus JS905 and Rhodococcus sp. strain PN1 were shown to also catalyse EC 1.14.13.29, 4-nitrophenol 2-monooxygenase [1,2] while the enzyme from Pseudomonas sp. WBC-3 was shown to also catalyse EC 1.14.13.167, 4-nitrophenol 4-monooxygenase .
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This record set is specific for:
Rhodococcus opacus
UNIPROT: Q6F4M8 not found.
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The taxonomic range for the selected organisms is: Rhodococcus opacus
The enzyme appears in selected viruses and cellular organisms
Synonyms
pnp 4-monooxygenase, npda2, p-nitrophenol monooxygenase, para-nitrophenol 4-monooxygenase, more
PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
4-nitrocatechol,NAD(P)H:oxygen 4-oxidoreductase (4-hydroxylating, nitrite-forming)
Contains FAD. The enzyme catalyses the oxidation of 4-nitrocatechol with the concomitant removal of the nitro group as nitrite. Forms a two-component system with a flavoprotein reductase [1]. The enzymes from the bacteria Lysinibacillus sphaericus JS905 and Rhodococcus sp. strain PN1 were shown to also catalyse EC 1.14.13.29, 4-nitrophenol 2-monooxygenase [1,2] while the enzyme from Pseudomonas sp. WBC-3 was shown to also catalyse EC 1.14.13.167, 4-nitrophenol 4-monooxygenase [3].
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NPCA_RHOOP
528
0
59739
Swiss-Prot
-
NPCB_RHOOP
185
0
20111
Swiss-Prot
-