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UniProtKB - Q2PWU9 (DNTB_BURSP)
Protein
4-methyl-5-nitrocatechol 5-monooxygenase
Gene
dntB
Organism
Burkholderia sp.
Status
Functioni
Involved in the degradation of 2,4-dinitrotoluene (2,4-DNT). Catalyzes the removal of the nitro group from 4-methyl-5-nitrocatechol (MNC) to yield 2-hydroxy-5-methylquinone (PubMed:8830701, PubMed:16751499).
It can use both NADH and NADPH as electron donors, but prefers NADPH (PubMed:8830701).
Also able to use 4-nitrocatechol as substrate (PubMed:8830701).
2 PublicationsCatalytic activityi
- 4-methyl-5-nitrocatechol + NADPH + O2 = 2-hydroxy-5-methylquinone + H+ + H2O + NADP+ + nitrite2 PublicationsEC:1.14.13.2102 Publications
- 4-methyl-5-nitrocatechol + NADH + O2 = 2-hydroxy-5-methylquinone + H+ + H2O + NAD+ + nitrite2 PublicationsEC:1.14.13.2102 Publications
Cofactori
FAD1 PublicationNote: Binds 1 FAD per subunit.1 Publication
Activity regulationi
Activated by magnesium or manganese ions. Inhibited by concentrations of 4-methyl-5-nitrocatechol (MNC) above 2 mM.1 Publication
Kineticsi
kcat is 0.014 sec(-1) with 4-nitrophenol (4NP) as substrate.1 Publication
- KM=15.5 µM for NADPH1 Publication
- KM=50 µM for oxygen1 Publication
- KM=350 µM for 4-nitrophenol (4NP)1 Publication
- KM=1220 µM for NADH1 Publication
- Vmax=14 nmol/min/mg enzyme with 4-nitrophenol (4NP) as substrate1 Publication
GO - Molecular functioni
- FAD binding Source: InterPro
- monooxygenase activity Source: UniProtKB-KW
GO - Biological processi
- aromatic compound catabolic process Source: UniProtKB-KW
Keywordsi
Molecular function | Monooxygenase, Oxidoreductase |
Biological process | Aromatic hydrocarbons catabolism |
Ligand | FAD, Flavoprotein, NAD, NADP |
Enzyme and pathway databases
BRENDAi | 1.14.13.210, 1033 |
Names & Taxonomyi
Protein namesi | Recommended name: 4-methyl-5-nitrocatechol 5-monooxygenase1 Publication (EC:1.14.13.2102 Publications)Short name: 4M5NC monooxygenase1 Publication Short name: MNC monooxygenase1 Publication Alternative name(s): 4-methyl-5-nitrocatechol oxygenase1 Publication |
Gene namesi | Name:dntB1 Publication |
Organismi | Burkholderia sp. |
Taxonomic identifieri | 36773 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 22 | M → L: Able to accept the two new substrates 4-nitrophenol (4NP) and 3-methyl-4-nitrophenol (3M4NP); when associated with I-380. 1 Publication | 1 | |
Mutagenesisi | 380 | L → I: Able to accept the two new substrates 4-nitrophenol (4NP) and 3-methyl-4-nitrophenol (3M4NP); when associated with L-22. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000443520 | 1 – 548 | 4-methyl-5-nitrocatechol 5-monooxygenaseAdd BLAST | 548 |
Interactioni
Subunit structurei
Monomer.
1 PublicationFamily & Domainsi
Sequence similaritiesi
Belongs to the PheA/TfdB FAD monooxygenase family.Curated
Family and domain databases
Gene3Di | 3.50.50.60, 1 hit |
InterProi | View protein in InterPro IPR002938, FAD-bd IPR036188, FAD/NAD-bd_sf |
Pfami | View protein in Pfam PF01494, FAD_binding_3, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit |
i Sequence
Sequence statusi: Complete.
Q2PWU9-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTRPLETPPD IEVPVLIVGG SMVGLSTALF LSHYGIQAMA VERHERTAIH
60 70 80 90 100
PRAGHFHLRT LELLRSVGLE EVVARTSAEA FFPNGGINAV QSLAGGETAS
110 120 130 140 150
FISNLNAGVE EFSPTRRLFI AQQALEPILR SRAEELGADL RYSTEVVSVV
160 170 180 190 200
DDGEGVTTVI RDKASGQERT VRSRYLVASD GWRSQRRAQL GIETRGQGLL
210 220 230 240 250
SRSATIYFRA DCRELLAGTH LGVIYVLNER LRGFFRFEKS LQSGFLGVAT
260 270 280 290 300
LGDPTRPGAL DVSAGFTTDT AVELVRAAIG VPDIDVEIQD VAHWEATAAL
310 320 330 340 350
ADRYRGGRIF LAGDAAHVVP PYGGFGGNTG VQDAHNLASK LALVLDGTAG
360 370 380 390 400
EALLDTYEAE RRPVGALTVD QAFSRYIRRL APEFLDEQTP ELVDDFSMEL
410 420 430 440 450
GYRYHSPAVL TEDDDKAVDQ AVVGHPREAL GRPGSRAPHV ALRVDDHDRS
460 470 480 490 500
VLDLLGRDFV VLAGPAGQVW AEAAERASKE LGLPLSAYVV GSDTPVADVE
510 520 530 540
GRFADAYGLS DAGVALVRPD GFIAWRSRDL AEDPEAALTD ALRAVLCR
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 312 | A → R in AAC44479 (PubMed:8830701).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U68411 Genomic DNA Translation: AAC44479.1 DQ298257 Genomic DNA Translation: ABC00744.1 |
Genome annotation databases
KEGGi | ag:AAC44479 ag:ABC00744 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U68411 Genomic DNA Translation: AAC44479.1 DQ298257 Genomic DNA Translation: ABC00744.1 |
3D structure databases
SMRi | Q2PWU9 |
ModBasei | Search... |
Genome annotation databases
KEGGi | ag:AAC44479 ag:ABC00744 |
Enzyme and pathway databases
BRENDAi | 1.14.13.210, 1033 |
Family and domain databases
Gene3Di | 3.50.50.60, 1 hit |
InterProi | View protein in InterPro IPR002938, FAD-bd IPR036188, FAD/NAD-bd_sf |
Pfami | View protein in Pfam PF01494, FAD_binding_3, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | DNTB_BURSP | |
Accessioni | Q2PWU9Primary (citable) accession number: Q2PWU9 Secondary accession number(s): P71029 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 28, 2018 |
Last sequence update: | January 24, 2006 | |
Last modified: | February 23, 2022 | |
This is version 51 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |