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Protein

4-methyl-5-nitrocatechol 5-monooxygenase

Gene

dntB

Organism
Burkholderia sp.
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 Publications

Catalytic activityi

4-methyl-5-nitrocatechol + NAD(P)H + O2 = 2-hydroxy-5-methylquinone + nitrite + NAD(P)+ + H2O.2 Publications

Cofactori

FAD1 PublicationNote: Binds 1 FAD per subunit.1 Publication

Enzyme 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
  1. KM=15.5 µM for NADPH1 Publication
  2. KM=50 µM for oxygene1 Publication
  3. KM=350 µM for 4-nitrophenol (4NP)1 Publication
  4. KM=1220 µM for NADH1 Publication
  1. Vmax=14 nmol/min/mg enzyme with 4-nitrophenol (4NP) as substrate1 Publication

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
Biological processAromatic hydrocarbons catabolism
LigandFAD, Flavoprotein, NAD, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13337

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
OrganismiBurkholderia sp.
Taxonomic identifieri36773 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi22M → L: Able to accept the two new substrates 4-nitrophenol (4NP) and 3-methyl-4-nitrophenol (3M4NP); when associated with I-380. 1 Publication1
Mutagenesisi380L → I: Able to accept the two new substrates 4-nitrophenol (4NP) and 3-methyl-4-nitrophenol (3M4NP); when associated with L-22. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004435201 – 5484-methyl-5-nitrocatechol 5-monooxygenaseAdd BLAST548

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ2PWU9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PheA/TfdB FAD monooxygenase family.Curated

Phylogenomic databases

KOiK21683

Family and domain databases

Gene3Di3.50.50.60, 3 hits
InterProiView protein in InterPro
IPR002938 FAD-bd
IPR036188 FAD/NAD-bd_sf
PfamiView protein in Pfam
PF01494 FAD_binding_3, 1 hit
SUPFAMiSSF51905 SSF51905, 2 hits

Sequencei

Sequence statusi: Complete.

Q2PWU9-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:548
Mass (Da):59,083
Last modified:January 24, 2006 - v1
Checksum:i846E65119A8F6593
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti312A → R in AAC44479 (PubMed:8830701).Curated1

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

KEGGiag:AAC44479
ag:ABC00744

Similar proteinsi

Entry informationi

Entry nameiDNTB_BURSP
AccessioniPrimary (citable) accession number: Q2PWU9
Secondary accession number(s): P71029
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 28, 2018
Last sequence update: January 24, 2006
Last modified: April 25, 2018
This is version 41 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health