KEGG   ENZYME: 1.14.12.23
Entry
EC 1.14.12.23               Enzyme                                 
Name
nitroarene dioxygenase;
cnbA (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor
Sysname
nitrobenzene,NADH:oxygen oxidoreductase (1,2-hydroxylating, nitrite-releasing)
Reaction(IUBMB)
nitrobenzene + NADH + O2 = catechol + nitrite + NAD+ [RN:R07706]
Reaction(KEGG)
R07706
Substrate
nitrobenzene [CPD:C06813];
NADH [CPD:C00004];
O2 [CPD:C00007]
Product
catechol [CPD:C00090];
nitrite [CPD:C00088];
NAD+ [CPD:C00003]
Comment
This enzyme is a member of the naphthalene family of bacterial Rieske non-heme iron dioxygenases. It comprises a multicomponent system, containing a Rieske [2Fe-2S] ferredoxin, an NADH-dependent flavoprotein reductase (EC 1.18.1.3, ferredoxin---NAD+ reductase), and an alpha3beta3 oxygenase. The enzyme forms of a cis-dihydroxylated product that spontaneously rearranges to form a catechol with accompanying release of nitrite. It can typically act on many different nitroaromatic compounds, including chlorinated species. Enzymes found in different strains may have different substrate preferences. Requires Fe2+.
History
EC 1.14.12.23 created 2015
Pathway
ec00627  Aminobenzoate degradation
ec01120  Microbial metabolism in diverse environments
Orthology
K14579  naphthalene 1,2-dioxygenase subunit alpha
K14580  naphthalene 1,2-dioxygenase subunit beta
Genes
PPIND055(nahAc) ND056(nahAd)
PFKPFAS1_28610 PFAS1_28615
PSCA458_06720 A458_06725
PSTUUIB01_22625 UIB01_22630
PBMCL52_14610 CL52_14615
ALTambt_17890 ambt_17895
CYQQ91_2226
CZACYCME_2544
CYYCPC19_01670
FCEJN531_005655
GBIPG2T_11300
RMNTK49_07945 TK49_07955
BMKDM80_1443(ndoB) DM80_1444(ndoC)
BUQAC233_10850 AC233_11010
BFNOI25_3057(ndoB)
PARBCJU94_38655 CJU94_38660
PNAPnap_2484 Pnap_2485
AJSAjs_3092 Ajs_3093
ACIDCBP33_05315
ACIPCBP36_05765
ACINCBP34_05150
ACISCBP35_13180
DELDelCs14_1743
DIJHND92_13275 HND92_13280
MASWAM586_27555
RBUPG1C_04275 PG1C_06465
NARSaro_3901
NPPPP1Y_AT15992 PP1Y_AT31065
NPNJI59_12270 JI59_24755
SBARH5V43_22625
SPHYCHN51_07270
CNAAB433_10400 AB433_18005
ERYCP97_14005
 » show all
Reference
1  [PMID:9495758]
  Authors
Parales JV, Parales RE, Resnick SM, Gibson DT
  Title
Enzyme specificity of 2-nitrotoluene 2,3-dioxygenase from Pseudomonas sp. strain  JS42 is determined by the C-terminal region of the alpha subunit of the oxygenase component.
  Journal
J Bacteriol 180:1194-9 (1998)
DOI:10.1128/JB.180.5.1194-1199.1998
Reference
2  [PMID:11823201]
  Authors
Lessner DJ, Johnson GR, Parales RE, Spain JC, Gibson DT
  Title
Molecular characterization and substrate specificity of nitrobenzene dioxygenase from Comamonas sp. strain JS765.
  Journal
Appl Environ Microbiol 68:634-41 (2002)
DOI:10.1128/AEM.68.2.634-641.2002
  Sequence
Reference
3  [PMID:21602392]
  Authors
Liu H, Wang SJ, Zhang JJ, Dai H, Tang H, Zhou NY
  Title
Patchwork assembly of nag-like nitroarene dioxygenase genes and the 3-chlorocatechol degradation cluster for evolution of the 2-chloronitrobenzene catabolism pathway in Pseudomonas stutzeri ZWLR2-1.
  Journal
Appl Environ Microbiol 77:4547-52 (2011)
DOI:10.1128/AEM.02543-10
  Sequence
Reference
4  [PMID:24491551]
  Authors
Singh D, Kumari A, Ramaswamy S, Ramanathan G
  Title
Expression, purification and substrate specificities of 3-nitrotoluene dioxygenase from Diaphorobacter sp. strain DS2.
  Journal
Biochem Biophys Res Commun 445:36-42 (2014)
DOI:10.1016/j.bbrc.2014.01.113
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.12.23
IUBMB Enzyme Nomenclature: 1.14.12.23
ExPASy - ENZYME nomenclature database: 1.14.12.23
BRENDA, the Enzyme Database: 1.14.12.23
LinkDB

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