KEGG   ENZYME: 1.14.13.244Help
Entry
EC 1.14.13.244              Enzyme                                 

Name
phenol 2-monooxygenase (NADH);
dmpLMNOP (gene names)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
phenol,NADH:oxygen oxidoreductase (2-hydroxylating)
Reaction(IUBMB)
phenol + NADH + H+ + O2 = catechol + NAD+ + H2O [RN:R10043]
Reaction(KEGG)
R10043;
(other) R10042
Show
Substrate
phenol [CPD:C00146];
NADH [CPD:C00004];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
catechol [CPD:C00090];
NAD+ [CPD:C00003];
H2O [CPD:C00001]
Comment
The enzyme, characterized from the bacteria Pseudomonas sp. CF600 and Acinetobacter radioresistens, consists of a multisubunit oxygenease component that contains the active site and a dinuclear iron center, a reductase component that contains FAD and one iron-sulfur cluster, and a regulatory component. The reductase component is responsible for transferring electrons from NADH to the dinuclear iron center.
History
EC 1.14.13.244 created 2019
Pathway
ec00361  Chlorocyclohexane and chlorobenzene degradation
ec00362  Benzoate degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K16242  phenol/toluene 2-monooxygenase (NADH) P3/A3
K16243  phenol/toluene 2-monooxygenase (NADH) P1/A1
K16244  phenol/toluene 2-monooxygenase (NADH) P2/A2
K16245  phenol/toluene 2-monooxygenase (NADH) P4/A4
K16246  phenol/toluene 2-monooxygenase (NADH) P5/A5
Genes
PSD: DSC_04415 DSC_04420 DSC_04425 DSC_04430 DSC_04435
RBD: ALSL_0896 ALSL_0897 ALSL_0898 ALSL_0899 ALSL_0900
PRE: PCA10_06970(dmpL) PCA10_06980(dmpM) PCA10_06990(dmpN) PCA10_07000(dmpO) PCA10_07010(dmpP)
PCQ: PcP3B5_25310(mphL) PcP3B5_25320(dmpM) PcP3B5_25330(tmoA) PcP3B5_25340 PcP3B5_25350(dmpP)
PPG: PputGB1_3306 PputGB1_3307 PputGB1_3308 PputGB1_3309 PputGB1_3310
PPJ: RK21_04242 RK21_04243 RK21_04244 RK21_04245 RK21_04246 RK21_04247
PVR: PverR02_14660 PverR02_14665 PverR02_14670 PverR02_14675 PverR02_14680
PKC: PKB_1742(dmpL) PKB_1743 PKB_1744(dmpN) PKB_1745 PKB_1746(dmpP)
PALK: PSAKL28_05880 PSAKL28_05890 PSAKL28_05900 PSAKL28_05910 PSAKL28_05920
AVN: Avin_08810(dmpP) Avin_08820(dmpO) Avin_08830(dmpN) Avin_08840(dmpM) Avin_08850(dpmL) Avin_30710(lapP) Avin_30720(lapO) Avin_30730(lapN) Avin_30740(lapM) Avin_30750(lapL)
AVL: AvCA_08810(dmpP) AvCA_08820(dmpO) AvCA_08830(dmpN) AvCA_08840(dmpM) AvCA_08850(dpmL) AvCA_30710(lapP) AvCA_30720(lapO) AvCA_30730(lapN) AvCA_30740(lapM) AvCA_30750(lapL)
AVD: AvCA6_08810(dmpP) AvCA6_08820(dmpO) AvCA6_08830(dmpN) AvCA6_08840(dmpM) AvCA6_08850(dpmL) AvCA6_30710(lapP) AvCA6_30720(lapO) AvCA6_30730(lapN) AvCA6_30740(lapM) AvCA6_30750(lapL)
ACC: BDGL_000470(mphP) BDGL_000471(mphO) BDGL_000472(mphN) BDGL_000473(mphM) BDGL_000474(mphL)
REH: H16_B0540(poxB) H16_B0541(poxC) H16_B0542(poxD) H16_B0543(poxE) H16_B0544(poxF)
CNC: CNE_2c04860(poxB) CNE_2c04870(poxC) CNE_2c04880(poxD) CNE_2c04890(poxE) CNE_2c04900(poxF)
RME: Rmet_1326(tomA5) Rmet_1327(tomA4) Rmet_1328(tomA3) Rmet_1329(tomA2) Rmet_1330(tomA1) Rmet_1782(phyE) Rmet_1783(phyD) Rmet_1784(phyC) Rmet_1785(phyB) Rmet_1786(phyA)
BCEN: DM39_4839(dmpP) DM39_4840(phO) DM39_4841(phN) DM39_4842(dmpM) DM39_4843(mphL)
BCED: DM42_4998(dmpP) DM42_4999(phO) DM42_5000(phN) DM42_5001(dmpM) DM42_5002(phL)
MPT: Mpe_A2280(dmpP) Mpe_A2281(dmpO) Mpe_A2282(dmpN) Mpe_A2283(dmpM) Mpe_A2284(dmpL) Mpe_A3306(dmpN) Mpe_A3307(dmpM) Mpe_A3308(dmpL)
AZO: azo1846(lapL) azo1847(lapM) azo1848(lapN) azo1849(lapO) azo1850(lapP) azo2439(poxF) azo2440(poxE) azo2441(poxD) azo2442(poxC) azo2443(poxB)
SJP: SJA_C1-11990(tomA1) SJA_C1-12000(tomA2) SJA_C1-12010(tomA3) SJA_C1-12020(tomA4) SJA_C1-12030(tomA5)
ASOC: CB4_02441(mphL) CB4_02442(dmpM) CB4_02443(tmoA) CB4_02444
 » show all
Taxonomy
Reference
1  [PMID:2254258]
  Authors
Nordlund I, Powlowski J, Shingler V
  Title
Complete nucleotide sequence and polypeptide analysis of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600.
  Journal
J Bacteriol 172:6826-33 (1990)
DOI:10.1128/jb.172.12.6826-6833.1990
Reference
2  [PMID:2254259]
  Authors
Powlowski J, Shingler V
  Title
In vitro analysis of polypeptide requirements of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600.
  Journal
J Bacteriol 172:6834-40 (1990)
Reference
3  [PMID:8995386]
  Authors
Powlowski J, Sealy J, Shingler V, Cadieux E
  Title
On the role of DmpK, an auxiliary protein associated with multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600.
  Journal
J Biol Chem 272:945-51 (1997)
Reference
4  [PMID:9012665]
  Authors
Qian H, Edlund U, Powlowski J, Shingler V, Sethson I
  Title
Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.
  Journal
Biochemistry 36:495-504 (1997)
DOI:10.1021/bi9619233
Reference
5  [PMID:12186554]
  Authors
Cadieux E, Vrajmasu V, Achim C, Powlowski J, Munck E
  Title
Biochemical, Mossbauer, and EPR studies of the diiron cluster of phenol hydroxylase from Pseudomonas sp. strain CF 600.
  Journal
Biochemistry 41:10680-91 (2002)
Other DBs
ExplorEnz - The Enzyme Database: 1.14.13.244
IUBMB Enzyme Nomenclature: 1.14.13.244
ExPASy - ENZYME nomenclature database: 1.14.13.244
BRENDA, the Enzyme Database: 1.14.13.244

DBGET integrated database retrieval system