KEGG   ENZYME: 1.14.12.25
Entry
EC 1.14.12.25               Enzyme                                 
Name
p-cumate 2,3-dioxygenase
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
4-isopropylbenzoate:oxygen 2,3-oxidoreductase
Reaction(IUBMB)
p-cumate + NADH + H+ + O2 = (2R,3S)-2,3-dihydroxy-2,3-dihydro-p-cumate + NAD+ [RN:R05247]
Reaction(KEGG)
R05247
Substrate
p-cumate [CPD:C06578];
NADH [CPD:C00004];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
(2R,3S)-2,3-dihydroxy-2,3-dihydro-p-cumate [CPD:C06579];
NAD+ [CPD:C00003]
Comment
The enzyme, characterized from several Pseudomonas strains, is involved in the degradation of p-cymene and p-cumate. It comprises four components: a ferredoxin, a ferredoxin reductase, and two subunits of a catalytic component. The enzyme can also act on indole, transforming it to the water-insoluble blue dye indigo.
History
EC 1.14.12.25 created 2016
Pathway
ec00622  Xylene degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K10619  p-cumate 2,3-dioxygenase subunit alpha
K16303  p-cumate 2,3-dioxygenase subunit beta
Genes
RBDALSL_1087 ALSL_1088
PAEPA2083 PA2085
PAEVN297_2148 N297_2150
PAEIN296_2148 N296_2150
PAUPA14_37550 PA14_37570
PAGPLES_32361 PLES_32381
PAFPAM18_2958 PAM18_2960
PNCNCGM2_3063 NCGM2_3065
PAEBNCGM1900_4396 NCGM1900_4398
PDKPADK2_15225 PADK2_15235
PSGG655_14675 G655_14685
PRPM062_10830 M062_10840
PAEPPA1S_15255 PA1S_15265
PAEMU769_14855 U769_14865
PAELT223_16535 T223_16545
PAESSCV20265_3298 SCV20265_3300
PAEUBN889_02279 BN889_02281
PAEGAI22_18505 AI22_18515
PAECM802_2145 M802_2147
PAEOM801_2147 M801_2149
PPFPput_2897 Pput_2898
PPXT1E_4248(cbdC) T1E_4249
PMONX969_10845 X969_10850
PMOTX970_10500 X970_10505
PSESPSCI_1386 PSCI_1388
SPOIIMCC21906_02711 IMCC21906_02712
ZALAZF00_03880 AZF00_03885 AZF00_17855 AZF00_17860
TLOJ9253_01265 J9253_01270
GBIPG2T_01290 PG2T_01295 PG2T_14345 PG2T_14350
BXEBxe_A3555 Bxe_A3556
BXBDR64_1254 DR64_1255
PFIBPI93_021400 PI93_021405
BRKCWS35_25065 CWS35_25070
BARHWN72_35375 WN72_35380
RHZRHPLAN_11150 RHPLAN_11160 RHPLAN_44350 RHPLAN_44360
MONG8E03_15190 G8E03_15195
NREBES08_18565 BES08_18570
SMAZLH19_27420 LH19_27425
SWISwit_1757 Swit_1758
SPHDHY78_16795 HY78_16800
RDICMV14_03910 CMV14_03915
SPANAWL63_19960 AWL63_19965
SECHB18_22315 B18_22325
SPHJBSL82_10970 BSL82_10975
BACIB1NLA3E_13990 B1NLA3E_13995
OCNCUC15_03700 CUC15_03705
VIGBKP57_09420 BKP57_09425
LAOAOX59_08275 AOX59_08280
RUEDT065_15140 DT065_15145
SALEEPH95_15060 EPH95_15065
PBJVN24_05635 VN24_05640
PNPIJ22_32370 IJ22_32380
EFFskT53_01990
SPAEE2C16_04425 E2C16_04430
MMANMMAN_42610 MMAN_42620
MSAKMSAS_43620 MSAS_43630
MPAGC0J29_30955 C0J29_30960
MCOOMCOO_07710 MCOO_07720
MNED174_16895 D174_16905 D174_16915 D174_16920
MYNMyAD_16560 MyAD_16570 MyAD_16580 MyAD_16585
MHASMHAS_04025(bnzB) MHAS_04026(cbdA_2)
MANYMANY_01930 MANY_01940
ROPROP_46330(cmtA2) ROP_46340(cmtA1)
RRZCS378_10910 CS378_10915
RHODAOT96_33475 AOT96_33510
RRT4535765_00187(cmtA1_1) 4535765_00188(cmtA2_1) 4535765_00374(cmtA2_2) 4535765_00375(cmtA1_2)
RKOJWS14_14210 JWS14_14215
GPDGII33_08510 GII33_08525
SALSSLNWT_6906 SLNWT_6907
SCZABE83_01985 ABE83_01990
STSIA4E84_36025 A4E84_36030
SALWCP975_27200 CP975_27205 CP975_33970 CP975_33975
SBATG4Z16_01225
SHUNDWB77_04977(antA) DWB77_04978(hcaF)
PSIMKR76_24910 KR76_24915
FSYFsymDg_2033 FsymDg_2034
AMQAMETH_1199(benA) AMETH_1200
AACDLWP59_08660 LWP59_08665 LWP59_25375 LWP59_25380
PDXPsed_4287 Psed_4289
PSEQAD006_28390 AD006_28395 AD006_28760 AD006_28765
PECQAD017_28780 AD017_28785 AD017_29150 AD017_29155
PBROHOP40_30820 HOP40_30825
SSYIEKG83_16160 EKG83_16165
PMADBAY61_11485 BAY61_11490 BAY61_20660 BAY61_20690
MICHFJK98_14410 FJK98_14415
MCABHXZ27_11850 HXZ27_11855 HXZ27_13045 HXZ27_13050
VMAVAB18032_10630 VAB18032_10635
PRYPrubr_43520(hcaF) Prubr_43530
ATBJ4859_03360
EUZDVS28_a1943 DVS28_a1944 DVS28_a1989
TTLTtJL18_2435 TtJL18_2436
 » show all
Reference
1  [PMID:845117]
  Authors
DeFrank JJ, Ribbons DW
  Title
p-cymene pathway in Pseudomonas putida: initial reactions.
  Journal
J Bacteriol 129:1356-64 (1977)
DOI:10.1128/JB.129.3.1356-1364.1977
Reference
2  [PMID:7204334]
  Authors
Wigmore GJ, Ribbons DW
  Title
p-Cymene pathway in Pseudomonas putida: selective enrichment of defective mutants by using halogenated substrate analogs.
  Journal
J Bacteriol 143:816-24 (1980)
DOI:10.1128/JB.143.2.816-824.1980
Reference
3  [PMID:7592495]
  Authors
Eaton RW, Chapman PJ
  Title
Formation of indigo and related compounds from indolecarboxylic acids by aromatic acid-degrading bacteria: chromogenic reactions for cloning genes encoding dioxygenases that act on aromatic acids.
  Journal
J Bacteriol 177:6983-8 (1995)
DOI:10.1128/JB.177.23.6983-6988.1995
Reference
4  [PMID:8631713]
  Authors
Eaton RW.
  Title
p-Cumate catabolic pathway in Pseudomonas putida Fl: cloning and characterization of DNA carrying the cmt operon.
  Journal
J Bacteriol 178:1351-62 (1996)
DOI:10.1128/JB.178.5.1351-1362.1996
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.12.25
IUBMB Enzyme Nomenclature: 1.14.12.25
ExPASy - ENZYME nomenclature database: 1.14.12.25
BRENDA, the Enzyme Database: 1.14.12.25
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