KEGG ORTHOLOGY: K10616

ORTHOLOGY: K10616

Entry

K10616                      KO

Symbol

cymAa

Name

p-cymene methyl-monooxygenase [EC:1.14.15.25]

Pathway

map00622

Xylene degradation

map01100

Metabolic pathways

map01120

Microbial metabolism in diverse environments

map01220

Degradation of aromatic compounds

Module

M00419

Cymene degradation, p-cymene => p-cumate

Brite

KEGG Orthology (KO) [BR:ko00001]
09100 Metabolism
  09111 Xenobiotics biodegradation and metabolism
   00622 Xylene degradation
    K10616  cymAa; p-cymene methyl-monooxygenase
Enzymes [BR:ko01000]
1. Oxidoreductases
  1.14  Acting on paired donors, with incorporation or reduction of molecular oxygen
   1.14.15  With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
    1.14.15.25  p-cymene methyl-monooxygenase
     K10616  cymAa; p-cymene methyl-monooxygenase

Other DBs

RN:

R05266

GO:

0018694

Genes

PPF:

Pput_2903

PPX:	T1E_4243(xylM)

PMON:

PMOT:

PASI:

SNAN:

STAW:

BXE:

BXB:

APET:

Reference

PMID:9150211

Authors

Eaton RW.

Title

p-Cymene catabolic pathway in Pseudomonas putida F1: cloning and characterization of DNA encoding conversion of p-cymene to p-cumate.

Journal

J Bacteriol 179:3171-80 (1997)
DOI:10.1128/JB.179.10.3171-3180.1997

Sequence

[ppf:Pput_2903]

Reference

PMID:11341314

Authors

Nishio T, Patel A, Wang Y, Lau PC

Title

Biotransformations catalyzed by cloned p-cymene monooxygenase from Pseudomonas putida F1.

Journal

Appl Microbiol Biotechnol 55:321-5 (2001)
DOI:10.1007/s002530000584

LinkDB

ORTHOLOGY: K18293

Entry

K18293                      KO

Symbol

cymAb

Name

p-cymene methyl-monooxygenase electron transfer component [EC:1.18.1.3]

Pathway

map00622

Xylene degradation

map01100

Metabolic pathways

map01120

Microbial metabolism in diverse environments

map01220

Degradation of aromatic compounds

Module

M00419

Cymene degradation, p-cymene => p-cumate

Brite

KEGG Orthology (KO) [BR:ko00001]
09100 Metabolism
  09111 Xenobiotics biodegradation and metabolism
   00622 Xylene degradation
    K18293  cymAb; p-cymene methyl-monooxygenase electron transfer component
Enzymes [BR:ko01000]
1. Oxidoreductases
  1.18  Acting on iron-sulfur proteins as donors
   1.18.1  With NAD+ or NADP+ as acceptor
    1.18.1.3  ferredoxin---NAD+ reductase
     K18293  cymAb; p-cymene methyl-monooxygenase electron transfer component

Other DBs

RN:

R05266

GO:

0018639

Genes

PPF:

Pput_2902

PPX:	T1E_4244(xylA)

PMON:

PMOT:

PASI:

BXE:

BXB:	DR64_1258(xylA)

IDC:	LRM40_19635

Reference

PMID:11341314

Authors

Nishio T, Patel A, Wang Y, Lau PC

Title

Biotransformations catalyzed by cloned p-cymene monooxygenase from Pseudomonas putida F1.

Journal

Appl Microbiol Biotechnol 55:321-5 (2001)
DOI:10.1007/s002530000584

Reference

PMID:9150211

Authors

Eaton RW.

Title

p-Cymene catabolic pathway in Pseudomonas putida F1: cloning and characterization of DNA encoding conversion of p-cymene to p-cumate.

Journal

J Bacteriol 179:3171-80 (1997)
DOI:10.1128/JB.179.10.3171-3180.1997

Sequence

[ppf:Pput_2902]

LinkDB

ENZYME: 1.14.15.25

Entry

EC 1.14.15.25               Enzyme

Name

p-cymene methyl-monooxygenase;
cymAa (gene name);
cymA (gene name);
p-cymene methyl hydroxylase

Class

Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor

Sysname

p-cymene,ferredoxin:oxygen oxidoreductase (methyl-hydroxylating)

Reaction(IUBMB)

p-cymene + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = 4-isopropylbenzyl alcohol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O [RN:R05266]

Reaction(KEGG)

R05266

Substrate

p-cymene [CPD:C06575];
O2 [CPD:C00007];
reduced ferredoxin [iron-sulfur] cluster [CPD:C00138];
H+ [CPD:C00080]

Product

4-isopropylbenzyl alcohol [CPD:C06576];
oxidized ferredoxin [iron-sulfur] cluster [CPD:C00139];
H2O [CPD:C00001]

Comment

The enzyme, characterized from several Pseudomonas strains, initiates p-cymene catabolism through hydroxylation of the methyl group. The enzyme has a distinct preference for substrates containing at least an alkyl or heteroatom substituent at the para-position of toluene. The electrons are provided by a reductase (EC 1.18.1.3, ferredoxin---NAD+ reductase) that transfers electrons from NADH via FAD and an [2Fe-2S] cluster. In Pseudomonas chlororaphis the presence of a third component of unknown function greatly increases the activity. cf. EC 1.14.15.26, toluene methyl-monooxygenase.

History

EC 1.14.15.25 created 2018

Pathway

ec00622

Xylene degradation

ec01100

Metabolic pathways

ec01120

Microbial metabolism in diverse environments

Orthology

K10616

p-cymene methyl-monooxygenase

Genes

PPF:

Pput_2903

PPX:	T1E_4243(xylM)

PMON:

X969_10820

PMOT:

X970_10475

PASI:

LG197_17340

SNAN:

I6N98_04605

STAW:

NCG89_08620

BXE:

Bxe_A3561

BXB:

DR64_1260

APET:

ToN1_06990

Reference

1 [PMID:9150211]

Authors

Eaton RW.

Title

p-Cymene catabolic pathway in Pseudomonas putida F1: cloning and characterization of DNA encoding conversion of p-cymene to p-cumate.

Journal

J Bacteriol 179:3171-80 (1997)
DOI:10.1128/JB.179.10.3171-3180.1997

Sequence

[ppf:Pput_2903 Pput_2902]

Reference

2 [PMID:9144566]

Authors

Dutta TK, Gunsalus IC

Title

Reductase gene sequences and protein structures: p-cymene methyl hydroxylase.

Journal

Biochem Biophys Res Commun 233:502-6 (1997)
DOI:10.1006/bbrc.1997.6493

Reference

3 [PMID:11341314]

Authors

Nishio T, Patel A, Wang Y, Lau PC

Title

Biotransformations catalyzed by cloned p-cymene monooxygenase from Pseudomonas putida F1.

Journal

Appl Microbiol Biotechnol 55:321-5 (2001)
DOI:10.1007/s002530000584

Reference

4 [PMID:21035544]

Authors

Dutta TK, Chakraborty J, Roy M, Ghosal D, Khara P, Gunsalus IC

Title

Cloning and characterization of a p-cymene monooxygenase from Pseudomonas chlororaphis subsp. aureofaciens.

Journal

Res Microbiol 161:876-82 (2010)
DOI:10.1016/j.resmic.2010.10.008

Other DBs

ExplorEnz - The Enzyme Database:

1.14.15.25

IUBMB Enzyme Nomenclature:

1.14.15.25

ExPASy - ENZYME nomenclature database:

1.14.15.25

BRENDA, the Enzyme Database:

1.14.15.25

LinkDB

REACTION: R05266

Entry

R05266                      Reaction

Name

p-cymene,ferredoxin:oxygen oxidoreductase (methyl-hydroxylating)

Definition

p-Cymene + Oxygen + 2 Reduced ferredoxin + 2 H+ <=> p-Cumic alcohol + 2 Oxidized ferredoxin + H2O

Equation

C06575 + C00007 + 2 C00138 + 2 C00080 <=> C06576 + 2 C00139 + C00001

Reaction class

RC00269

C06575_C06576

Enzyme

1.14.15.25

Pathway

rn00622

Xylene degradation

rn01100

Metabolic pathways

rn01120

Microbial metabolism in diverse environments

rn01220

Degradation of aromatic compounds

Module

M00419

Cymene degradation, p-cymene => p-cumate

Orthology

K10616

p-cymene methyl-monooxygenase [EC:1.14.15.25]

K18293

p-cymene methyl-monooxygenase electron transfer component [EC:1.18.1.3]

Other DBs

RHEA:

51607

LinkDB

DBGET integrated database retrieval system