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Literature summary extracted from

  • Suzuki, M.; Hayakawa, T.; Shaw, J.; Rekik, M.; Harayama, S.
    Primary structure of xylene monooxygenase Similarities to and differences from the alkane hydroxylation system (1991), J. Bacteriol., 173, 1690-1695 .
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.15.26 membrane
-
 Pseudomonas putida 16020
-
1.18.1.3 membrane
-
 Pseudomonas putida 16020
-

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.26 Pseudomonas putida P21395 P21395 i.e. subunit XylM, acts with electron transfer component XylA, cf. EC 1.18.1.3
-
1.18.1.3 Pseudomonas putida P21394 acts with xylene monooxygenase component XylM, cf. EC 1.14.15.26
-
1.18.1.3 Pseudomonas putida P21394 enzyme acts as reductase component of toluene monooxygenase, EC 1.14.15.26
-

Synonyms

EC Number Synonyms Comment Organism
1.14.15.26 xylM
-
 Pseudomonas putida
1.18.1.3 xylM
-
 Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.3 Ferredoxin enzyme reduces ferredoxin with the concomitant oxidation of NADH Pseudomonas putida
1.18.1.3 NADH enzyme reduces ferredoxin with the concomitant oxidation of NADH Pseudomonas putida