Literature summary extracted from

Nam, J.W.; Noguchi, H.; Fujimoto, Z.; Mizuno, H.; Ashikawa, Y.; Abo, M.; Fushinobu, S.; Kobashi, N.; Wakagi, T.; Iwata, K.; Yoshida, T.; Habe, H.; Yamane, H.; Omori, T.; Nojiri, H.
Crystal structure of the ferredoxin component of carbazole 1,9a-dioxygenase of Pseudomonas resinovorans strain CA10, a novel Rieske non-heme iron oxygenase system (2005), Proteins, 58, 779-789.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.14.12.22	crystal structure of ferredoxin component CarAc at 1.9 A resolution by molecular replacement using the structure of BphF, the biphenyl 2,3-dioxygenase ferredoxin from Burkholderia cepacia strain LB400 as a search model. CarAc is composed of three beta-sheets, and the structure can be divided into a cluster-binding domain and a basal domain. The Rieske [2Fe-2S] cluster is located at the tip of the cluster-binding domain, where it is exposed to solvent. While the overall folding of CarAc and BphF is strongly conserved, the properties of their surfaces are very different from each other. The structure of the cluster-binding domain of CarAc is more compact and protruding than that of BphF	Pseudomonas resinovorans

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.12.22	Pseudomonas resinovorans	-	-	-
1.14.12.22	Pseudomonas resinovorans CA10	-	-	-

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.14.12.22	Ferredoxin	ferredoxin component CarAc acts as a mediator in the electron transfer from ferredoxin reductase CarAd to terminal oxygenase CarAa. It contains a Rieske [2Fe-2S] cluster, which is located at the tip of the cluster-binding domain, where it is exposed to solvent	Pseudomonas resinovorans

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Release 2023.1 (January 2023)