Coronafacic acid polyketide synthase I; This gene is the first of two multimodular polyketide synthetases involved in the biosynthesis of coronafacic acid. This synthetase is proposed to receive CPC (2-carboxy-2-cyclopentenone) from an acyl carrier protein (cfa1), it then adds a buyrate group and then completely reduces the ketone of the (former) carboxylate group. The resulting product is then passed to the second polyketide synthetase (cfa7); similar to GP:13346874; identified by sequence similarity; putative; see PMID:20190049 for expression data; This gene is the first of two multi [...]

This gene is aparrently the terminal component of a non-ribosomal peptide synthetase (due to the presence of the terminal thioesterase domain) and is most likely associated with the previous gene which appears to be a initiating component. This gene contains three complete amino acid activation, thiolation and condensation domain modules and appears to be specific for glycine, an unidentified amino acid and serine according to the prediction algorithm at http://raynam.chm.jhu.edu/; nrps/index2.html. Taken together these two genes appear to direct the biosynthesis of a previously undesc [...]

Coronamic acid synthetase CmaA; Non-ribosomal peptide synthetase with adenylation and thiolation domains; reacts with the AMP derivative of L-allo-isoleucine to produce an aminoacyl thiolester intermediate during coronamic acid biosynthesis; see PMID: 14679222; see PMID:20190049 for expression data; non-ribosomal peptide synthetase with adenylation and thiolation domains, reacts with the AMP derivative of L-allo-isoleucine to produce an aminoacyl thiolester intermediate during coronamic acid biosynthesis, see PMID: 14679222.

NADH dehydrogenase I, B subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.

NADH dehydrogenase I, F subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.

This gene is aparrently the initiating component of a non-ribosomal peptide synthetase (due to the presence of an initial non-amino acid adenylation/ligase domain) and is most likely associated with the following gene which appears to be a terminating component. This gene contains a thiolation domain as well as one complete amino acid activation, thiolation and condensation domain modules which appears to be specific for serine according to the prediction algorithm at http://raynam.chm.jhu.edu/; nrps/index2.html. Taken together these two genes appear to direct the biosynthesis of a pre [...]

NADH dehydrogenase I, E subunit; See PMID:20190049 for expression data.

Ferredoxin; Similar to GP:1518927, GB:M23219, SP:P17583, PID:145644, GB:U00096, PID:1657537, and PID:1786536; identified by sequence similarity; putative.

NADH dehydrogenase I, I subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.