Protein Variants | Comment | Organism |
---|---|---|
C112I | NqrD-C112I. The substitutions of the conserved cysteine residue in NqrD blocks the Na+-dependent and HQNO-sensitive quinone reductase activity of the enzyme, being without effect on the interaction of the enzyme with reduced nicotinamide hypoxanthine dinucleotide and menadione. The substitution of the conserved cysteine residues results in inability of covalently bound flavins to stabilize flavosemiquinone states, i.e. leads to incorrect folding of the NQR complex | Vibrio cholerae serotype O1 |
C120G | NqrE-C120G. The substitution of the conserved cysteine residue in NqrE subunit of the enzyme blocks the Na+-dependent and HQNO-sensitive quinone reductase activity of the enzyme, being without effect on the interaction of the enzyme with reduced nicotinamide hypoxanthine dinucleotide and menadione. The substitution of the conserved cysteine residues results in inability of covalently bound flavins to stabilize flavosemiquinone states, i.e. leads to incorrect folding of the NQR complex | Vibrio cholerae serotype O1 |
C26G | NqrE-C26G. The substitution of the conserved cysteine residue in NqrE subunits of the enzyme blocks the Na+-dependent and HQNO-sensitive quinone reductase activity of the enzyme, being without effect on the interaction of the enzyme with reduced nicotinamide hypoxanthine dinucleotide and menadione. The substitution of the conserved cysteine residues results in inability of covalently bound flavins to stabilize flavosemiquinone states, i.e. leads to incorrect folding of the NQR complex | Vibrio cholerae serotype O1 |
C29A | NqrD-C29A. The substitutions of the conserved cysteine residue in NqrD subunit of the enzyme blocks the Na+-dependent and HQNO-sensitive quinone reductase activity of the enzyme, being without effect on the interaction of the enzyme with reduced nicotinamide hypoxanthine dinucleotide and menadione. The substitution of the conserved cysteine residues results in inability of covalently bound flavins to stabilize flavosemiquinone states, i.e. leads to incorrect folding of the NQR complex | Vibrio cholerae serotype O1 |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe | the enzyme contains 650-780 ng Fe per mg protein, which corresponds to 2.5-3.0 atoms of Fe per enzyme complex. The enzyme bears only the 2Fe-2S cluster as the sole metal-containing prosthetic group | Vibrio cholerae serotype O1 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Vibrio cholerae serotype O1 | Q9KPS1 and Q9KPS2 and P0C6E0 and Q9X4Q6 and Q9X4Q7 and Q9X4Q8 | Q9KPS1: subunit NqrA, Q9KPS2: subunit NqrB, P0C6E0: subunit NqrC, Q9X4Q6: subunit NqrD, Q9X4Q7: subunit NqrE, Q9X4Q8: subunit NqrF. The enzyme consists of six subunits encoded by the NQR operon. | - |
Vibrio cholerae serotype O1 ATCC 39315 | Q9KPS1 and Q9KPS2 and P0C6E0 and Q9X4Q6 and Q9X4Q7 and Q9X4Q8 | Q9KPS1: subunit NqrA, Q9KPS2: subunit NqrB, P0C6E0: subunit NqrC, Q9X4Q6: subunit NqrD, Q9X4Q7: subunit NqrE, Q9X4Q8: subunit NqrF. The enzyme consists of six subunits encoded by the NQR operon. | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
reduced nicotinamide hypoxanthine dinucleotide + menadione | - |
Vibrio cholerae serotype O1 | oxidized nicotinamide hypoxanthine dinucleotide + menadiol | - |
? | |
reduced nicotinamide hypoxanthine dinucleotide + menadione | - |
Vibrio cholerae serotype O1 ATCC 39315 | oxidized nicotinamide hypoxanthine dinucleotide + menadiol | - |
? |
Synonyms | Comment | Organism |
---|---|---|
dNADH:K3 oxidoreductase | - |
Vibrio cholerae serotype O1 |
Na(+)-translocating NADH-quinone reductase subunit D | - |
Vibrio cholerae serotype O1 |
Na(+)-translocating NADH-quinone reductase subunit E | - |
Vibrio cholerae serotype O1 |
Na+-NQR | - |
Vibrio cholerae serotype O1 |
Na+-translocating NADH:quinone oxidoreductase | - |
Vibrio cholerae serotype O1 |
NADH:quinone oxidoreductase | - |
Vibrio cholerae serotype O1 |