Organism | UniProt | Comment | Textmining |
---|---|---|---|
Neisseria gonorrhoeae | Q5F885 and Q5F884 and Q5F883 | Q5F885 i.e. oxidoreductase domain, Q5F884 i.e. LUD_dom domain-containing protein, Q5F883 i.e. (Fe-S)-binding protein | - |
Neisseria gonorrhoeae ATCC 700825 | Q5F885 and Q5F884 and Q5F883 | Q5F885 i.e. oxidoreductase domain, Q5F884 i.e. LUD_dom domain-containing protein, Q5F883 i.e. (Fe-S)-binding protein | - |
Synonyms | Comment | Organism |
---|---|---|
LutACB | - |
Neisseria gonorrhoeae |
NGO0904 | - |
Neisseria gonorrhoeae |
NGO0905 | - |
Neisseria gonorrhoeae |
NGO0906 | - |
Neisseria gonorrhoeae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
Fe-S center | - |
Neisseria gonorrhoeae |
Organism | Comment | Expression |
---|---|---|
Neisseria gonorrhoeae | expression of LutACB is induced by iron-limited conditions | up |
General Information | Comment | Organism |
---|---|---|
physiological function | the growth of the LutACB mutants is similar to that of the wild-type strain on L-lactate. The isoforms LutACB/LldD double mutant fails to grow on L-lactate, and complementation of this strain with LutACB restores growth to wild-type levels. LutACB contributes to L-lactate dehydrogenase activity under iron-replete conditions, and the LutACB deletion mutant is impaired in its ability to survive within human primary cervical epithelial cells | Neisseria gonorrhoeae |