1.8.5.4: bacterial sulfide:quinone reductase
This is an abbreviated version!
For detailed information about bacterial sulfide:quinone reductase, go to the full flat file.
Word Map on EC 1.8.5.4
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1.8.5.4
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sulfur
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h2s
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thiosulfate
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persulfide
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polysulfide
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acidithiobacillus
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sulfurtransferase
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sulfide-oxidizing
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rhodanese
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sulfane
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ferrooxidans
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3-mercaptopyruvate
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anoxygenic
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sulfur-oxidizing
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chemolithotrophic
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sulfide-dependent
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echiuran
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unicinctus
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limnetica
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urechis
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monotopic
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oscillatoria
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tepidum
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chlorobaculum
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sulfide-rich
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medicine
- 1.8.5.4
- sulfur
- h2s
- thiosulfate
- persulfide
- polysulfide
- acidithiobacillus
- sulfurtransferase
-
sulfide-oxidizing
- rhodanese
-
sulfane
- ferrooxidans
- 3-mercaptopyruvate
-
anoxygenic
-
sulfur-oxidizing
-
chemolithotrophic
-
sulfide-dependent
-
echiuran
- unicinctus
- limnetica
-
urechis
-
monotopic
- oscillatoria
- tepidum
- chlorobaculum
-
sulfide-rich
- medicine
Reaction
n HS- + n quinone = + n quinol
Synonyms
CmSQR, CpSQR, CT1087, HMT2, III SQR, membrane-bound sulfide:quinone oxidoreductases, SQOR, SQR, Sqrdl, sqrF, Suden_1879, Suden_2082, Suden_619, sulfide quinone oxidoreductase, sulfide quinone reductase, sulfide-quinone oxidoreductase, sulfide-quinone reductase, sulfide: quinone oxidoreductase, sulfide:decylubiquinone oxidoreductase, sulfide:quinone oxidoreductase, sulfidequinone reductase-like protein, TrSqrF, type I SQR, type III sulfide:quinone oxidoreductase, type VI sulfide:quinone oxidoreductase
ECTree
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Cofactor
Cofactor on EC 1.8.5.4 - bacterial sulfide:quinone reductase
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FAD
the enzyme harbors one noncovalently bound FAD cofactor per monomer
FAD
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FAD is not covalently bound to the protein. Activity is not increased by the addition of FAD (0.020 mM) to the assay buffer
FAD
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is not covalently bound to the protein, the cofactor is in an apolar environment, one equivalent of FAD per sulfide:quinone xidoreductase polypeptide
FAD
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residues Gly12, Gly16, Ala77, and Pro44 are determined to be important for flavin binding, binding structure analysis, overview