1.7.7.1: ferredoxin-nitrite reductase
This is an abbreviated version!
For detailed information about ferredoxin-nitrite reductase, go to the full flat file.
Word Map on EC 1.7.7.1
Reaction
Synonyms
aNiR, assimilatory NiR, assimilatory nitrite reductase, CYME_CMG021C, CYME_CMJ117C, ferredoxin-nitrite reductase, ferredoxin:nitrite oxidoreductase, ferredoxin:nitrite reductase, Nii1, nii3, nii4, NiR, NiR1, NirA, nitrite reductase, NrfA, NrfH, reductase, ferredoxin-nitrite, SiRA, SirB
ECTree
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Engineering on EC 1.7.7.1 - ferredoxin-nitrite reductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G212S/L213T/Y214L/S217C/C220I/S221N
mutations mimic partially isoform SiRA
S217C
mutation mimics the corresponding residue in isoform SiRA, recovers sulfite reduction activity
G212S/L213T/Y214L/S217C/C220I/S221N
-
mutations mimic partially isoform SiRA
-
S217C
-
mutation mimics the corresponding residue in isoform SiRA, recovers sulfite reduction activity
-
M175E
the conformation of the Gln47 and Lys91 side-chains changes significantly. Compared with the conformation in wild-type, the Gln47 side-chain rotates about 120 degrees and the amino group in the Lys91 side-chain moves toward the side-chain of residue 175
M175G
the conformation of the Gln47 and Lys91 side-chains changes significantly. Compared with the conformation in wild-type, the Gln47 side-chain rotates about 120 degrees and the amino group in the Lys91 side-chain moves toward the side-chain of residue 175
M175K
the conformation of the Gln47 and Lys91 side-chains changes significantly. Compared with the conformation in wild-type, the Gln47 side-chain rotates about 120 degrees and the amino group in the Lys91 side-chain moves toward the side-chain of residue 175
Q448K
mutation had only a negligible effect on the overall fold of the protein. In addition, the mutation did not affect the hydrogen bond interaction at the distal position of the siroheme
