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

NH3
+ 2 H2O + 6 oxidized ferredoxin =
nitrite
+ 6 reduced ferredoxin + 7 H+

Synonyms

aNiR, assimilatory NiR, assimilatory nitrite reductase, CYME_CMG021C, CYME_CMJ117C, ferredoxin:nitrite oxidoreductase, ferredoxin:nitrite reductase, Nii1, nii3, nii4, NiR, nitrite reductase, NrfA, NrfH, reductase, ferredoxin-nitrite, SiRA, SirB

ECTree

     1 Oxidoreductases
         1.7 Acting on other nitrogenous compounds as donors
             1.7.7 With an iron-sulfur protein as acceptor
                1.7.7.1 ferredoxin-nitrite reductase

Engineering

Engineering on EC 1.7.7.1 - ferredoxin-nitrite reductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
-
K449Q
mutation does not affect enzymatic 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
C514S
-
almost complete loss of activity
C518S
-
almost complete loss of activity
G513A
-
increased Km for nitrite compared to the wild type enzyme
G513E
-
loss of most of the activity
G513V
-
loss of most of the activity
G519A
-
68% activity of wild type enzyme
G519E
-
8% activity of wild type enzyme
G519V
-
9% activity of wild type enzyme
P515A
-
marginal loss of activity
P515S
-
marginal loss of activity
P515T
-
marginal loss of activity
additional information
-
various mutants that differ in enzymatic activity