CATH Classification

Domain Context

CATH Clusters

Superfamily C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase
Functional Family Nitrite reductase NirS

Enzyme Information

1.7.99.1
Hydroxylamine reductase.
based on mapping to UniProt P24474
NH(3) + H(2)O + acceptor = hydroxylamine + reduced acceptor.
-!- Reduced pyocyanine, methylene blue and flavins act as donors for the reduction of hydroxylamine. -!- May be identical to EC 1.7.2.1.
1.7.2.1
Nitrite reductase (NO-forming).
based on mapping to UniProt P24474
Nitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H(+).
-!- The reaction is catalyzed by two types of enzymes, found in the perimplasm of denitrifying bacteria. -!- One type comprises proteins containing multiple copper centers, the other a heme protein, cytochrome cd1. -!- Acceptors include c-type cytochromes such as cytochrome c-550 or cytochrome c-551 from Paracoccus denitrificans or Pseudomonas aeruginosa, and small blue copper proteins such as azurin and pseudoazurin. -!- Cytochrome cd1 also has oxidase and hydroxylamine reductase activities. -!- May also catalyze the reaction of EC 1.7.99.1 since this is a well- known activity of cytochrome cd1. -!- Formerly EC 1.6.6.5, EC 1.7.99.3 and EC 1.9.3.2.

UniProtKB Entries (1)

P24474
NIRS_PSEAE
Pseudomonas aeruginosa PAO1
Nitrite reductase

PDB Structure

PDB 1NIR
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
N-terminal arm exchange is observed in the 2.15 A crystal structure of oxidized nitrite reductase from Pseudomonas aeruginosa.
Nurizzo, D., Silvestrini, M.C., Mathieu, M., Cutruzzola, F., Bourgeois, D., Fulop, V., Hajdu, J., Brunori, M., Tegoni, M., Cambillau, C.
Structure