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)

Q59647
NORB_PSEAE
Pseudomonas aeruginosa PAO1
Nitric oxide reductase subunit B

PDB Structure

PDB 5GUW
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Dynamics of nitric oxide controlled by protein complex in bacterial system
Terasaka, E., Yamada, K., Wang, P.H., Hosokawa, K., Yamagiwa, R., Matsumoto, K., Ishii, S., Mori, T., Yagi, K., Sawai, H., Arai, H., Sugimoto, H., Sugita, Y., Shiro, Y., Tosha, T.
Proc. Natl. Acad. Sci. U.S.A.
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