CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.140 | 8 Propeller |
|
2.140.10 | Methanol Dehydrogenase; Chain A |
|
2.140.10.20 | C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase |
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 P72181
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 P72181
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)
| P72181 |
NIRS_PARPN
Paracoccus pantotrophus
Nitrite reductase
|
PDB Structure
| PDB | 1GQ1 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure and Kinetic Properties of Paracoccus Pantotrophus Cytochrome Cd1 Nitrite Reductase with the D1 Heme Active Site Ligand Tyrosine 25 Replaced by Serine
J.Biol.Chem.
|
