spacer

Overview for MACiE Entry M0117

Version history

General Information

EC Number: 1.6.2.4 (A member of the Oxidoreductases, Acting on NADH or NADPH, With a heme protein as acceptor)

Enzyme Name: NADPH-hemoprotein reductase

Biological Species: Rattus norvegicus (Rat)

Catalytic Chain UniprotKB Accession Codes:

  • P00388 - NADPH--cytochrome P450 reductase

Representative PDB Code: 1amo - THREE-DIMENSIONAL STRUCTURE OF NADPH-CYTOCHROME P450REDUCTASE: PROTOTYPE FOR FMN-AND FAD-CONTAINING ENZYMES (Resolution = 2.60 Å).

Catalytic CATH Codes:

  • 2.40.30.10 - Translation factors
  • 3.40.50.80 - Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module

"Other" CATH Codes:

Display structure information

Overall Reaction:

Image of NADPH

Image of oxidised hemoprotein

right arrow

Image of proton

Image of NADP

Image of reduced hemoprotein

NADPH
C00005
CHEBI:16474
oxidised hemoprotein
X00107
proton
C00080
CHEBI:24636
NADP
C00006
CHEBI:18009
reduced hemoprotein
X00108

It is unknown whether this reaction is reversible or not.

Overall Comment: This enzyme can catalyse a two-electron reduction of one hemoprotein or a one-electron reduction of two hemoproteins.


View similar reactions


Stepwise Description of the Reaction

Step 1NADP eliminates a hydride ion, which adds to FAD, with concomitant deprotonation of water at the FAD N1.
Step 2Water deprotonates the N1, initiating a single electron transfer from FAD to FMN, with concomitant deprotonation of water at the FMN N5.
Step 3Water deprotonates Cys630, which deprotonates Ser457 which deprotonates FAD facilitating the second single electron transfer from FAD to FMN.
Step 4FMN transfers a single electron to the hemoprotein.
Step 5Water deprotonates the FMN, facilitating the transfer of the second single electron to the hemoprotein.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Ser 457 A Side Chain
Cys 630 A Side Chain
Asp 675 A Side Chain

Organic Cofactors for M0117

Type Identity Chain
FAD FAD 750 A Overview
FMN FMN 751 A Overview

References

  1. P. A. Hubbard et al. (2001), J. Biol. Chem., 276, 29163-29170. NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer.
    Medline: 11371558

Homologue information for M0117 (1amo)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ
Link to EzCatDB

GOA logo
iron ion binding (molecular function)
FMN binding (molecular function)
oxidoreductase activity (molecular function)
oxidation-reduction process (biological process)
spacer
spacer