AC   MF_03212;
DC   Protein; auto
TR   HAMAP; MF_03212; -; 1; level=0
XX
Names: NCPR
XX
ID   NCPR
DE   RecName: Full=NADPH--cytochrome P450 reductase;
DE            Short=CPR;
DE            Short=P450R;
DE            EC=1.6.2.4;
case <OC:Vertebrata>
GN   Name=POR;
else case <OC:Saccharomycetales>
GN   Name=NCP1;
else case <OC:Pezizomycotina>
GN   Name=cprA;
end case
XX
case <OC:Fungi>
CC   -!- FUNCTION: This enzyme is required for electron transfer from NADP to
CC       cytochrome P450 in microsomes. It can also provide electron transfer to
CC       heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein; Cytoplasmic side. Mitochondrion outer membrane;
CC       Single-pass membrane protein; Cytoplasmic side. Cell membrane; Single-
CC       pass membrane protein; Cytoplasmic side.
else
CC   -!- FUNCTION: This enzyme is required for electron transfer from NADP to
CC       cytochrome P450 in microsomes. It can also provide electron transfer to
CC       heme oxygenase and cytochrome B5.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein; Cytoplasmic side.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC         reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC         COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:60344; EC=1.6.2.4;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC       Note=Binds 1 FAD per monomer.;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC       Note=Binds 1 FMN per monomer.;
CC   -!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase family.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC       family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family.
XX
DR   PROSITE; PS51384; FAD_FR; 1; trigger=yes
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1; trigger=no
DR   Pfam; PF00667; FAD_binding_1; 1; trigger=no
DR   Pfam; PF00258; Flavodoxin_1; 1; trigger=no
DR   Pfam; PF00175; NAD_binding_1; 1; trigger=no
DR   PRINTS; PR00369; FLAVODOXIN; 1; trigger=no
DR   PRINTS; PR00371; FPNCR; 1; trigger=no
DR   PIRSF; PIRSF000208; P450R; 1; trigger=no
DR   General; Transmembrane; -; 1; trigger=yes
DR   ADD_TOPO_DOMAIN; Lumenal; -; 1; trigger=yes
DR   ADD_TOPO_DOMAIN; Cytoplasmic; -; 1; trigger=yes
XX
case <OC:Fungi>
KW   Cell membrane
KW   Mitochondrion
KW   Mitochondrion outer membrane
KW   Lipid biosynthesis
KW   Lipid metabolism
KW   Steroid biosynthesis
KW   Steroid metabolism
KW   Sterol biosynthesis
KW   Sterol metabolism
end case
KW   Endoplasmic reticulum
KW   FAD
KW   Flavoprotein
KW   FMN
KW   Membrane
KW   NADP
KW   Oxidoreductase
XX
case <OC:Fungi>
GO   GO:0005739; C:mitochondrion
GO   GO:0005886; C:plasma membrane
GO   GO:0006696; P:ergosterol biosynthetic process
end case
GO   GO:0005737; C:cytoplasm
GO   GO:0005789; C:endoplasmic reticulum membrane
GO   GO:0050660; F:flavin adenine dinucleotide binding
GO   GO:0010181; F:FMN binding
GO   GO:0050661; F:NADP binding
GO   GO:0003958; F:NADPH-hemoprotein reductase activity
XX
FT   From: NCPR_RAT (P00388)
FT   DOMAIN          80..224
FT                   /note="Flavodoxin-like"
FT   BINDING         86..91
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: [ST]-Q-T-G-T-[AG]
FT   BINDING         138..141
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: [AS]-T-Y-G
FT   BINDING         173..182
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: L-G-[ND]-x-[TQ]-Y-E-x-[FY]-[NQ]
FT   BINDING         454..457
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Condition: R-[YF]-Y-S
FT   BINDING         472..474
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Condition: [CT]-x-[AVI]
FT   BINDING         488..491
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Condition: G-[VL]-x-[ST]
FT   BINDING         596..597
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: S-R
FT   BINDING         602..606
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: K-x-Y-V-[QT]
FT   BINDING         208
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: D
FT   BINDING         298
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Optional; Condition: R
FT   BINDING         424
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Optional; Condition: R
FT   BINDING         478
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Optional; Condition: Y
FT   BINDING         535
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: T
FT   BINDING         639
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Optional; Condition: [DE]
FT   BINDING         677
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Condition: W
XX
Size: 662-741;
Related: None;
Template: P00388; P16435; P16603;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: in ARATH
Plasmid: None
Comments: None
XX
# Revision 1.7 2022/11/19
//