HAMAP rule MF_03212
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_03212 |
| Accession | MF_03212 |
| Dates | 20-NOV-2015 (Created)
03-SEP-2024 (Last updated, Version 9) |
| Name | NCPR |
| Scope(s) |
Eukaryota |
| Template(s) | P00388; P16435; P16603; [ Recover all ] |
| Triggered by |
HAMAP; MF_03212 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | NCPR |
| Protein name | RecName: Full=NADPH--cytochrome P450 reductase; Short=CPR; Short=P450R; EC=1.6.2.4; |
| case <OC:Vertebrata> | |
| Gene name | Name=POR; |
| else case <OC:Saccharomycetales> | |
| Gene name | Name=NCP1; |
| else case <OC:Pezizomycotina> | |
| Gene name | Name=cprA; |
| end case | |
Comments
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| case <OC:Fungi> | |
| FUNCTION | This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis. |
| SUBCELLULAR LOCATION | Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side. Mitochondrion outer membrane; Single-pass membrane protein; Cytoplasmic side. Cell membrane; Single- pass membrane protein; Cytoplasmic side. |
| else | |
| FUNCTION | This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. |
| SUBCELLULAR LOCATION | Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side. |
| end case | |
| CATALYTIC ACTIVITY | Reaction=2 oxidized [cytochrome P450] + NADPH = 2 reduced [cytochrome P450] + NADP(+) + H(+); Xref=Rhea:RHEA:24040, Rhea:RHEA- COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60344; EC=1.6.2.4; |
| COFACTOR | Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD per monomer.; |
| COFACTOR | Name=FMN; Xref=ChEBI:CHEBI:58210; Note=Binds 1 FMN per monomer.; |
| SIMILARITY | Belongs to the NADPH--cytochrome P450 reductase family. |
| SIMILARITY | In the N-terminal section; belongs to the flavodoxin family. |
| SIMILARITY | In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. |
Keywords
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Gene Ontology
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| case <OCellular component:Fungi> | |
| GO:0005739; Cellular component:mitochondrion | |
| GO:0005886; Cellular component:plasma membrane | |
| GO:0006696; Biological process:ergosterol biosynthetic process | |
| end case | |
| GO:0005737; Cellular component:cytoplasm | |
| GO:0005789; Cellular component:endoplasmic reticulum membrane | |
| GO:0050660; Molecular function:flavin adenine dinucleotide binding | |
| GO:0010181; Molecular function:FMN binding | |
| GO:0050661; Molecular function:NADP binding | |
| GO:0003958; Molecular function:NADPH-hemoprotein reductase activity | |
Cross-references
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| PROSITE | PS51384; FAD_FR; 1; |
| PROSITE | PS50902; FLAVODOXIN_LIKE; 1; |
| Pfam | PF00667; FAD_binding_1; 1; |
| Pfam | PF00258; Flavodoxin_1; 1; |
| Pfam | PF00175; NAD_binding_1; 1; |
| PRINTS | PR00369; FLAVODOXIN; 1; |
| PRINTS | PR00371; FPNCR; 1; |
| PIRSF | PIRSF000208; P450R; 1; |
| General | Transmembrane; -; 1; |
| ADD_TOPO_DOMAIN | Lumenal; -; 1; |
| ADD_TOPO_DOMAIN | Cytoplasmic; -; 1; |
Features
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| From: NCPR_RAT (P00388) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DOMAIN | 80 | 224 | /note="Flavodoxin-like" | |||||||||
| BINDING | 86 | 91 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
[ST]-Q-T-G-T-[AG] | ||||||||
| BINDING | 138 | 141 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
[AS]-T-Y-G | ||||||||
| BINDING | 173 | 182 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
L-G-[ND]-x-[TQ]-Y-E-x-[FY]-[NQ] | ||||||||
| BINDING | 454 | 457 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
R-[YF]-Y-S | ||||||||
| BINDING | 472 | 474 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
[CT]-x-[AVI] | ||||||||
| BINDING | 488 | 491 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
G-[VL]-x-[ST] | ||||||||
| BINDING | 596 | 597 | /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349" |
S-R | ||||||||
| BINDING | 602 | 606 | /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349" |
K-x-Y-V-[QT] | ||||||||
| BINDING | 208 | 208 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
D | ||||||||
| BINDING | 298 | 298 | /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349" |
R | ||||||||
| BINDING | 424 | 424 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
R | ||||||||
| BINDING | 478 | 478 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
Y | ||||||||
| BINDING | 535 | 535 | /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349" |
T | ||||||||
| BINDING | 639 | 639 | /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349" |
[DE] | ||||||||
| BINDING | 677 | 677 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
W | ||||||||
Additional information
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| Size range | 662-741 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |