| IED ID | IndEnz0005000327 |
| Enzyme Type ID | lipase000327 |
| Protein Name |
NADPH--cytochrome P450 reductase CPR P450R EC 1.6.2.4 |
| Gene Name | Por |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MGDSHEDTSATVPEAVAEEVSLFSTTDIVLFSLIVGVLTYWFIFKKKKEEIPEFSKIQTTAPPVKESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLADLSSLPEIDKSLVVFCMATYGEGDPTDNAQDFYDWLQETDVDLTGVKFAVFGLGNKTYEHFNAMGKYVDQRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEFFGVEATGEESSIRQYELVVHEDMDTAKVYTGEMGRLKSYENQKPPFDAKNPFLAAVTTNRKLNQGTERHLMHLELDISDSKIRYESGDHVAVYPANDSTLVNQIGEILGADLDVIMSLNNLDEESNKKHPFPCPTTYRTALTYYLDITNPPRTNVLYELAQYASEPSEQEHLHKMASSSGEGKELYLSWVVEARRHILAILQDYPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVAVEYEAKSGRVNKGVATSWLRTKEPAGENGRRALVPMFVRKSQFRLPFKPTTPVIMVGPGTGVAPFMGFIQERAWLREQGKEVGETLLYYGCRRSDEDYLYREELARFHKDGALTQLNVAFSREQAHKVYVQHLLKRDKEHLWKLIHEGGAHIYVCGDARNMAKDVQNTFYDIVAEFGPMEHTQAVDYVKKLMTKGRYSLDVWS |
| Enzyme Length | 678 |
| Uniprot Accession Number | P37040 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 208; /note=FMN; /evidence=ECO:0000255|HAMAP-Rule:MF_03212; BINDING 298; /note=NADP; /evidence=ECO:0000255|HAMAP-Rule:MF_03212; BINDING 424; /note=FAD; /evidence=ECO:0000255|HAMAP-Rule:MF_03212; BINDING 478; /note=FAD; /evidence=ECO:0000255|HAMAP-Rule:MF_03212; BINDING 535; /note=NADP; /evidence=ECO:0000255|HAMAP-Rule:MF_03212; BINDING 639; /note=NADP; /evidence=ECO:0000255|HAMAP-Rule:MF_03212; BINDING 677; /note=FAD; /evidence=ECO:0000255|HAMAP-Rule:MF_03212 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450]; 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; Evidence={ECO:0000255|HAMAP-Rule:MF_03212}; |
| DNA Binding | |
| EC Number | 1.6.2.4 |
| Enzyme Function | 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. {ECO:0000255|HAMAP-Rule:MF_03212}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 86..91; /note=FMN; /evidence=ECO:0000255|HAMAP-Rule:MF_03212; NP_BIND 138..141; /note=FMN; /evidence=ECO:0000255|HAMAP-Rule:MF_03212; NP_BIND 173..182; /note=FMN; /evidence=ECO:0000255|HAMAP-Rule:MF_03212; NP_BIND 454..457; /note=FAD; /evidence=ECO:0000255|HAMAP-Rule:MF_03212; NP_BIND 472..474; /note=FAD; /evidence=ECO:0000255|HAMAP-Rule:MF_03212; NP_BIND 488..491; /note=FAD; /evidence=ECO:0000255|HAMAP-Rule:MF_03212; NP_BIND 596..597; /note=NADP; /evidence=ECO:0000255|HAMAP-Rule:MF_03212; NP_BIND 602..606; /note=NADP; /evidence=ECO:0000255|HAMAP-Rule:MF_03212 |
| Features | Binding site (7); Chain (1); Domain (2); Initiator methionine (1); Modified residue (1); Nucleotide binding (8); Topological domain (2); Transmembrane (1) |
| Keywords | Acetylation;Endoplasmic reticulum;FAD;FMN;Flavoprotein;Membrane;NADP;Oxidoreductase;Reference proteome;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}. |
| Modified Residue | MOD_RES 2; /note=N-acetylglycine; /evidence=ECO:0000250|UniProtKB:P16435 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10633870; 11013070; 11130978; 11217851; 11742006; 11779826; 12466851; 12520002; 12566435; 12697746; 12917333; 12929087; 1420354; 14610273; 14681479; 15102471; 15328377; 15472464; 15717863; 15805261; 15899812; 16006652; 16141072; 16455785; 16488195; 16615898; 16887103; 17126317; 17374357; 17435107; 17699788; 17722906; 18778245; 18799693; 19056912; 19273610; 19793088; 20139973; 20375200; 20808945; 20840855; 21267068; 21362632; 21376747; 21677750; 21726529; 21751364; 21987461; 22111624; 22453923; 22626646; 22969154; 23169610; 23727388; 23732084; 23846873; 23922855; 24086598; 24248381; 24548803; 24989705; 25020125; 25068656; 2516426; 25377919; 26898952; 27863990; 28659616; 30685480; 33321093; 3917435; 6802825; 7476982; 7588219; 8589531; 9052933; |
| Motif | |
| Gene Encoded By | |
| Mass | 77,044 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:24040 |
| Cross Reference Brenda |