IED Industry Enzyme Database

Detail Information for IndEnz0005000824
IED ID IndEnz0005000824
Enzyme Type ID lipase000824
Protein Name NADPH--cytochrome P450 reductase
CPR
P450R
EC 1.6.2.4
Gene Name Por
Organism Rattus norvegicus (Rat)
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 Rattus Rattus norvegicus (Rat)
Enzyme Sequence MGDSHEDTSATMPEAVAEEVSLFSTTDMVLFSLIVGVLTYWFIFRKKKEEIPEFSKIQTTAPPVKESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLADLSSLPEIDKSLVVFCMATYGEGDPTDNAQDFYDWLQETDVDLTGVKFAVFGLGNKTYEHFNAMGKYVDQRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEFFGVEATGEESSIRQYELVVHEDMDVAKVYTGEMGRLKSYENQKPPFDAKNPFLAAVTANRKLNQGTERHLMHLELDISDSKIRYESGDHVAVYPANDSALVNQIGEILGADLDVIMSLNNLDEESNKKHPFPCPTTYRTALTYYLDITNPPRTNVLYELAQYASEPSEQEHLHKMASSSGEGKELYLSWVVEARRHILAILQDYPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVAVEYEAKSGRVNKGVATSWLRAKEPAGENGGRALVPMFVRKSQFRLPFKSTTPVIMVGPGTGIAPFMGFIQERAWLREQGKEVGETLLYYGCRRSDEDYLYREELARFHKDGALTQLNVAFSREQAHKVYVQHLLKRDREHLWKLIHEGGAHIYVCGDARNMAKDVQNTFYDIVAEFGPMEHTQAVDYVKKLMTKGRYSLDVWS
Enzyme Length 678
Uniprot Accession Number P00388
Absorption
Active Site
Activity Regulation
Binding Site BINDING 208; /note="FMN"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990"; BINDING 298; /note="NADP"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990"; BINDING 424; /note="FAD"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|Ref.8"; BINDING 478; /note="FAD"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8"; BINDING 535; /note="NADP"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8"; BINDING 639; /note="NADP"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990"; BINDING 677; /note="FAD"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8"
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, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8"; NP_BIND 138..141; /note="FMN"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8"; NP_BIND 173..182; /note="FMN"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8"; NP_BIND 454..457; /note="FAD"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8"; NP_BIND 472..474; /note="FAD"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8"; NP_BIND 488..491; /note="FAD"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8"; NP_BIND 596..597; /note="NADP"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8"; NP_BIND 602..606; /note="NADP"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8"
Features Beta strand (31); Binding site (7); Chain (1); Domain (2); Helix (27); Initiator methionine (1); Modified residue (1); Nucleotide binding (8); Sequence conflict (1); Topological domain (2); Transmembrane (1); Turn (8)
Keywords 3D-structure;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 X-ray crystallography (26)
Cross Reference PDB 1AMO; 1J9Z; 1JA0; 1JA1; 3ES9; 3OJW; 3OJX; 3WKT; 4Y7C; 4Y9R; 4Y9U; 4YAF; 4YAL; 4YAO; 4YAU; 4YAW; 5URD; 5URE; 5URG; 5URH; 5URI; 6J79; 6J7A; 6J7I; 6NJR; 7L18;
Mapped Pubmed ID 11350928; 15031143; 15516695; 15680923; 15823091; 15942020; 16055078; 16226717; 16249336; 16527817; 16616465; 17392395; 17400174; 17446262; 17693640; 18194664; 18801337; 18803703; 19023562; 19077323; 19152507; 19264869; 19265259; 19908820; 20624491; 21462923; 24550278; 24853741; 2495435; 25450017; 25512382; 27189945; 27856527; 28684414; 29308883; 30883732; 31009206; 33556357; 34196520; 9774150;
Motif
Gene Encoded By
Mass 76,963
Kinetics
Metal Binding
Rhea ID RHEA:24040
Cross Reference Brenda 1.6.2.4;