ID NCPR_CANTR Reviewed; 680 AA. AC P37201; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 22-FEB-2023, entry version 122. DE RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000255|HAMAP-Rule:MF_03212}; DE Short=CPR {ECO:0000255|HAMAP-Rule:MF_03212}; DE Short=P450R {ECO:0000255|HAMAP-Rule:MF_03212}; DE EC=1.6.2.4 {ECO:0000255|HAMAP-Rule:MF_03212}; GN Name=NCP1 {ECO:0000255|HAMAP-Rule:MF_03212}; Synonyms=CPR; OS Candida tropicalis (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=5482; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 750 / CBS 94 / DSM 11953 / JCM 1541 / NBRC 1400; RX PubMed=2118906; DOI=10.1016/s0021-9258(17)46240-5; RA Sutter T.R., Sanglard D., Loper J.C.; RT "Isolation and characterization of the alkane-inducible NADPH-cytochrome P- RT 450 oxidoreductase gene from Candida tropicalis. Identification of RT invariant residues within similar amino acid sequences of divergent RT flavoproteins."; RL J. Biol. Chem. 265:16428-16436(1990). RN [2] RP ERRATUM OF PUBMED:2118906. RA Sutter T.R., Sanglard D., Loper J.C.; RL J. Biol. Chem. 265:22056-22056(1990). 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 {ECO:0000255|HAMAP-Rule:MF_03212}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03212}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03212}; CC Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03212}; CC Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein CC {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_03212}. Mitochondrion outer membrane {ECO:0000255|HAMAP- CC Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}. CC Cell membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane CC protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side CC {ECO:0000255|HAMAP-Rule:MF_03212}. CC -!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase family. CC {ECO:0000255|HAMAP-Rule:MF_03212}. CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin CC family. {ECO:0000255|HAMAP-Rule:MF_03212}. CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein CC pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP- CC Rule:MF_03212}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M35199; AAA34333.1; -; Genomic_DNA. DR PIR; A37890; A37890. DR AlphaFoldDB; P37201; -. DR SMR; P37201; -. DR VEuPathDB; FungiDB:CTMYA2_036990; -. DR VEuPathDB; FungiDB:CTRG_00485; -. DR SABIO-RK; P37201; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron transfer activity; IEA:EnsemblFungi. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003959; F:NADPH dehydrogenase activity; IEA:EnsemblFungi. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006696; P:ergosterol biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd06204; CYPOR; 1. DR Gene3D; 3.40.50.360; -; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR HAMAP; MF_03212; NCPR; 1. DR InterPro; IPR003097; CysJ-like_FAD-binding. DR InterPro; IPR017927; FAD-bd_FR_type. DR InterPro; IPR001094; Flavdoxin-like. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR029039; Flavoprotein-like_sf. DR InterPro; IPR039261; FNR_nucleotide-bd. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR023208; P450R. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR PANTHER; PTHR19384:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 1. DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1. DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PIRSF; PIRSF000208; P450R; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF52218; Flavoproteins; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 3: Inferred from homology; KW Cell membrane; Endoplasmic reticulum; FAD; Flavoprotein; FMN; KW Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion; KW Mitochondrion outer membrane; NADP; Oxidoreductase; Steroid biosynthesis; KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane; KW Transmembrane helix. FT CHAIN 1..680 FT /note="NADPH--cytochrome P450 reductase" FT /id="PRO_0000167606" FT TOPO_DOM 1..5 FT /note="Lumenal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT TRANSMEM 6..23 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT TOPO_DOM 24..680 FT /note="Cytoplasmic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT DOMAIN 60..204 FT /note="Flavodoxin-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT DOMAIN 264..509 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 66..71 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 117..120 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 152..161 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 187 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 283 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 439..442 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 457..459 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 473..476 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 537 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 599..600 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 606..610 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 642 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" FT BINDING 680 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212" SQ SEQUENCE 680 AA; 76689 MW; AB31ABFF8ADA41DA CRC64; MALDKLDLYV IITLVVAIAA YFAKNQFLDQ QQDTGFLNTD SGDGNSRDIL QALKKNNKNT LLLFGSQTGT AEDYANKLSR ELHSRFGLKT MVADFADYDF ENFGDITEDI LVFFIVATYG EGEPTDNADE FHTWLTEEAD TLSTLKYTVF GLGNSTYEFF NAIGRKFDRL LGEKGGDRFA EYGEGDDGTG TLDEDFLAWK DNVFDSLKND LNFEEKELKY EPNVKLTERD DLSGNDPDVS LGEPNVKYIK SEGVDLTKGP FDHTHPFLAR IVKTKELFTS EDRHCVHVEF DISESNLKYT TGDHLAIWPS NSDENIKQFA KCFGLEDKLD TVIELKALDS TYSIPFPNPI TYGAVIRHHL EISGPVSRQF FLSIAGFAPD EETKKSFTRI GGDKQEFASK VTRRKFNIAD ALLFASNNRP WSDVPFEFLI ENVQHLTPRY YSISSSSLSE KQTINVTAVV EAEEEADGRP VTGVVTNLLK NIEIEQNKTG ETPMVHYDLN GPRGKFSKFR LPVHVRRSNF KLPKNSTTPV ILIGPGTGVA PLRGFVRERV QQVKNGVNVG KTVLFYGCRN SEQDFLYKQE WSEYASVLGE NFEMFNAFSR QDPTKKVYVQ DKILENSALV DELLSSGAII YVCGDASRMA RDVQAAIAKI VAKSRDIHED KAAELVKSWK VQNRYQEDVW //