ID NCPR_CANMA Reviewed; 680 AA. AC P50126; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-SEP-2023, entry version 120. 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}; OS Candida maltosa (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=5479; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=EH15; RX PubMed=8701606; RX DOI=10.1002/(sici)1097-0061(19960330)12:4<333::aid-yea915>3.0.co;2-c; RA Kaergel E., Honeck H., Vogel F., Boehmer A., Schunk W.-H.; RT "Candida maltosa NADPH-cytochrome P450 reductase: cloning of a full-length RT cDNA, heterologous expression in Saccharomyces cerevisiae and function of RT the N-terminal region for membrane anchoring and proliferation of the RT endoplasmic reticulum."; RL Yeast 12:333-348(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 28140 / CBS 5611 / IAM 12247 / JCM 1504 / NBRC 1977; RX PubMed=7545482; DOI=10.1271/bbb.59.1328; RA Ohkuma M., Masuda Y., Park S.M., Ohtomo R., Ohta A., Takagi M.; RT "Evidence that the expression of the gene for NADPH-cytochrome P-450 RT reductase is n-alkane-inducible in Candida maltosa."; RL Biosci. Biotechnol. Biochem. 59:1328-1330(1995). 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; X76226; CAA53812.1; -; mRNA. DR EMBL; D25327; BAA04997.1; -; Genomic_DNA. DR PIR; S63698; S63698. DR PIR; S63895; S63895. DR AlphaFoldDB; P50126; -. DR SMR; P50126; -. DR OMA; QKRYQRD; -. DR BioCyc; MetaCyc:MONOMER-18776; -. 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: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: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 2: Evidence at transcript level; 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_0000167605" 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" FT CONFLICT 30 FT /note="Q -> E (in Ref. 2; BAA04997)" FT /evidence="ECO:0000305" FT CONFLICT 170..171 FT /note="LL -> VF (in Ref. 2; BAA04997)" FT /evidence="ECO:0000305" FT CONFLICT 565 FT /note="F -> P (in Ref. 2; BAA04997)" FT /evidence="ECO:0000305" FT CONFLICT 579 FT /note="Q -> K (in Ref. 2; BAA04997)" FT /evidence="ECO:0000305" FT CONFLICT 619 FT /note="V -> L (in Ref. 2; BAA04997)" FT /evidence="ECO:0000305" FT CONFLICT 664 FT /note="E -> D (in Ref. 2; BAA04997)" FT /evidence="ECO:0000305" SQ SEQUENCE 680 AA; 77131 MW; E396F81E169705C9 CRC64; MALDKLDLYV IIVLAVAVAA YFAKNQFLDQ PQDTGFLSND TAGGNSRDIL ETLKKNNKNT LLLFGSQTGT AEDYANKLSR EIHSRFGLKT MVADFADYDW DNFGDIPNDI LVFFIVATYG EGEPTDNADE FHTWLTDEAD TLSTLRYTVF GLGNSTYEFY NAIGRKFDRL LEEKGGERFA DYGEGDDGTG TLDEDFLTWK DNVFDTLKND LNFEERELKY EPNVKLTERD DLTVDDSEVS LGEPNKKYIQ SEEIDLTKGP FDHTHPYLAK ISKTRELFAS KERNCVHVEF DVSESNLKYT TGDHLAVWPS NSDENIAKFI KCFGLDDKIN TVFELKALDS TYQIPFPNPI TYGAVVRHHL EISGPVSRQF FLAIAGFAPD EETKKTFTRI GNDKQEFANK ITRKKLNVAD ALLFASNGRP WSDVPFEFII ENVPHLQPRY YSISSSSLSE KQTINITAVV EVEEEADGRA VTGVVTNLLK NIEIEQNKTG EKPVVHYDLS GPRNKFNKFK LPVHVRRSNF KLPKNTTTPV ILIGPGTGVA PLRGFVRERV QQVKNGVNVG KTVLFYGCRN EHDDFLYKQE WSEYASVLGE NFEMFTAFSR QDPSKKVYVQ DKIAENSKVV NDLLNEGAII YVCGDASRMA RDVQSTIAKI VAKHREIQED KAVELVKSWK VQNRYQEDVW //