ID A0A5B6UBJ4_9ROSI Unreviewed; 673 AA. AC A0A5B6UBJ4; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 03-AUG-2022, entry version 11. DE RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000256|HAMAP-Rule:MF_03212, ECO:0000256|PIRNR:PIRNR000208}; DE Short=CPR {ECO:0000256|HAMAP-Rule:MF_03212}; DE Short=P450R {ECO:0000256|HAMAP-Rule:MF_03212}; DE EC=1.6.2.4 {ECO:0000256|HAMAP-Rule:MF_03212, ECO:0000256|PIRNR:PIRNR000208}; GN ORFNames=EPI10_009896 {ECO:0000313|EMBL:KAA3453914.1}; OS Gossypium australe. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium. OX NCBI_TaxID=47621 {ECO:0000313|EMBL:KAA3453914.1, ECO:0000313|Proteomes:UP000325315}; RN [1] {ECO:0000313|Proteomes:UP000325315} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. PA1801 {ECO:0000313|Proteomes:UP000325315}; RX PubMed=31479566; DOI=10.1111/pbi.13249; RA Cai Y., Cai X., Wang Q., Wang P., Zhang Y., Cai C., Xu Y., Wang K., RA Zhou Z., Wang C., Geng S., Li B., Dong Q., Hou Y., Wang H., Ai P., Liu Z., RA Yi F., Sun M., An G., Cheng J., Zhang Y., Shi Q., Xie Y., Shi X., Chang Y., RA Huang F., Chen Y., Hong S., Mi L., Sun Q., Zhang L., Zhou B., Peng R., RA Zhang X., Liu F.; RT "Genome sequencing of the Australian wild diploid species Gossypium RT australe highlights disease resistance and delayed gland morphogenesis."; RL Plant Biotechnol. J. 0:0-0(2019). 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. {ECO:0000256|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:0000256|HAMAP- CC Rule:MF_03212, ECO:0000256|PIRNR:PIRNR000208}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03212}; CC Note=Binds 1 FAD per monomer. {ECO:0000256|HAMAP-Rule:MF_03212}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03212}; CC Note=Binds 1 FMN per monomer. {ECO:0000256|HAMAP-Rule:MF_03212}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|HAMAP-Rule:MF_03212}; Single-pass membrane protein CC {ECO:0000256|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000256|HAMAP- CC Rule:MF_03212}. CC -!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase family. CC {ECO:0000256|HAMAP-Rule:MF_03212}. CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein CC pyridine nucleotide cytochrome reductase family. {ECO:0000256|HAMAP- CC Rule:MF_03212, ECO:0000256|PIRNR:PIRNR000208}. CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin CC family. {ECO:0000256|HAMAP-Rule:MF_03212}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03212}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAA3453914.1}. 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; SMMG02000013; KAA3453914.1; -; Genomic_DNA. DR Proteomes; UP000325315; Chromosome 5. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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 Gene3D; 1.20.990.10; -; 1. DR Gene3D; 3.40.50.360; -; 1. DR Gene3D; 3.40.50.80; -; 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 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; SSF52218; SSF52218; 1. DR SUPFAM; SSF52343; SSF52343; 1. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 3: Inferred from homology; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP- KW Rule:MF_03212}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_03212}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP- KW Rule:MF_03212}; KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_03212}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_03212, ECO:0000256|PIRNR:PIRNR000208}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_03212}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_03212}; Reference proteome {ECO:0000313|Proteomes:UP000325315}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_03212}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_03212}. FT TRANSMEM 27..46 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212" FT DOMAIN 85..215 FT /note="Flavodoxin-like" FT /evidence="ECO:0000259|PROSITE:PS50902" FT DOMAIN 271..518 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000259|PROSITE:PS51384" FT BINDING 91..96 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212" FT BINDING 126..129 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212" FT BINDING 164..173 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212" FT BINDING 199 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212" FT BINDING 291 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212" FT BINDING 451..454 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212" FT BINDING 469..471 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212" FT BINDING 485..488 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212" FT BINDING 532 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212" FT BINDING 593..594 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212" FT BINDING 599..603 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212" FT BINDING 635 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212" FT BINDING 673 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212" SQ SEQUENCE 673 AA; 74890 MW; 27E46BBE894B0332 CRC64; MSSSSDLVGF VESVLGVSLE GSVTDSMIVI ATTSLAVILG LLVFFWKKSG SERSRDVKPL VAPKPVSLKD EEDDDAVIAA GKTKVTIFYG TQTGTAEGFA KDDYAMDDEQ YEEKLKKETL AFFMVATYGD GEPTDNAARF YKWFTEGNER LPWLQQLTYG VFGLGNRQYE HFNKIAKVLD EQLSEQGAKR LIEVGLGDDD QCIEDDFTAW RELLWPELDQ LLRDEDDENA TSTPYTAAIP EYRVVVHDPA VMHVEENYSN KANGNATYDL HHPCRVNVAV QRELHKPESD RSCIHLEFDI SGTGITYETG DHVGVYADNC VETVEEAARL LGQPLDLLFS IHTDNEDGTS AGSSLPPPFA SPCTLRMALA RYADLLNPPR KAALIALAAH ATEPSEAEKL KFLSSPQGKD EYSQWVVASQ RSLLEVMAEF PSAKPPLGVF FAAVAPRLQP RYYSISSSPR FVPARVHVTC ALVYGPTPTG RIHRGVCSTW MKNAVPLEKS NDCSWAPIFI RQSNFKLPAD PSVPIIMVGP GTGLAPFRGF LQERLVLKED GAELGSSLLF FGCRNRRMDF IYEDELNNFV EQGALSELVV AFSREGPQKE YVQHKMMDKA ADIWNLISKG GYLYVCGDAK GMARDVHRTL HTIIQEQENV DSSKAESMVK KLQMDGRYLR DVW //