ID A0A1D6IAL1_MAIZE Unreviewed; 709 AA. AC A0A1D6IAL1; DT 30-NOV-2016, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 1. DT 15-FEB-2017, entry version 3. 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}; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; OC Zea. OX NCBI_TaxID=4577 {ECO:0000313|EnsemblPlants:Zm00001d021385_T002, ECO:0000313|Proteomes:UP000007305}; RN [1] {ECO:0000313|EnsemblPlants:Zm00001d021385_T002, ECO:0000313|Proteomes:UP000007305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001d021385_T002, RC ECO:0000313|Proteomes:UP000007305}; RX PubMed=19965430; DOI=10.1126/science.1178534; RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S., RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D., RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K., RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., RA Abbott R.M., Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., RA Gillam B., Chen W., Yan L., Higginbotham J., Cardenas M., RA Waligorski J., Applebaum E., Phelps L., Falcone J., Kanchi K., RA Thane T., Scimone A., Thane N., Henke J., Wang T., Ruppert J., RA Shah N., Rotter K., Hodges J., Ingenthron E., Cordes M., Kohlberg S., RA Sgro J., Delgado B., Mead K., Chinwalla A., Leonard S., Crouse K., RA Collura K., Kudrna D., Currie J., He R., Angelova A., Rajasekar S., RA Mueller T., Lomeli R., Scara G., Ko A., Delaney K., Wissotski M., RA Lopez G., Campos D., Braidotti M., Ashley E., Golser W., Kim H., RA Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A., Fan C., RA Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T., RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L., RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P., RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A., RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C., RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., RA Jeddeloh J.A., Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., RA Nagel D.H., McCann M.C., SanMiguel P., Myers A.M., Nettleton D., RA Nguyen J., Penning B.W., Ponnala L., Schneider K.L., Schwartz D.C., RA Sharma A., Soderlund C., Springer N.M., Sun Q., Wang H., Waterman M., RA Westerman R., Wolfgruber T.K., Yang L., Yu Y., Zhang L., Zhou S., RA Zhu Q., Bennetzen J.L., Dawe R.K., Jiang J., Jiang N., Presting G.G., RA Wessler S.R., Aluru S., Martienssen R.A., Clifton S.W., McCombie W.R., RA Wing R.A., Wilson R.K.; RT "The B73 maize genome: complexity, diversity, and dynamics."; RL Science 326:1112-1115(2009). RN [2] {ECO:0000313|EnsemblPlants:Zm00001d021385_T002} RP IDENTIFICATION. RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001d021385_T002}; RG EnsemblPlants; RL Submitted (OCT-2016) to UniProtKB. CC -!- CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP(+) + n CC reduced hemoprotein. {ECO:0000256|HAMAP-Rule:MF_03212, CC ECO:0000256|PIRNR:PIRNR000208}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP- CC 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03212}; CC Note=Binds 1 FMN per monomer. {ECO:0000256|HAMAP-Rule:MF_03212}; CC -!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase CC family. {ECO:0000256|HAMAP-Rule:MF_03212}. CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein CC pyridine nucleotide cytochrome reductase family. CC {ECO:0000256|HAMAP-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 CC of feature annotation. {ECO:0000256|HAMAP-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 RefSeq; XP_008653023.1; XM_008654801.1. DR EnsemblPlants; Zm00001d021385_T001; Zm00001d021385_T001; Zm00001d021385. DR EnsemblPlants; Zm00001d021385_T002; Zm00001d021385_T002; Zm00001d021385. DR GeneID; 103633123; -. DR Gramene; Zm00001d021385_T001; Zm00001d021385_T001; Zm00001d021385. DR Gramene; Zm00001d021385_T002; Zm00001d021385_T002; Zm00001d021385. DR Proteomes; UP000007305; Chromosome 7. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-HAMAP. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.990.10; -; 1. DR Gene3D; 3.40.50.360; -; 1. DR HAMAP; MF_03212; NCPR; 1. DR InterPro; IPR003097; FAD-binding_1. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001094; Flavdoxin-like. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR029039; Flavoprotein-like_dom. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_dom3. 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; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007305}; KW Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03212, KW ECO:0000256|PIRNR:PIRNR000208}; KW FAD {ECO:0000256|HAMAP-Rule:MF_03212}; KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_03212}; KW FMN {ECO:0000256|HAMAP-Rule:MF_03212}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_03212, KW ECO:0000256|PIRNR:PIRNR000208}; KW NADP {ECO:0000256|HAMAP-Rule:MF_03212, ECO:0000256|PIRNR:PIRNR000208}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03212, KW ECO:0000256|PIRNR:PIRNR000208}; KW Reference proteome {ECO:0000313|Proteomes:UP000007305}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_03212}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_03212}. FT TRANSMEM 42 62 Helical. {ECO:0000256|HAMAP-Rule: FT MF_03212}. FT DOMAIN 99 249 Flavodoxin-like. {ECO:0000259|PROSITE: FT PS50902}. FT DOMAIN 305 553 FAD-binding FR-type. FT {ECO:0000259|PROSITE:PS51384}. FT NP_BIND 105 110 FMN. {ECO:0000256|HAMAP-Rule:MF_03212}. FT NP_BIND 160 163 FMN. {ECO:0000256|HAMAP-Rule:MF_03212}. FT NP_BIND 198 207 FMN. {ECO:0000256|HAMAP-Rule:MF_03212}. FT NP_BIND 486 489 FAD. {ECO:0000256|HAMAP-Rule:MF_03212}. FT NP_BIND 504 506 FAD. {ECO:0000256|HAMAP-Rule:MF_03212}. FT NP_BIND 520 523 FAD. {ECO:0000256|HAMAP-Rule:MF_03212}. FT NP_BIND 628 629 NADP. {ECO:0000256|HAMAP-Rule:MF_03212}. FT NP_BIND 634 638 NADP. {ECO:0000256|HAMAP-Rule:MF_03212}. FT BINDING 233 233 FMN. {ECO:0000256|HAMAP-Rule:MF_03212}. FT BINDING 325 325 NADP. {ECO:0000256|HAMAP-Rule:MF_03212}. FT BINDING 567 567 NADP. {ECO:0000256|HAMAP-Rule:MF_03212}. FT BINDING 670 670 NADP. {ECO:0000256|HAMAP-Rule:MF_03212}. FT BINDING 709 709 FAD. {ECO:0000256|HAMAP-Rule:MF_03212}. SQ SEQUENCE 709 AA; 78321 MW; 4CBDD09FBB64655A CRC64; MDSAASAALK PSALDLLAAL LTGRDPEGGA HWASALAENR HLFLLLTTSL AVLVGCGVAL LVRRSSAPRA AAAAAQAPPR PLAVKPKDEP DPDDGRQRVI VFFGTQTGTA EGFAKALAEE AKARYDKAVF KVVDLEDYAA EDEEYEEKLK KESIALFFLA TYGDGEPTDN AARFYKWFSE GNERGEWLNN LRFGVFGLGN RQYEHFNKVG KVVDQLLAEQ GAKRIVPVGL GDDDQCIEDD FNAWKELLWP ELDKLLRQED DSSTAPTPYT AAIPEYRVVF VKPEDDMYIN KSFALSNGHT VYDIQHPCRA NVAVRRELHT PASDRSCIHL EFDIAGTGLK YETGDHVGVY AENCIETVEE AEKLLGYSPD TLFSIYADQE DGTPLCGGSL PPPFPSPCTV RTALTRYADL LNSPKKSALL ALAAHASDSK EAERLRHLAS PAGKKEYSQW IVTSQRSLLE VMSEFPSAKP PLGVFFAAIC PRLQPRYYSI SSSPRIAPTR IHVTCALVYG PTPTGRIHKG VCSTWMKHST PLEDSKDCSW APIFVRQSNF KLPADPTVPI IMIGPGTGLA PFRGFLQERL ALKQAEVELG HAVLFFGCRN RKMDFIYEDE LNNFVDAGAL SELIVAFSRE GPTKEYVQHK MAQKAAELWS IISQGGYIYV CGDAKGMARD VHRTLHTIVQ EQGSMDNNSK AESYVKSLQM EGRYLRDVW //