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NADPH--cytochrome P450 reductase 1 (CPR 1) (P450R 1) (EC 1.6.2.4)

 NCPR1_ARATH             Reviewed;         692 AA.
Q9SB48; Q39035;
18-APR-2012, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
23-MAY-2018, entry version 135.
RecName: Full=NADPH--cytochrome P450 reductase 1 {ECO:0000255|HAMAP-Rule:MF_03212};
Short=CPR 1 {ECO:0000255|HAMAP-Rule:MF_03212};
Short=P450R 1 {ECO:0000255|HAMAP-Rule:MF_03212};
EC=1.6.2.4 {ECO:0000255|HAMAP-Rule:MF_03212};
Name=ATR1; Synonyms=AR1; OrderedLocusNames=At4g24520;
ORFNames=F22K18.280;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=cv. Landsberg erecta;
PubMed=9235908; DOI=10.1074/jbc.272.31.19176;
Urban P., Mignotte C., Kazmaier M., Delorme F., Pompon D.;
"Cloning, yeast expression, and characterization of the coupling of
two distantly related Arabidopsis thaliana NADPH-cytochrome P450
reductases with P450 CYP73A5.";
J. Biol. Chem. 272:19176-19186(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
PubMed=9990323; DOI=10.1046/j.1432-1327.1998.2581040.x;
Louerat-Oriou B., Perret A., Pompon D.;
"Differential redox and electron-transfer properties of purified
yeast, plant and human NADPH-cytochrome P-450 reductases highly
modulate cytochrome P-450 activities.";
Eur. J. Biochem. 258:1040-1049(1998).
[6]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
PubMed=9449848; DOI=10.1104/pp.116.1.357;
Mizutani M., Ohta D.;
"Two isoforms of NADPH:cytochrome P450 reductase in Arabidopsis
thaliana. Gene structure, heterologous expression in insect cells, and
differential regulation.";
Plant Physiol. 116:357-367(1998).
[7]
FUNCTION.
PubMed=10208644;
Louerat-Oriou B., Flinois J.P., Beaune P.H., Pompon D.;
"High yield purification and characterization of engineered human P450
1A2 and generation of immuno-inhibitor antibodies.";
Pharmacogenetics 9:61-70(1999).
[8]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9880378; DOI=10.1104/pp.119.1.353;
Fukuchi-Mizutani M., Mizutani M., Tanaka Y., Kusumi T., Ohta D.;
"Microsomal electron transfer in higher plants: cloning and
heterologous expression of NADH-cytochrome b5 reductase from
Arabidopsis.";
Plant Physiol. 119:353-361(1999).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- 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. Reduces a variety of
substrates in vitro, such as cytochrome c, feericyanide and
dichloroindophenol. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:10208644, ECO:0000269|PubMed:9235908,
ECO:0000269|PubMed:9449848, ECO:0000269|PubMed:9880378,
ECO:0000269|PubMed:9990323}.
-!- CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP(+) + n
reduced hemoprotein. {ECO:0000255|HAMAP-Rule:MF_03212}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:9990323};
Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212};
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:9990323};
Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.2 uM for NADPH (at pH 7.0 and 25 degrees Celsius)
{ECO:0000269|PubMed:9449848, ECO:0000269|PubMed:9880378,
ECO:0000269|PubMed:9990323};
KM=21.9 uM for NADPH (at pH 7.7 and 28 degrees Celsius)
{ECO:0000269|PubMed:9449848, ECO:0000269|PubMed:9880378,
ECO:0000269|PubMed:9990323};
KM=2.0 uM for NADPH (at pH 7.25 and 25 degrees Celsius)
{ECO:0000269|PubMed:9449848, ECO:0000269|PubMed:9880378,
ECO:0000269|PubMed:9990323};
KM=17 uM for cytochrome c (at pH 7.0 and 25 degrees Celsius)
{ECO:0000269|PubMed:9449848, ECO:0000269|PubMed:9880378,
ECO:0000269|PubMed:9990323};
KM=24.3 uM for cytochrome c (at pH 7.7 and 28 degrees Celsius)
{ECO:0000269|PubMed:9449848, ECO:0000269|PubMed:9880378,
ECO:0000269|PubMed:9990323};
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q9SB48-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
siliques. {ECO:0000269|PubMed:9449848}.
-!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase
family. {ECO:0000255|HAMAP-Rule:MF_03212}.
-!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
family. {ECO:0000255|HAMAP-Rule:MF_03212}.
-!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
pyridine nucleotide cytochrome reductase family.
{ECO:0000255|HAMAP-Rule:MF_03212}.
-----------------------------------------------------------------------
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EMBL; X66016; CAA46814.1; -; mRNA.
EMBL; AL035356; CAA23011.1; -; Genomic_DNA.
EMBL; AL161561; CAB79362.1; -; Genomic_DNA.
EMBL; CP002687; AEE84919.1; -; Genomic_DNA.
EMBL; AY054688; AAK96879.1; -; mRNA.
EMBL; BT008426; AAP37785.1; -; mRNA.
PIR; T05582; T05582.
RefSeq; NP_194183.1; NM_118585.4. [Q9SB48-1]
UniGene; At.144; -.
UniGene; At.70123; -.
ProteinModelPortal; Q9SB48; -.
SMR; Q9SB48; -.
BioGrid; 13843; 2.
STRING; 3702.AT4G24520.1; -.
iPTMnet; Q9SB48; -.
PaxDb; Q9SB48; -.
PRIDE; Q9SB48; -.
EnsemblPlants; AT4G24520.1; AT4G24520.1; AT4G24520. [Q9SB48-1]
GeneID; 828554; -.
Gramene; AT4G24520.1; AT4G24520.1; AT4G24520. [Q9SB48-1]
KEGG; ath:AT4G24520; -.
Araport; AT4G24520; -.
TAIR; locus:2121894; AT4G24520.
eggNOG; KOG1158; Eukaryota.
eggNOG; COG0369; LUCA.
HOGENOM; HOG000282027; -.
InParanoid; Q9SB48; -.
KO; K00327; -.
OMA; HLEFELG; -.
OrthoDB; EOG093604WR; -.
PhylomeDB; Q9SB48; -.
BioCyc; ARA:AT4G24520-MONOMER; -.
BioCyc; MetaCyc:MONOMER-2101; -.
Reactome; R-ATH-211897; Cytochrome P450 - arranged by substrate type.
PRO; PR:Q9SB48; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9SB48; baseline and differential.
Genevisible; Q9SB48; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0010181; F:FMN binding; IEA:InterPro.
GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:TAIR.
GO; GO:0009698; P:phenylpropanoid metabolic process; IDA:TAIR.
GO; GO:0009737; P:response to abscisic acid; IDA:TAIR.
GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
Gene3D; 1.20.990.10; -; 4.
Gene3D; 3.40.50.360; -; 1.
HAMAP; MF_03212; NCPR; 1.
InterPro; IPR003097; FAD-binding_1.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR001094; Flavdoxin-like.
InterPro; IPR008254; Flavodoxin/NO_synth.
InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
InterPro; IPR029039; Flavoprotein-like_sf.
InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR023208; P450R.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00667; FAD_binding_1; 1.
Pfam; PF00258; Flavodoxin_1; 1.
Pfam; PF00175; NAD_binding_1; 1.
PIRSF; PIRSF000208; P450R; 1.
PRINTS; PR00369; FLAVODOXIN.
PRINTS; PR00371; FPNCR.
SUPFAM; SSF52218; SSF52218; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome;
Endoplasmic reticulum; FAD; Flavoprotein; FMN; Membrane; NADP;
Oxidoreductase; Phenylpropanoid metabolism; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 692 NADPH--cytochrome P450 reductase 1.
/FTId=PRO_0000416839.
TOPO_DOM 2 26 Lumenal. {ECO:0000255|HAMAP-
Rule:MF_03212}.
TRANSMEM 27 47 Helical. {ECO:0000255|HAMAP-
Rule:MF_03212}.
TOPO_DOM 48 692 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_03212}.
DOMAIN 85 235 Flavodoxin-like. {ECO:0000255|HAMAP-
Rule:MF_03212}.
DOMAIN 290 537 FAD-binding FR-type. {ECO:0000255|HAMAP-
Rule:MF_03212}.
NP_BIND 91 96 FMN. {ECO:0000255|HAMAP-Rule:MF_03212}.
NP_BIND 146 149 FMN. {ECO:0000255|HAMAP-Rule:MF_03212}.
NP_BIND 184 193 FMN. {ECO:0000255|HAMAP-Rule:MF_03212}.
NP_BIND 470 473 FAD. {ECO:0000255|HAMAP-Rule:MF_03212}.
NP_BIND 488 490 FAD. {ECO:0000255|HAMAP-Rule:MF_03212}.
NP_BIND 504 507 FAD. {ECO:0000255|HAMAP-Rule:MF_03212}.
NP_BIND 612 613 NADP. {ECO:0000255|HAMAP-Rule:MF_03212}.
NP_BIND 618 622 NADP. {ECO:0000255|HAMAP-Rule:MF_03212}.
BINDING 219 219 FMN. {ECO:0000255|HAMAP-Rule:MF_03212}.
BINDING 310 310 NADP. {ECO:0000255|HAMAP-Rule:MF_03212}.
BINDING 551 551 NADP. {ECO:0000255|HAMAP-Rule:MF_03212}.
BINDING 654 654 NADP. {ECO:0000255|HAMAP-Rule:MF_03212}.
BINDING 692 692 FAD. {ECO:0000255|HAMAP-Rule:MF_03212}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000244|PubMed:19245862}.
CONFLICT 161 161 Y -> S (in Ref. 1; CAA46814).
{ECO:0000305}.
CONFLICT 477 480 SPRL -> CQDW (in Ref. 1; CAA46814).
{ECO:0000305}.
SEQUENCE 692 AA; 76766 MW; 7DD77E418CCF2FA6 CRC64;
MTSALYASDL FKQLKSIMGT DSLSDDVVLV IATTSLALVA GFVVLLWKKT TADRSGELKP
LMIPKSLMAK DEDDDLDLGS GKTRVSIFFG TQTGTAEGFA KALSEEIKAR YEKAAVKVID
LDDYAADDDQ YEEKLKKETL AFFCVATYGD GEPTDNAARF YKWFTEENER DIKLQQLAYG
VFALGNRQYE HFNKIGIVLD EELCKKGAKR LIEVGLGDDD QSIEDDFNAW KESLWSELDK
LLKDEDDKSV ATPYTAVIPE YRVVTHDPRF TTQKSMESNV ANGNTTIDIH HPCRVDVAVQ
KELHTHESDR SCIHLEFDIS RTGITYETGD HVGVYAENHV EIVEEAGKLL GHSLDLVFSI
HADKEDGSPL ESAVPPPFPG PCTLGTGLAR YADLLNPPRK SALVALAAYA TEPSEAEKLK
HLTSPDGKDE YSQWIVASQR SLLEVMAAFP SAKPPLGVFF AAIAPRLQPR YYSISSSPRL
APSRVHVTSA LVYGPTPTGR IHKGVCSTWM KNAVPAEKSH ECSGAPIFIR ASNFKLPSNP
STPIVMVGPG TGLAPFRGFL QERMALKEDG EELGSSLLFF GCRNRQMDFI YEDELNNFVD
QGVISELIMA FSREGAQKEY VQHKMMEKAA QVWDLIKEEG YLYVCGDAKG MARDVHRTLH
TIVQEQEGVS SSEAEAIVKK LQTEGRYLRD VW


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