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Q9SB48

- NCPR1_ARATH

UniProt

Q9SB48 - NCPR1_ARATH

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Protein

NADPH--cytochrome P450 reductase 1

Gene
ATR1, AR1, At4g24520, F22K18.280
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.5 Publications

Catalytic activityi

NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.

Cofactori

FAD.1 Publication
FMN.1 Publication

Kineticsi

  1. KM=2.2 µM for NADPH (at pH 7.0 and 25 degrees Celsius) (1 Publication)3 Publications
  2. KM=21.9 µM for NADPH (at pH 7.7 and 28 degrees Celsius) (1 Publication)
  3. KM=2.0 µM for NADPH (at pH 7.25 and 25 degrees Celsius) (1 Publication)
  4. KM=17 µM for cytochrome c (at pH 7.0 and 25 degrees Celsius) (1 Publication)
  5. KM=24.3 µM for cytochrome c (at pH 7.7 and 28 degrees Celsius) (1 Publication)

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi91 – 955FMN By similarity
Nucleotide bindingi181 – 21232FMN By similarityAdd
BLAST
Nucleotide bindingi326 – 33712FAD By similarityAdd
BLAST
Nucleotide bindingi467 – 47711FAD By similarityAdd
BLAST
Nucleotide bindingi545 – 56319NADP By similarityAdd
BLAST
Nucleotide bindingi639 – 65517NADP By similarityAdd
BLAST

GO - Molecular functioni

  1. FMN binding Source: InterPro
  2. iron ion binding Source: InterPro
  3. NADPH-hemoprotein reductase activity Source: TAIR

GO - Biological processi

  1. phenylpropanoid metabolic process Source: TAIR
  2. response to abscisic acid Source: TAIR
  3. response to oxidative stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Phenylpropanoid metabolism

Keywords - Ligandi

FAD, Flavoprotein, FMN, NADP

Enzyme and pathway databases

BioCyciARA:AT4G24520-MONOMER.
ARA:GQT-1216-MONOMER.
MetaCyc:MONOMER-2101.

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH--cytochrome P450 reductase 1 (EC:1.6.2.4)
Gene namesi
Name:ATR1
Synonyms:AR1
Ordered Locus Names:At4g24520
ORF Names:F22K18.280
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G24520.

Subcellular locationi

Endoplasmic reticulum membrane; Peripheral membrane protein Inferred
Note: Anchored to the ER membrane by its N-terminal hydrophobic region By similarity.

GO - Cellular componenti

  1. cytosol Source: TAIR
  2. endoplasmic reticulum Source: TAIR
  3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 692691NADPH--cytochrome P450 reductase 1PRO_0000416839Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication
Modified residuei249 – 2491Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ9SB48.

Expressioni

Tissue specificityi

Expressed in roots, leaves, stems, flowers and siliques.1 Publication

Gene expression databases

GenevestigatoriQ9SB48.

Structurei

3D structure databases

ProteinModelPortaliQ9SB48.
SMRiQ9SB48. Positions 85-692.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 235151Flavodoxin-likeAdd
BLAST
Domaini290 – 537248FAD-binding FR-typeAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.

Phylogenomic databases

HOGENOMiHOG000282027.
InParanoidiQ9SB48.
KOiK00327.
OMAiFLYREEW.
PhylomeDBiQ9SB48.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000208. P450R. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9SB48-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MTSALYASDL FKQLKSIMGT DSLSDDVVLV IATTSLALVA GFVVLLWKKT    50
TADRSGELKP LMIPKSLMAK DEDDDLDLGS GKTRVSIFFG TQTGTAEGFA 100
KALSEEIKAR YEKAAVKVID LDDYAADDDQ YEEKLKKETL AFFCVATYGD 150
GEPTDNAARF YKWFTEENER DIKLQQLAYG VFALGNRQYE HFNKIGIVLD 200
EELCKKGAKR LIEVGLGDDD QSIEDDFNAW KESLWSELDK LLKDEDDKSV 250
ATPYTAVIPE YRVVTHDPRF TTQKSMESNV ANGNTTIDIH HPCRVDVAVQ 300
KELHTHESDR SCIHLEFDIS RTGITYETGD HVGVYAENHV EIVEEAGKLL 350
GHSLDLVFSI HADKEDGSPL ESAVPPPFPG PCTLGTGLAR YADLLNPPRK 400
SALVALAAYA TEPSEAEKLK HLTSPDGKDE YSQWIVASQR SLLEVMAAFP 450
SAKPPLGVFF AAIAPRLQPR YYSISSSPRL APSRVHVTSA LVYGPTPTGR 500
IHKGVCSTWM KNAVPAEKSH ECSGAPIFIR ASNFKLPSNP STPIVMVGPG 550
TGLAPFRGFL QERMALKEDG EELGSSLLFF GCRNRQMDFI YEDELNNFVD 600
QGVISELIMA FSREGAQKEY VQHKMMEKAA QVWDLIKEEG YLYVCGDAKG 650
MARDVHRTLH TIVQEQEGVS SSEAEAIVKK LQTEGRYLRD VW 692
Length:692
Mass (Da):76,766
Last modified:May 1, 2000 - v1
Checksum:i7DD77E418CCF2FA6
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti161 – 1611Y → S in CAA46814. 1 Publication
Sequence conflicti477 – 4804SPRL → CQDW in CAA46814. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66016 mRNA. Translation: CAA46814.1.
AL035356 Genomic DNA. Translation: CAA23011.1.
AL161561 Genomic DNA. Translation: CAB79362.1.
CP002687 Genomic DNA. Translation: AEE84919.1.
AY054688 mRNA. Translation: AAK96879.1.
BT008426 mRNA. Translation: AAP37785.1.
PIRiT05582.
RefSeqiNP_194183.1. NM_118585.3. [Q9SB48-1]
UniGeneiAt.144.
At.70123.

Genome annotation databases

EnsemblPlantsiAT4G24520.1; AT4G24520.1; AT4G24520. [Q9SB48-1]
GeneIDi828554.
KEGGiath:AT4G24520.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66016 mRNA. Translation: CAA46814.1 .
AL035356 Genomic DNA. Translation: CAA23011.1 .
AL161561 Genomic DNA. Translation: CAB79362.1 .
CP002687 Genomic DNA. Translation: AEE84919.1 .
AY054688 mRNA. Translation: AAK96879.1 .
BT008426 mRNA. Translation: AAP37785.1 .
PIRi T05582.
RefSeqi NP_194183.1. NM_118585.3. [Q9SB48-1 ]
UniGenei At.144.
At.70123.

3D structure databases

ProteinModelPortali Q9SB48.
SMRi Q9SB48. Positions 85-692.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q9SB48.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G24520.1 ; AT4G24520.1 ; AT4G24520 . [Q9SB48-1 ]
GeneIDi 828554.
KEGGi ath:AT4G24520.

Organism-specific databases

TAIRi AT4G24520.

Phylogenomic databases

HOGENOMi HOG000282027.
InParanoidi Q9SB48.
KOi K00327.
OMAi FLYREEW.
PhylomeDBi Q9SB48.

Enzyme and pathway databases

BioCyci ARA:AT4G24520-MONOMER.
ARA:GQT-1216-MONOMER.
MetaCyc:MONOMER-2101.

Gene expression databases

Genevestigatori Q9SB48.

Family and domain databases

Gene3Di 1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProi IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
Pfami PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000208. P450R. 1 hit.
PRINTSi PR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMi SSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEi PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, yeast expression, and characterization of the coupling of two distantly related Arabidopsis thaliana NADPH-cytochrome P450 reductases with P450 CYP73A5."
    Urban P., Mignotte C., Kazmaier M., Delorme F., Pompon D.
    J. Biol. Chem. 272:19176-19186(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: cv. Landsberg erecta.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    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.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Differential redox and electron-transfer properties of purified yeast, plant and human NADPH-cytochrome P-450 reductases highly modulate cytochrome P-450 activities."
    Louerat-Oriou B., Perret A., Pompon D.
    Eur. J. Biochem. 258:1040-1049(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
  6. "Two isoforms of NADPH:cytochrome P450 reductase in Arabidopsis thaliana. Gene structure, heterologous expression in insect cells, and differential regulation."
    Mizutani M., Ohta D.
    Plant Physiol. 116:357-367(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
  7. "High yield purification and characterization of engineered human P450 1A2 and generation of immuno-inhibitor antibodies."
    Louerat-Oriou B., Flinois J.P., Beaune P.H., Pompon D.
    Pharmacogenetics 9:61-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Microsomal electron transfer in higher plants: cloning and heterologous expression of NADH-cytochrome b5 reductase from Arabidopsis."
    Fukuchi-Mizutani M., Mizutani M., Tanaka Y., Kusumi T., Ohta D.
    Plant Physiol. 119:353-361(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  9. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNCPR1_ARATH
AccessioniPrimary (citable) accession number: Q9SB48
Secondary accession number(s): Q39035
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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