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Q9SUM3

- NCPR2_ARATH

UniProt

Q9SUM3 - NCPR2_ARATH

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Protein

NADPH--cytochrome P450 reductase 2

Gene
ATR2, AR2, At4g30210, F9N11.60
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=23 µM for NADPH (at pH 7.7 and 28 degrees Celsius) (1 Publication)4 Publications
  2. KM=2.0 µM for NADPH (at pH 7.25 and 25 degrees Celsius) (PubMed:99097071)
  3. KM=15 µM for cytochrome c (at pH 7.7 and 30 degrees Celsius) (1 Publication)
  4. KM=16 µM for cytochrome c (at pH 7.0 and 25 degrees Celsius) (1 Publication)
  5. KM=22.5 µM for cytochrome c (at pH 7.7 and 28 degrees Celsius) (1 Publication)

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi111 – 1155FMN By similarity
Nucleotide bindingi201 – 23232FMN By similarityAdd
BLAST
Nucleotide bindingi346 – 35712FAD By similarityAdd
BLAST
Nucleotide bindingi486 – 49611FAD By similarityAdd
BLAST
Nucleotide bindingi564 – 58219NADP By similarityAdd
BLAST
Nucleotide bindingi658 – 67417NADP 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. oxidation-reduction process Source: GOC
  2. phenylpropanoid metabolic process 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:GQT-1816-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH--cytochrome P450 reductase 2 (EC:1.6.2.4)
Gene namesi
Name:ATR2
Synonyms:AR2
Ordered Locus Names:At4g30210
ORF Names:F9N11.60
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G30210.

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. chloroplast 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
Chaini1 – 711711NADPH--cytochrome P450 reductase 2PRO_0000416840Add
BLAST

Proteomic databases

PRIDEiQ9SUM3.

Expressioni

Tissue specificityi

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

Inductioni

By wounding and transition from dark to light.1 Publication

Gene expression databases

ArrayExpressiQ9SUM3.
GenevestigatoriQ9SUM3.

Structurei

3D structure databases

ProteinModelPortaliQ9SUM3.
SMRiQ9SUM3. Positions 96-711.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini105 – 255151Flavodoxin-likeAdd
BLAST
Domaini310 – 556247FAD-binding FR-typeAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000282027.
KOiK00327.
OMAiHEFLQSK.
PhylomeDBiQ9SUM3.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9SUM3-1) [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

MSSSSSSSTS MIDLMAAIIK GEPVIVSDPA NASAYESVAA ELSSMLIENR    50
QFAMIVTTSI AVLIGCIVML VWRRSGSGNS KRVEPLKPLV IKPREEEIDD 100
GRKKVTIFFG TQTGTAEGFA KALGEEAKAR YEKTRFKIVD LDDYAADDDE 150
YEEKLKKEDV AFFFLATYGD GEPTDNAARF YKWFTEGNDR GEWLKNLKYG 200
VFGLGNRQYE HFNKVAKVVD DILVEQGAQR LVQVGLGDDD QCIEDDFTAW 250
REALWPELDT ILREEGDTAV ATPYTAAVLE YRVSIHDSED AKFNDINMAN 300
GNGYTVFDAQ HPYKANVAVK RELHTPESDR SCIHLEFDIA GSGLTYETGD 350
HVGVLCDNLS ETVDEALRLL DMSPDTYFSL HAEKEDGTPI SSSLPPPFPP 400
CNLRTALTRY ACLLSSPKKS ALVALAAHAS DPTEAERLKH LASPAGKDEY 450
SKWVVESQRS LLEVMAEFPS AKPPLGVFFA GVAPRLQPRF YSISSSPKIA 500
ETRIHVTCAL VYEKMPTGRI HKGVCSTWMK NAVPYEKSEN CSSAPIFVRQ 550
SNFKLPSDSK VPIIMIGPGT GLAPFRGFLQ ERLALVESGV ELGPSVLFFG 600
CRNRRMDFIY EEELQRFVES GALAELSVAF SREGPTKEYV QHKMMDKASD 650
IWNMISQGAY LYVCGDAKGM ARDVHRSLHT IAQEQGSMDS TKAEGFVKNL 700
QTSGRYLRDV W 711
Length:711
Mass (Da):78,927
Last modified:May 1, 2000 - v1
Checksum:iF0503108EB7F508F
GO
Isoform 2 (identifier: Q9SUM3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     447-447: K → KV

Note: May be due to a competing donor splice site. No experimental confirmation available.

Show »
Length:712
Mass (Da):79,026
Checksum:i75656CFE0CC4DB63
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei447 – 4471K → KV in isoform 2. VSP_042906

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti297 – 2982NM → TL in CAA46815. 1 Publication
Sequence conflicti346 – 3483YET → MKL in CAA46815. 1 Publication
Sequence conflicti540 – 5445NCSSA → KLFLGR in CAA46815. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66017 mRNA. Translation: CAA46815.1.
AL109796 Genomic DNA. Translation: CAB52465.1.
AL161576 Genomic DNA. Translation: CAB81014.1.
CP002687 Genomic DNA. Translation: AEE85737.1.
CP002687 Genomic DNA. Translation: AEE85738.1.
AF325101 mRNA. Translation: AAK17169.1.
PIRiS21531.
T14081.
RefSeqiNP_194750.1. NM_119167.3. [Q9SUM3-1]
NP_849472.2. NM_179141.2. [Q9SUM3-2]
UniGeneiAt.145.

Genome annotation databases

EnsemblPlantsiAT4G30210.2; AT4G30210.2; AT4G30210. [Q9SUM3-1]
GeneIDi829144.
KEGGiath:AT4G30210.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66017 mRNA. Translation: CAA46815.1 .
AL109796 Genomic DNA. Translation: CAB52465.1 .
AL161576 Genomic DNA. Translation: CAB81014.1 .
CP002687 Genomic DNA. Translation: AEE85737.1 .
CP002687 Genomic DNA. Translation: AEE85738.1 .
AF325101 mRNA. Translation: AAK17169.1 .
PIRi S21531.
T14081.
RefSeqi NP_194750.1. NM_119167.3. [Q9SUM3-1 ]
NP_849472.2. NM_179141.2. [Q9SUM3-2 ]
UniGenei At.145.

3D structure databases

ProteinModelPortali Q9SUM3.
SMRi Q9SUM3. Positions 96-711.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q9SUM3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G30210.2 ; AT4G30210.2 ; AT4G30210 . [Q9SUM3-1 ]
GeneIDi 829144.
KEGGi ath:AT4G30210.

Organism-specific databases

TAIRi AT4G30210.

Phylogenomic databases

HOGENOMi HOG000282027.
KOi K00327.
OMAi HEFLQSK.
PhylomeDBi Q9SUM3.

Enzyme and pathway databases

BioCyci ARA:GQT-1816-MONOMER.

Gene expression databases

ArrayExpressi Q9SUM3.
Genevestigatori Q9SUM3.

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] (ISOFORM 1), 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] (ISOFORM 1).
    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, INDUCTION.
  7. "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.
  8. "Bacterial expression and purification of the Arabidopsis NADPH-cytochrome P450 reductase ATR2."
    Hull A.K., Celenza J.L.
    Protein Expr. Purif. 18:310-315(2000) [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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.

Entry informationi

Entry nameiNCPR2_ARATH
AccessioniPrimary (citable) accession number: Q9SUM3
Secondary accession number(s): F4JPK2, Q39036
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 95 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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