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Q9HDG2

- NCPR_PHACH

UniProt

Q9HDG2 - NCPR_PHACH

Protein

NADPH--cytochrome P450 reductase

Gene

CPR

Organism
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    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.By similarity

    Catalytic activityi

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

    Cofactori

    FAD.By similarity
    FMN.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi162 – 19332FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi310 – 32112FADBy similarityAdd
    BLAST
    Nucleotide bindingi452 – 46312FADBy similarityAdd
    BLAST
    Nucleotide bindingi572 – 59019NADPBy similarityAdd
    BLAST
    Nucleotide bindingi682 – 69817NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, FMN, NADP

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH--cytochrome P450 reductase (EC:1.6.2.4)
    Short name:
    CPR
    Short name:
    P450R
    Gene namesi
    Name:CPR
    OrganismiPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)Imported
    Taxonomic identifieri5306 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesCorticialesCorticiaceaePhanerochaete

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 736736NADPH--cytochrome P450 reductasePRO_0000167607Add
    BLAST

    Proteomic databases

    PRIDEiQ9HDG2.

    Interactioni

    Protein-protein interaction databases

    STRINGi5306.JGI74736.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HDG2.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei8 – 2417HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini66 – 216151Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini269 – 546278FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.Curated
    Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
    Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0369.
    OMAiLWQLIHE.

    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. 2 hits.
    PROSITEiPS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9HDG2-1 [UniParc]FASTAAdd to Basket

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    MAVSSSSDVI VLSVGIILAA LYLFREQIFS AAKPKTVQVP SSKAAAGGNG    50
    NPRDFIAKMK EGKKRIVIFY GSQTGTAEEY AIRLAKEAKS KFGLASLVCD 100
    PEEYDFENLD QVPEDCCVFF VMATYGEGEP TDNAVQLCQN LSDESFEFSN 150
    GEHKLPGLKY VIFGLGNKTY EHYNLISRNV DRDLQKMGAI RIGERGEGDD 200
    DKSMEEDYLE WKDGMWEAFA KAMNVEEGQG GDSPDFVVTE VFDHPEEKVY 250
    LGELSARALT RTKGIHDAKN PYPAPIIAAK ELFAPGSDRN CVHIELSTES 300
    SGITYQHGDH VGVWPSNADK EVDRLLYALG LHEKKDTVIN IESLDPALAK 350
    VPFPVPTTYA TVLRHYIDIS ALAGRQILGV LAKFAPNPEA EAVLKDLNSN 400
    KEHYQNIVAN GCMKLGEVLQ YAAGNDLHAD PTASNTTAWK IPFDIIVSSI 450
    PRLQPRYYSI SSSPKLYPNA IHATVVVLKY KSEKAPRVEE RWIYGVGSNF 500
    LLNLKYASHH DKAATLVSDD SPSEPSIVSH YPTYSIEGPR GAYKQGDVVK 550
    VPIHVRRSTF RLPTNPKSPV IMIGPGTGVA PFRGFVQERV AMARRTIEKH 600
    GPEGLADWGP IRLYYGCRRS DQDFLYKDEW PEYAKELHGK FIMRCAFSRE 650
    PPYKPDGSKI YVQDLIWEDA EQIADAILNG KGYVYICGDA KSMSKSVEET 700
    LCRILGEAKG GSAEVEGAAE LKLLKERNRL LLDVWS 736
    Length:736
    Mass (Da):81,628
    Last modified:March 1, 2001 - v1
    Checksum:iAC45F12C96198AB1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF193060 Genomic DNA. Translation: AAG31349.1.
    AF193061 mRNA. Translation: AAG31350.1.
    AF193062 mRNA. Translation: AAG31351.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF193060 Genomic DNA. Translation: AAG31349.1 .
    AF193061 mRNA. Translation: AAG31350.1 .
    AF193062 mRNA. Translation: AAG31351.1 .

    3D structure databases

    ProteinModelPortali Q9HDG2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5306.JGI74736.

    Proteomic databases

    PRIDEi Q9HDG2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0369.
    OMAi LWQLIHE.

    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. 2 hits.
    PROSITEi PS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cytochrome P450 oxidoreductase gene and its differentially terminated cDNAs from the white rot fungus Phanerochaete chrysosporium."
      Yadav J.S., Loper J.C.
      Curr. Genet. 37:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM F-1767.
    2. "Phanerochaete chrysosporium NADPH-cytochrome P450 reductase kinetic mechanism."
      Warrilow A.G.S., Lamb D.C., Kelly D.E., Kelly S.L.
      Biochem. Biophys. Res. Commun. 299:189-195(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: KINETIC MECHANISM.

    Entry informationi

    Entry nameiNCPR_PHACH
    AccessioniPrimary (citable) accession number: Q9HDG2
    Secondary accession number(s): Q9HG14
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2003
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3