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P50126

- NCPR_CANMA

UniProt

P50126 - NCPR_CANMA

Protein

NADPH--cytochrome P450 reductase

Gene

NCP1

Organism
Candida maltosa (Yeast)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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.

    Catalytic activityi

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

    Cofactori

    FAD.
    FMN.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi149 – 18032FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi304 – 31512FADBy similarityAdd
    BLAST
    Nucleotide bindingi435 – 44612FADBy similarityAdd
    BLAST
    Nucleotide bindingi532 – 55019NADPBy similarityAdd
    BLAST
    Nucleotide bindingi628 – 64417NADPBy 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:NCP1
    OrganismiCandida maltosa (Yeast)
    Taxonomic identifieri5479 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

    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 – 680680NADPH--cytochrome P450 reductasePRO_0000167605Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP50126.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

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

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini60 – 204145Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini264 – 509246FAD-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

    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.

    P50126-1 [UniParc]FASTAAdd to Basket

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    MALDKLDLYV IIVLAVAVAA YFAKNQFLDQ PQDTGFLSND TAGGNSRDIL    50
    ETLKKNNKNT LLLFGSQTGT AEDYANKLSR EIHSRFGLKT MVADFADYDW 100
    DNFGDIPNDI LVFFIVATYG EGEPTDNADE FHTWLTDEAD TLSTLRYTVF 150
    GLGNSTYEFY NAIGRKFDRL LEEKGGERFA DYGEGDDGTG TLDEDFLTWK 200
    DNVFDTLKND LNFEERELKY EPNVKLTERD DLTVDDSEVS LGEPNKKYIQ 250
    SEEIDLTKGP FDHTHPYLAK ISKTRELFAS KERNCVHVEF DVSESNLKYT 300
    TGDHLAVWPS NSDENIAKFI KCFGLDDKIN TVFELKALDS TYQIPFPNPI 350
    TYGAVVRHHL EISGPVSRQF FLAIAGFAPD EETKKTFTRI GNDKQEFANK 400
    ITRKKLNVAD ALLFASNGRP WSDVPFEFII ENVPHLQPRY YSISSSSLSE 450
    KQTINITAVV EVEEEADGRA VTGVVTNLLK NIEIEQNKTG EKPVVHYDLS 500
    GPRNKFNKFK LPVHVRRSNF KLPKNTTTPV ILIGPGTGVA PLRGFVRERV 550
    QQVKNGVNVG KTVLFYGCRN EHDDFLYKQE WSEYASVLGE NFEMFTAFSR 600
    QDPSKKVYVQ DKIAENSKVV NDLLNEGAII YVCGDASRMA RDVQSTIAKI 650
    VAKHREIQED KAVELVKSWK VQNRYQEDVW 680
    Length:680
    Mass (Da):77,131
    Last modified:October 1, 1996 - v1
    Checksum:iE396F81E169705C9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 301Q → E in BAA04997. (PubMed:7545482)Curated
    Sequence conflicti170 – 1712LL → VF in BAA04997. (PubMed:7545482)Curated
    Sequence conflicti565 – 5651F → P in BAA04997. (PubMed:7545482)Curated
    Sequence conflicti579 – 5791Q → K in BAA04997. (PubMed:7545482)Curated
    Sequence conflicti619 – 6191V → L in BAA04997. (PubMed:7545482)Curated
    Sequence conflicti664 – 6641E → D in BAA04997. (PubMed:7545482)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76226 mRNA. Translation: CAA53812.1.
    D25327 Genomic DNA. Translation: BAA04997.1.
    PIRiS63698.
    S63895.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76226 mRNA. Translation: CAA53812.1 .
    D25327 Genomic DNA. Translation: BAA04997.1 .
    PIRi S63698.
    S63895.

    3D structure databases

    ProteinModelPortali P50126.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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

    1. "Candida maltosa NADPH-cytochrome P450 reductase: cloning of a full-length cDNA, heterologous expression in Saccharomyces cerevisiae and function of the N-terminal region for membrane anchoring and proliferation of the endoplasmic reticulum."
      Kaergel E., Honeck H., Vogel F., Boehmer A., Schunk W.-H.
      Yeast 12:333-348(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: EH15.
    2. "Evidence that the expression of the gene for NADPH-cytochrome P-450 reductase is n-alkane-inducible in Candida maltosa."
      Ohkuma M., Masuda Y., Park S.M., Ohtomo R., Ohta A., Takagi M.
      Biosci. Biotechnol. Biochem. 59:1328-1330(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 28140 / CBS 5611 / IAM 12247 / JCM 1504 / NBRC 1977.

    Entry informationi

    Entry nameiNCPR_CANMA
    AccessioniPrimary (citable) accession number: P50126
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 92 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