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P50126

- NCPR_CANMA

UniProt

P50126 - NCPR_CANMA

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Protein

NADPH--cytochrome P450 reductase

Gene

NCP1

Organism
Candida maltosa (Yeast)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript 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.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

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
Complete GO annotation...

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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

Subcellular locationi

Topology

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

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

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...

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

« Hide

        10         20         30         40         50
MALDKLDLYV IIVLAVAVAA YFAKNQFLDQ PQDTGFLSND TAGGNSRDIL
60 70 80 90 100
ETLKKNNKNT LLLFGSQTGT AEDYANKLSR EIHSRFGLKT MVADFADYDW
110 120 130 140 150
DNFGDIPNDI LVFFIVATYG EGEPTDNADE FHTWLTDEAD TLSTLRYTVF
160 170 180 190 200
GLGNSTYEFY NAIGRKFDRL LEEKGGERFA DYGEGDDGTG TLDEDFLTWK
210 220 230 240 250
DNVFDTLKND LNFEERELKY EPNVKLTERD DLTVDDSEVS LGEPNKKYIQ
260 270 280 290 300
SEEIDLTKGP FDHTHPYLAK ISKTRELFAS KERNCVHVEF DVSESNLKYT
310 320 330 340 350
TGDHLAVWPS NSDENIAKFI KCFGLDDKIN TVFELKALDS TYQIPFPNPI
360 370 380 390 400
TYGAVVRHHL EISGPVSRQF FLAIAGFAPD EETKKTFTRI GNDKQEFANK
410 420 430 440 450
ITRKKLNVAD ALLFASNGRP WSDVPFEFII ENVPHLQPRY YSISSSSLSE
460 470 480 490 500
KQTINITAVV EVEEEADGRA VTGVVTNLLK NIEIEQNKTG EKPVVHYDLS
510 520 530 540 550
GPRNKFNKFK LPVHVRRSNF KLPKNTTTPV ILIGPGTGVA PLRGFVRERV
560 570 580 590 600
QQVKNGVNVG KTVLFYGCRN EHDDFLYKQE WSEYASVLGE NFEMFTAFSR
610 620 630 640 650
QDPSKKVYVQ DKIAENSKVV NDLLNEGAII YVCGDASRMA RDVQSTIAKI
660 670 680
VAKHREIQED KAVELVKSWK VQNRYQEDVW
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:
EMBLi
GenBanki
DDBJi
Links Updated
X76226 mRNA. Translation: CAA53812.1.
D25327 Genomic DNA. Translation: BAA04997.1.
PIRiS63698.
S63895.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 94 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