SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P50126

- NCPR_CANMA

UniProt

P50126 - NCPR_CANMA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

FAD.
FMN.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi149 – 18032FMN By similarityAdd
BLAST
Nucleotide bindingi304 – 31512FAD By similarityAdd
BLAST
Nucleotide bindingi435 – 44612FAD By similarityAdd
BLAST
Nucleotide bindingi532 – 55019NADP By similarityAdd
BLAST
Nucleotide bindingi628 – 64417NADP By 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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei8 – 2417Helical; Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini60 – 204145Flavodoxin-likeAdd
BLAST
Domaini264 – 509246FAD-binding FR-typeAdd
BLAST

Sequence similaritiesi

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

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

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301Q → E in BAA04997. 1 Publication
Sequence conflicti170 – 1712LL → VF in BAA04997. 1 Publication
Sequence conflicti565 – 5651F → P in BAA04997. 1 Publication
Sequence conflicti579 – 5791Q → K in BAA04997. 1 Publication
Sequence conflicti619 – 6191V → L in BAA04997. 1 Publication
Sequence conflicti664 – 6641E → D in BAA04997. 1 Publication

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: September 3, 2014
This is version 91 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

Similar proteinsi