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Protein

NADPH--cytochrome P450 reductase

Gene

NCP1

Organism
Candida maltosa (Yeast)
Status
Reviewed-Annotation score: Annotation score: 4 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. Involved in ergosterol biosynthesis.UniRule annotation

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • FADUniRule annotationNote: Binds 1 FAD per monomer.UniRule annotation
  • FMNUniRule annotationNote: Binds 1 FMN per monomer.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei187FMNUniRule annotation1
Binding sitei283NADPUniRule annotation1
Binding sitei537NADPUniRule annotation1
Binding sitei642NADPUniRule annotation1
Binding sitei680FADUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi66 – 71FMNUniRule annotation6
Nucleotide bindingi117 – 120FMNUniRule annotation4
Nucleotide bindingi152 – 161FMNUniRule annotation10
Nucleotide bindingi439 – 442FADUniRule annotation4
Nucleotide bindingi457 – 459FADUniRule annotation3
Nucleotide bindingi473 – 476FADUniRule annotation4
Nucleotide bindingi599 – 600NADPUniRule annotation2
Nucleotide bindingi606 – 610NADPUniRule annotation5

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

FAD, Flavoprotein, FMN, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18776.

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH--cytochrome P450 reductaseUniRule annotation (EC:1.6.2.4UniRule annotation)
Short name:
CPRUniRule annotation
Short name:
P450RUniRule annotation
Gene namesi
Name:NCP1UniRule annotation
OrganismiCandida maltosa (Yeast)
Taxonomic identifieri5479 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

Subcellular locationi

  • Endoplasmic reticulum membrane UniRule annotation; Single-pass membrane protein UniRule annotation; Cytoplasmic side UniRule annotation
  • Mitochondrion outer membrane UniRule annotation; Single-pass membrane protein UniRule annotation; Cytoplasmic side UniRule annotation
  • Cell membrane UniRule annotation; Single-pass membrane protein UniRule annotation; Cytoplasmic side UniRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 5LumenalUniRule annotation5
Transmembranei6 – 23HelicalUniRule annotationAdd BLAST18
Topological domaini24 – 680CytoplasmicUniRule annotationAdd BLAST657

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001676051 – 680NADPH--cytochrome P450 reductaseAdd BLAST680

Structurei

3D structure databases

ProteinModelPortaliP50126.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini60 – 204Flavodoxin-likeUniRule annotationAdd BLAST145
Domaini264 – 509FAD-binding FR-typeUniRule annotationAdd BLAST246

Sequence similaritiesi

Belongs to the NADPH--cytochrome P450 reductase family.UniRule annotation
In the N-terminal section; belongs to the flavodoxin family.UniRule annotation
In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.UniRule annotation
Contains 1 FAD-binding FR-type domain.UniRule annotation
Contains 1 flavodoxin-like domain.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
HAMAPiMF_03212. NCPR. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
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)DescriptionActionsGraphical viewLength
Sequence conflicti30Q → E in BAA04997 (PubMed:7545482).Curated1
Sequence conflicti170 – 171LL → VF in BAA04997 (PubMed:7545482).Curated2
Sequence conflicti565F → P in BAA04997 (PubMed:7545482).Curated1
Sequence conflicti579Q → K in BAA04997 (PubMed:7545482).Curated1
Sequence conflicti619V → L in BAA04997 (PubMed:7545482).Curated1
Sequence conflicti664E → D in BAA04997 (PubMed:7545482).Curated1

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.
PIRiS63698.
S63895.

3D structure databases

ProteinModelPortaliP50126.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18776.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
HAMAPiMF_03212. NCPR. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
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]
ProtoNetiSearch...

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 2, 2016
This is version 100 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.