[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2118906 [NCBI, ExPASy, EBI, Israel, Japan] Sutter T.R., Sanglard D., Loper J.C.; "Isolation and characterization of the alkane-inducible NADPH-cytochrome P-450 oxidoreductase gene from Candida tropicalis. Identification of invariant residues within similar amino acid sequences of divergent flavoproteins."; J. Biol. Chem. 265:16428-16436(1990).
[2]	ERRATUM. Sutter T.R., Sanglard D., Loper J.C.; J. Biol. Chem. 265:22056-22056(1990).

Comments

FUNCTION: 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 ACTIVITY: NADPH + n oxidized hemoprotein = NADP⁺ + n reduced hemoprotein.
COFACTOR: FAD.
COFACTOR: FMN.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein.
SIMILARITY: In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.
SIMILARITY: Contains 1 flavodoxin-like domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M35199; AAA34333.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A37890; A37890.

3D structure databases

HSSP

P16435; 1B1C. [HSSP ENTRY / PDB]

ModBase

P37201.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0010181;	Molecular function: FMN binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0003958;	Molecular function: NADPH-hemoprotein reductase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003097; FAD-binding_1.
IPR001094; Flavdoxin_like.
IPR008254; Flavodoxin/NO_synth.
IPR001709; FPN_cyt_redctse.
IPR015702; NADPH_Cyt_Red.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.

PANTHER

PTHR19384:SF17; NADPH_Cyt_Red; 1.

Pfam

PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00369; FLAVODOXIN.
PR00371; FPNCR.

PROSITE

PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P37201.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Endoplasmic reticulum; FAD; Flavoprotein; FMN; Membrane; NADP; Oxidoreductase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 680`	`680`	`NADPH--cytochrome P450 reductase.`	`PRO_0000167606`
`TRANSMEM`	`8 24`	`17`	`Potential.`
`DOMAIN`	`60 204`	`145`	`Flavodoxin-like.`
`DOMAIN`	`264 509`	`246`	`FAD-binding FR-type.`
`NP_BIND`	`149 180`	`32`	`FMN (By similarity).`
`NP_BIND`	`304 315`	`12`	`FAD (By similarity).`
`NP_BIND`	`435 446`	`12`	`FAD (By similarity).`
`NP_BIND`	`532 550`	`19`	`NADP (By similarity).`
`NP_BIND`	`628 644`	`17`	`NADP (By similarity).`

Sequence information

Length: 680 AA [This is the length of the unprocessed precursor]

Molecular weight: 76689 Da [This is the MW of the unprocessed precursor]

CRC64: AB31ABFF8ADA41DA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALDKLDLYV IITLVVAIAA YFAKNQFLDQ QQDTGFLNTD SGDGNSRDIL QALKKNNKNT 

        70         80         90        100        110        120 
LLLFGSQTGT AEDYANKLSR ELHSRFGLKT MVADFADYDF ENFGDITEDI LVFFIVATYG 

       130        140        150        160        170        180 
EGEPTDNADE FHTWLTEEAD TLSTLKYTVF GLGNSTYEFF NAIGRKFDRL LGEKGGDRFA 

       190        200        210        220        230        240 
EYGEGDDGTG TLDEDFLAWK DNVFDSLKND LNFEEKELKY EPNVKLTERD DLSGNDPDVS 

       250        260        270        280        290        300 
LGEPNVKYIK SEGVDLTKGP FDHTHPFLAR IVKTKELFTS EDRHCVHVEF DISESNLKYT 

       310        320        330        340        350        360 
TGDHLAIWPS NSDENIKQFA KCFGLEDKLD TVIELKALDS TYSIPFPNPI TYGAVIRHHL 

       370        380        390        400        410        420 
EISGPVSRQF FLSIAGFAPD EETKKSFTRI GGDKQEFASK VTRRKFNIAD ALLFASNNRP 

       430        440        450        460        470        480 
WSDVPFEFLI ENVQHLTPRY YSISSSSLSE KQTINVTAVV EAEEEADGRP VTGVVTNLLK 

       490        500        510        520        530        540 
NIEIEQNKTG ETPMVHYDLN GPRGKFSKFR LPVHVRRSNF KLPKNSTTPV ILIGPGTGVA 

       550        560        570        580        590        600 
PLRGFVRERV QQVKNGVNVG KTVLFYGCRN SEQDFLYKQE WSEYASVLGE NFEMFNAFSR 

       610        620        630        640        650        660 
QDPTKKVYVQ DKILENSALV DELLSSGAII YVCGDASRMA RDVQAAIAKI VAKSRDIHED 

       670        680 
KAAELVKSWK VQNRYQEDVW

P37201 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools