NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=EH15D;
DOI=10.1002/(SICI)1097-0061(19960330)12:4<333::AID-YEA915>3.3.CO;2-3; PubMed=8701606 [NCBI, ExPASy, EBI, Israel, Japan]
Kaergel E., Honeck H., Vogel F., Boehmer A., Schunk W.-H.;
"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.";
Yeast 12:333-348(1996).

[2]

NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 28140 / CBS 5611 / IAM 12247 / IFO 1977 / JCM 1504;
PubMed=7545482 [NCBI, ExPASy, EBI, Israel, Japan]
Ohkuma M., Masuda Y., Park S.M., Ohtomo R., Ohta A., Takagi M.;
"Evidence that the expression of the gene for NADPH-cytochrome P-450 reductase is n-alkane-inducible in Candida maltosa.";
Biosci. Biotechnol. Biochem. 59:1328-1330(1995).

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

X76226; CAA53812.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D25327; BAA04997.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S63698; S63698.
S63895; S63895.

3D structure databases

HSSP

P00388; 1AMO. [HSSP ENTRY / PDB]

ModBase

P50126.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003958;	Molecular function: NADPH-hemoprotein reductase activity (inferred from electronic annotation from EC).
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).

Other

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_0000167605`
`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).`
`CONFLICT`	`30 30`		`Q -> E (in Ref. 2; BAA04997).`
`CONFLICT`	`170 171`		`LL -> VF (in Ref. 2; BAA04997).`
`CONFLICT`	`565 565`		`F -> P (in Ref. 2; BAA04997).`
`CONFLICT`	`579 579`		`Q -> K (in Ref. 2; BAA04997).`
`CONFLICT`	`619 619`		`V -> L (in Ref. 2; BAA04997).`
`CONFLICT`	`664 664`		`E -> D (in Ref. 2; BAA04997).`

Sequence information

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

Molecular weight: 77131 Da [This is the MW of the unprocessed precursor]

CRC64: E396F81E169705C9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALDKLDLYV IIVLAVAVAA YFAKNQFLDQ PQDTGFLSND TAGGNSRDIL ETLKKNNKNT 

        70         80         90        100        110        120 
LLLFGSQTGT AEDYANKLSR EIHSRFGLKT MVADFADYDW DNFGDIPNDI LVFFIVATYG 

       130        140        150        160        170        180 
EGEPTDNADE FHTWLTDEAD TLSTLRYTVF GLGNSTYEFY NAIGRKFDRL LEEKGGERFA 

       190        200        210        220        230        240 
DYGEGDDGTG TLDEDFLTWK DNVFDTLKND LNFEERELKY EPNVKLTERD DLTVDDSEVS 

       250        260        270        280        290        300 
LGEPNKKYIQ SEEIDLTKGP FDHTHPYLAK ISKTRELFAS KERNCVHVEF DVSESNLKYT 

       310        320        330        340        350        360 
TGDHLAVWPS NSDENIAKFI KCFGLDDKIN TVFELKALDS TYQIPFPNPI TYGAVVRHHL 

       370        380        390        400        410        420 
EISGPVSRQF FLAIAGFAPD EETKKTFTRI GNDKQEFANK ITRKKLNVAD ALLFASNGRP 

       430        440        450        460        470        480 
WSDVPFEFII ENVPHLQPRY YSISSSSLSE KQTINITAVV EVEEEADGRA VTGVVTNLLK 

       490        500        510        520        530        540 
NIEIEQNKTG EKPVVHYDLS GPRNKFNKFK LPVHVRRSNF KLPKNTTTPV ILIGPGTGVA 

       550        560        570        580        590        600 
PLRGFVRERV QQVKNGVNVG KTVLFYGCRN EHDDFLYKQE WSEYASVLGE NFEMFTAFSR 

       610        620        630        640        650        660 
QDPSKKVYVQ DKIAENSKVV NDLLNEGAII YVCGDASRMA RDVQSTIAKI VAKHREIQED 

       670        680 
KAVELVKSWK VQNRYQEDVW

P50126 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