Reviewed, UniProtKB/Swiss-Prot P50126 (NCPR_CANMA)

Names and origin

Protein names

Recommended name:
    NADPH--cytochrome P450 reductase
      Short name=CPR
      Short name=P450R
    EC=1.6.2.4

Gene names

Name:

NCP1

Organism

Candida maltosa (Yeast)

Taxonomic identifier

5479 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	680 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (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. FMN.
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence similarities	In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	FAD FMN Flavoprotein NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro NADPH-hemoprotein reductase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 680	680	NADPH--cytochrome P450 reductase		PRO_0000167605
Regions
	Transmembrane	8 – 24	17	Potential
	Domain	60 – 204	145	Flavodoxin-like
	Domain	264 – 509	246	FAD-binding FR-type
	Nucleotide binding	149 – 180	32	FMN By similarity
	Nucleotide binding	304 – 315	12	FAD By similarity
	Nucleotide binding	435 – 446	12	FAD By similarity
	Nucleotide binding	532 – 550	19	NADP By similarity
	Nucleotide binding	628 – 644	17	NADP By similarity
Experimental info
	Sequence conflict	30	1	Q → E in BAA04997. Ref.2
	Sequence conflict	170 – 171	2	LL → VF in BAA04997. Ref.2
	Sequence conflict	565	1	F → P in BAA04997. Ref.2
	Sequence conflict	579	1	Q → K in BAA04997. Ref.2
	Sequence conflict	619	1	V → L in BAA04997. Ref.2
	Sequence conflict	664	1	E → D in BAA04997. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P50126-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: E396F81E169705C9	FASTA	680	77,131
	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

References

[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: 8701606] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: EH15D.

[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: 7545482] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 28140 / CBS 5611 / IAM 12247 / IFO 1977 / JCM 1504.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X76226 mRNA. Translation: CAA53812.1. D25327 Genomic DNA. Translation: BAA04997.1.
PIR	S63698. S63895.
3D structure databases
SMR	P50126. Positions 46-680.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.6.2.4. 3846.
Family and domain databases
InterPro	IPR003097. FAD-binding_1. IPR017927. Fd_Rdtase_FAD-bd. IPR001094. Flavdoxin-like. IPR008254. Flavodoxin/NO_synth. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR015702. NADPH_Cyt_P450_Rdtase. IPR001433. OxRdtase_FAD/NAD_bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
PANTHER	PTHR19384:SF17. NADPH_Cyt_Red. 1 hit.
Pfam	PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00369. FLAVODOXIN. PR00371. FPNCR.
PROSITE	PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NCPR_CANMA

Accession

Primary (citable) accession number: P50126

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 19, 2010
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)