NADH-cytochrome b5 reductase 1 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P38626 (NCB5R_YEAST)

Last modified January 19, 2010. Version 87. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    NADH-cytochrome b5 reductase 1
    EC=1.6.2.2
Alternative name(s):
    Microsomal cytochrome b reductase
    P35

Gene names

Name:	CBR1
Synonyms:	CBR, CBR5
Ordered Locus Names:	YIL043C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	284 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Electron donor reductase for cytochrome b5. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes. Plays a role in bud morphology. Ref.5
Catalytic activity	NADH + 2 ferricytochrome b5 = NAD⁺ + H⁺ + 2 ferrocytochrome b5.
Cofactor	FAD.
Enzyme regulation	Competitively inhibited by NAD⁺. Inhibited by mercurials such as p-chloromercuribenzoate (PCMB) and HgCl₂. Enzymatic activity increases under anaerobic conditions. Ref.3 Ref.4
Subunit structure	Monomer. Interacts with STE20. Ref.3 Ref.11
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion outer membrane; Single-pass membrane protein Potential Ref.7 Ref.10.
Induction	Protein levels are highest during exponential growth phase and lowest in stationary phase. Ref.3 Ref.4
Miscellaneous	Present with 4820 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain.
Biophysicochemical properties	Kinetic parameters: K_M=6.3 µM for NADH K_M=0.8 µM for cytochrome b5 pH dependence: Optimum pH is 5.6. Active from pH 5 to 7.5.

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Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
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 microsome Ref.3 Inferred from direct assay. Source: SGD mitochondrial outer membrane Ref.10 Inferred from direct assay. Source: SGD
Molecular function	cytochrome-b5 reductase activity Ref.3 Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
	Q12164	1	EBI-2048224,EBI-30000
AGP1	P25376	1	EBI-2048224,EBI-2357
CAN1	P04817	1	EBI-2048224,EBI-3993
CHO1	P08456	1	EBI-2048224,EBI-14055
ERP1	Q05359	1	EBI-2048224,EBI-6581
ERP2	P39704	1	EBI-2048224,EBI-6587
ERV25	P54837	1	EBI-2048224,EBI-6642
GAP1	P19145	1	EBI-2048224,EBI-7314
ORM1	P53224	1	EBI-2048224,EBI-12592
ORM2	Q06144	1	EBI-2048224,EBI-34916
OST1	P41543	1	EBI-2048224,EBI-12651
PHO84	P25297	1	EBI-2048224,EBI-13320
PHS1	P40857	1	EBI-2048224,EBI-26003
PMP2	P40975	1	EBI-2048224,EBI-2043041
PMP3	P87284	1	EBI-2048224,EBI-13555
RTN1	Q04947	1	EBI-2048224,EBI-38020
SAC1	P32368	1	EBI-2048224,EBI-16210
SEC63	P14906	1	EBI-2048224,EBI-16636
SPF1	P39986	1	EBI-2048224,EBI-3128
YER053C-A	Q3E7B0	1	EBI-2048224,EBI-2047907
YOP1	Q12402	1	EBI-2048224,EBI-37092

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 284

284

NADH-cytochrome b5 reductase 1

PRO_0000167627

Regions

Transmembrane

7 – 27

Potential

Domain

38 – 142

105

FAD-binding FR-type

Nucleotide binding

122 – 137

FAD By similarity

Nucleotide binding

148 – 180

FAD By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P38626-1 [UniParc].

Last modified April 29, 2008. Version 2.
Checksum: 0E71E7AB083BB623
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FASTA

284

31,494

        10         20         30         40         50         60 
MAIDAQKLVV VIVIVVVPLL FKFIIGPKTK PVLDPKRNDF QSFPLVEKTI LTHNTSMYKF 

        70         80         90        100        110        120 
GLPHADDVLG LPIGQHIVIK ANINGKDITR SYTPTSLDGD TKGNFELLVK SYPTGNVSKM 

       130        140        150        160        170        180 
IGELKIGDSI QIKGPRGNYH YERNCRSHLG MIAGGTGIAP MYQIMKAIAM DPHDTTKVSL 

       190        200        210        220        230        240 
VFGNVHEEDI LLKKELEALV AMKPSQFKIV YYLDSPDRED WTGGVGYITK DVIKEHLPAA 

       250        260        270        280 
TMDNVQILIC GPPAMVASVR RSTVDLGFRR SKPLSKMEDQ VFVF

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and complete sequence of CBR, a gene encoding a putative cytochrome b reductase in Saccharomyces cerevisiae." Csukai M., Murray M., Orr E. Eur. J. Biochem. 219:441-448(1994) [PubMed: 8307010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 842.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. Barrell B.G. Nature 387:84-87(1997) [PubMed: 9169870] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Studies on the microsomal electron-transport system of anaerobically grown yeast. IV. Purification and characterization of NADH-cytochrome b5 reductase." Kubota S., Yoshida Y., Kumaoka H. J. Biochem. 81:187-195(1977) [PubMed: 14930] [Abstract] Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
[4]	"Influence of oxygen on the microsomal electron transport system in Saccharomyces cerevisiae." Bertrand J.-C., Mattei G., Parra C., Giordani R., Gilewicz M. Biochimie 66:583-588(1984) [PubMed: 6442167] [Abstract] Cited for: INDUCTION, ENZYME REGULATION.
[5]	"Biodiversity of the P450 catalytic cycle: yeast cytochrome b5/NADH cytochrome b5 reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction." Lamb D.C., Kelly D.E., Manning N.J., Kaderbhai M.A., Kelly S.L. FEBS Lett. 462:283-288(1999) [PubMed: 10622712] [Abstract] Cited for: FUNCTION.
[6]	"Sequencing and comparison of yeast species to identify genes and regulatory elements." Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S. Nature 423:241-254(2003) [PubMed: 12748633] [Abstract] Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[7]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"Mapping of transcription start sites in Saccharomyces cerevisiae using 5' SAGE." Zhang Z., Dietrich F.S. Nucleic Acids Res. 33:2838-2851(2005) [PubMed: 15905473] [Abstract] Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[10]	"Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins." Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N., Schoenfisch B., Guiard B., Pfanner N., Meisinger C. Mol. Biol. Cell 17:1436-1450(2006) [PubMed: 16407407] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[11]	"Proteins involved in sterol synthesis interact with Ste20 and regulate cell polarity." Tiedje C., Holland D.G., Just U., Hofken T. J. Cell Sci. 120:3613-3624(2007) [PubMed: 17895367] [Abstract] Cited for: INTERACTION WITH STE20.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	Z28365 Genomic DNA. Translation: CAA82214.1. Different initiation. Z46861 Genomic DNA. Translation: CAA86908.1. Different initiation.
PIR	S49935.
RefSeq	NP_012221.2.
3D structure databases
SMR	P38626. Positions 28-284.
ModBase	Search...
Protein-protein interaction databases
IntAct	P38626. 22 interactions.
STRING	P38626.
Proteomic databases
PeptideAtlas	P38626.
PRIDE	P38626.
Genome annotation databases
Ensembl	YIL043C; YIL043C; YIL043C; Saccharomyces cerevisiae. [Genome view]
GeneID	854768.
KEGG	sce:YIL043C.
NMPDR	fig\|4932.3.peg.1754.
Organism-specific databases
CYGD	YIL043c.
SGD	S000001305. CBR1.
Phylogenomic databases
eggNOG	fuNOG05226.
HOGENOM	HBG591994.
OrthoDB	EOG9KM0KS.
PhylomeDB	P38626.
Enzyme and pathway databases
BRENDA	1.6.2.2. 250.
Gene expression databases
ArrayExpress	P38626.
Genevestigator	P38626.
GermOnline	YIL043C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR001834. NADH-Cyt_B5_reductase. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD_bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Pfam	PF00970. FAD_binding_6. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00406. CYTB5RDTASE. PR00371. FPNCR.
PROSITE	PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	977526.

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Entry information

Entry name

NCB5R_YEAST

Accession

Primary (citable) accession number: P38626

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	April 29, 2008
Last modified:	January 19, 2010
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents