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A6ZZH2 (MCR1_YEAS7) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
NADH-cytochrome b5 reductase 2

EC=1.6.2.2
Alternative name(s):
Mitochondrial cytochrome b reductase
p34/p32
Gene names
Name:MCR1
ORF Names:SCY_3232
OrganismSaccharomyces cerevisiae (strain YJM789) (Baker's yeast) [Complete proteome]
Taxonomic identifier307796 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

The outer membrane form may mediate the reduction of outer membrane cytochrome b5, and the soluble inter-membrane space form may transfer electrons from external NADH to cytochrome c, thereby mediating an antimycin-insensitive, energy-coupled oxidation of external NADH by yeast mitochondria. Involved in the reduction of D-erythroascorbyl free radicals By similarity.

Catalytic activity

NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5.

Cofactor

FAD By similarity.

Subcellular location

NADH-cytochrome b5 reductase p32 form: Mitochondrion intermembrane space By similarity.

NADH-cytochrome b5 reductase p34 form: Mitochondrion outer membrane; Single-pass membrane protein By similarity.

Induction

By osmotic stress By similarity.

Post-translational modification

There are two isoforms of NADH-cytochrome b5 reductase, a 34 kDa form (p34) and a 32 kDa form (p32). The p34 form becomes firmly anchored to the outer mitochondrial membrane after an incomplete translocation arrest. The p32 form is formed after translocation of the p34 precursor to the inner mitochondrial membrane, where it is processed by mitochondrial inner membrane peptidase (IMP) complex and released to the intermembrane space By similarity.

Sequence similarities

Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.

Contains 1 FAD-binding FR-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 302302NADH-cytochrome b5 reductase p34 form
PRO_0000330195
Propeptide1 – 4141Removed in mature form By similarity
PRO_0000330196
Chain42 – 302261NADH-cytochrome b5 reductase p32 form
PRO_0000330197

Regions

Transmembrane12 – 3221Helical; Potential
Domain51 – 155105FAD-binding FR-type
Nucleotide binding158 – 19336FAD By similarity

Sites

Site41 – 422Cleavage; by IMP1 By similarity

Amino acid modifications

Modified residue2781Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6ZZH2 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: D3D68BF56E8C433B

FASTA30234,108
        10         20         30         40         50         60 
MFSRLSRSHS KALPIALGTV AIAAATAFYF ANRNQHSFVF NESNKVFKGD DKWIDLPISK 

        70         80         90        100        110        120 
IEEESHDTRR FTFKLPTEDS EMGLVLASAL FAKFVTPKGS NVVRPYTPVS DLSQKGHFQL 

       130        140        150        160        170        180 
VVKHYEGGKM TSHLFGLKPN DTVSFKGPIM KWKWQPNQFK SITLLGAGTG INPLYQLAHH 

       190        200        210        220        230        240 
IVENPNDKTK VNLLYGNKTP QDILLRKELD ALKEKYPDKF NVTYFVDDKQ DDQDFDGEIG 

       250        260        270        280        290        300 
FISKDFIQEH VPGPKESTHL FVCGPPPFMN AYSGEKKSPK DQGELIGILN NLGYSKDQVF 


KF 

« Hide

References

[1]"Genome sequencing and comparative analysis of Saccharomyces cerevisiae strain YJM789."
Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z., Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X., Jia P., Luedi P., Oefner P.J., David L. expand/collapse author list , Dietrich F.S., Li Y., Davis R.W., Steinmetz L.M.
Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007) [PubMed: 17652520] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YJM789.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAFW02000151 Genomic DNA. Translation: EDN60020.1.

3D structure databases

ProteinModelPortalA6ZZH2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR017927. 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]
PfamPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00406. CYTB5RDTASE.
PR00371. FPNCR.
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMCR1_YEAS7
AccessionPrimary (citable) accession number: A6ZZH2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: September 11, 2007
Last modified: September 21, 2011
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families