Reviewed, UniProtKB/Swiss-Prot A6ZZH2 (MCR1_YEAS7)

Names and origin

Protein names

Recommended name:
    NADH-cytochrome b5 reductase 2
    EC=1.6.2.2
Alternative name(s):
    Mitochondrial cytochrome b reductase
    p34/p32
Cleaved into the following 2 chains:
    1- Recommended name:
            NADH-cytochrome b5 reductase p34 form
    2- Recommended name:
            NADH-cytochrome b5 reductase p32 form

Gene names

Name:	MCR1
ORF Names:	SCY_3232

Organism

Saccharomyces cerevisiae (strain YJM789) (Baker's yeast) [Complete proteome]

Taxonomic identifier

307796 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cytochrome-b5 reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 302	302	NADH-cytochrome b5 reductase p34 form		PRO_0000330195
	Propeptide	1 – 41	41	Removed in mature form By similarity		PRO_0000330196
	Chain	42 – 302	261	NADH-cytochrome b5 reductase p32 form		PRO_0000330197
Regions
	Transmembrane	12 – 32	21	Potential
	Domain	51 – 155	105	FAD-binding FR-type
	Nucleotide binding	158 – 193	36	FAD By similarity
Sites
	Site	41 – 42	2	Cleavage; by IMP1 By similarity
Amino acid modifications
	Modified residue	278	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6ZZH2-1 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: D3D68BF56E8C433B	FASTA	302	34,108
	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

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. , 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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFW02000151 Genomic DNA. Translation: EDN60020.1.
3D structure databases
SMR	A6ZZH2. Positions 50-302.
ModBase	Search...
Phylogenomic databases
OrthoDB	EOG9TB5TC.
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...

Entry information

Entry name

MCR1_YEAS7

Accession

Primary (citable) accession number: A6ZZH2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	September 11, 2007
Last modified:	January 19, 2010
This is version 20 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)