MCR1_YEAS7
ID MCR1_YEAS7 Reviewed; 302 AA.
AC A6ZZH2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=NADH-cytochrome b5 reductase 2;
DE EC=1.6.2.2;
DE AltName: Full=Mitochondrial cytochrome b reductase;
DE AltName: Full=p34/p32;
DE Contains:
DE RecName: Full=NADH-cytochrome b5 reductase p34 form;
DE Contains:
DE RecName: Full=NADH-cytochrome b5 reductase p32 form;
DE Flags: Precursor;
GN Name=MCR1; ORFNames=SCY_3232;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: The outer membrane form may mediate the reduction of outer
CC membrane cytochrome b5, and the soluble inter-membrane space form may
CC transfer electrons from external NADH to cytochrome c, thereby
CC mediating an antimycin-insensitive, energy-coupled oxidation of
CC external NADH by yeast mitochondria. Involved in the reduction of D-
CC erythroascorbyl free radicals (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] +
CC H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.2;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: [NADH-cytochrome b5 reductase p32 form]:
CC Mitochondrion intermembrane space {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [NADH-cytochrome b5 reductase p34 form]:
CC Mitochondrion outer membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- INDUCTION: By osmotic stress. {ECO:0000250}.
CC -!- PTM: There are two isoforms of NADH-cytochrome b5 reductase, a 34 kDa
CC form (p34) and a 32 kDa form (p32). The p34 form becomes firmly
CC anchored to the outer mitochondrial membrane after an incomplete
CC translocation arrest. The p32 form is formed after translocation of the
CC p34 precursor to the inner mitochondrial membrane, where it is
CC processed by mitochondrial inner membrane peptidase (IMP) complex and
CC released to the intermembrane space (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000305}.
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DR EMBL; AAFW02000151; EDN60020.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZZH2; -.
DR SMR; A6ZZH2; -.
DR PRIDE; A6ZZH2; -.
DR TopDownProteomics; A6ZZH2; -.
DR EnsemblFungi; EDN60020; EDN60020; SCY_3232.
DR HOGENOM; CLU_003827_9_1_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR001834; CBR-like.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370; PTHR19370; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW NAD; Oxidoreductase; Phosphoprotein; Transmembrane; Transmembrane helix.
FT CHAIN 1..302
FT /note="NADH-cytochrome b5 reductase p34 form"
FT /id="PRO_0000330195"
FT PROPEP 1..41
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000330196"
FT CHAIN 42..302
FT /note="NADH-cytochrome b5 reductase p32 form"
FT /id="PRO_0000330197"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 51..155
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 158..193
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT SITE 41..42
FT /note="Cleavage; by IMP1"
FT /evidence="ECO:0000250"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36060"
SQ SEQUENCE 302 AA; 34108 MW; D3D68BF56E8C433B CRC64;
MFSRLSRSHS KALPIALGTV AIAAATAFYF ANRNQHSFVF NESNKVFKGD DKWIDLPISK
IEEESHDTRR FTFKLPTEDS EMGLVLASAL FAKFVTPKGS NVVRPYTPVS DLSQKGHFQL
VVKHYEGGKM TSHLFGLKPN DTVSFKGPIM KWKWQPNQFK SITLLGAGTG INPLYQLAHH
IVENPNDKTK VNLLYGNKTP QDILLRKELD ALKEKYPDKF NVTYFVDDKQ DDQDFDGEIG
FISKDFIQEH VPGPKESTHL FVCGPPPFMN AYSGEKKSPK DQGELIGILN NLGYSKDQVF
KF
