MCR1_CANAL
ID MCR1_CANAL Reviewed; 301 AA.
AC Q59M70; A0A1D8PPU2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=NADH-cytochrome b5 reductase 2;
DE EC=1.6.2.2;
DE AltName: Full=Mitochondrial cytochrome b reductase;
GN Name=MCR1; OrderedLocusNames=CAALFM_C602040WA;
GN ORFNames=CaO19.11001, CaO19.3507;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- FUNCTION: May mediate the reduction of outer membrane cytochrome b5.
CC {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: Mitochondrion outer membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000305}.
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DR EMBL; CP017628; AOW30140.1; -; Genomic_DNA.
DR RefSeq; XP_710845.1; XM_705753.1.
DR AlphaFoldDB; Q59M70; -.
DR SMR; Q59M70; -.
DR BioGRID; 1230654; 1.
DR STRING; 237561.Q59M70; -.
DR PRIDE; Q59M70; -.
DR GeneID; 3647561; -.
DR KEGG; cal:CAALFM_C602040WA; -.
DR CGD; CAL0000182452; MCR1.
DR VEuPathDB; FungiDB:C6_02040W_A; -.
DR eggNOG; KOG0534; Eukaryota.
DR HOGENOM; CLU_003827_9_1_1; -.
DR InParanoid; Q59M70; -.
DR OMA; NKHDHIA; -.
DR OrthoDB; 1311668at2759; -.
DR PRO; PR:Q59M70; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IEA:EnsemblFungi.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IBA:GO_Central.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:EnsemblFungi.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IBA:GO_Central.
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; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..301
FT /note="NADH-cytochrome b5 reductase 2"
FT /id="PRO_0000330176"
FT TRANSMEM 14..30
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"
SQ SEQUENCE 301 AA; 33460 MW; 7F16134D770DBDFB CRC64;
MLTHHLSKLA TPKFLVPFAG ATALSIGLAL QYSTSNNYIA NETGKTFTDS NEWVDLKLSK
SIDLTHNTKH LVFKLKDEND VSGLITASCL LTKFVTPKGN NVIRPYTPVS DVNQSGEIDF
VIKKYDGGKM SSHIFDLKEG ETLSFKGPIV KWKWEPNQFK SIALIGGGTG ITPLYQLLHQ
ITSNPKDNTK VNLIYGNLTP EDILLKKEID AIASKHKDQV KVHYFVDKAD EKKWEGQIGF
ITKEFLQKEL EKPGSDFKVF VCGPPGLYKA ISGPKVSPTD QGELTGALKD LGFEKEHVFK
F
