ID   MCR1_CANGA              Reviewed;         298 AA.
AC   Q6FUX5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   28-JAN-2026, entry version 114.
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=CAGL0E06424g;
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS
RC   138;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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         NAD(+) + H(+); 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; CR380951; CAG58888.1; -; Genomic_DNA.
DR   RefSeq; XP_445969.1; XM_445969.1.
DR   AlphaFoldDB; Q6FUX5; -.
DR   SMR; Q6FUX5; -.
DR   FunCoup; Q6FUX5; 359.
DR   STRING; 284593.Q6FUX5; -.
DR   EnsemblFungi; CAGL0E06424g-T; CAGL0E06424g-T-p1; CAGL0E06424g.
DR   GeneID; 2887376; -.
DR   KEGG; cgr:2887376; -.
DR   CGD; CAL0128682; CAGL0E06424g.
DR   VEuPathDB; FungiDB:B1J91_E06424g; -.
DR   VEuPathDB; FungiDB:CAGL0E06424g; -.
DR   eggNOG; KOG0534; Eukaryota.
DR   HOGENOM; CLU_003827_9_1_1; -.
DR   InParanoid; Q6FUX5; -.
DR   OMA; KGPEMQK; -.
DR   Proteomes; UP000002428; Chromosome E.
DR   GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0090524; F:cytochrome-b5 reductase activity, acting on NADH; IEA:UniProtKB-EC.
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; IEA:EnsemblFungi.
DR   CDD; cd06183; cyt_b5_reduct_like; 1.
DR   FunFam; 2.40.30.10:FF:000032; NADH-cytochrome b5 reductase; 1.
DR   FunFam; 3.40.50.80:FF:000009; NADH-cytochrome b5 reductase; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 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; NADH-CYTOCHROME B5 REDUCTASE; 1.
DR   PANTHER; PTHR19370:SF171; NADH-CYTOCHROME B5 REDUCTASE 2; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 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..298
FT                   /note="NADH-cytochrome b5 reductase 2"
FT                   /id="PRO_0000330177"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          48..152
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         155..190
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   298 AA;  33610 MW;  76B38A123EEB1C7A CRC64;
     MAFARFARPT QRFLPFAIGA VAVTAGALYL NGWNTIKNEN PKVFIGDRKW IDLELEKIIE
     ESHDTKRFFF KLPTDDSVSG LTLASAVLTK FMTPKGNPVI RPYTPVSDLS EKGYIEFVIK
     HYEGGKMTDH LFQLKPKDTL AFQGPIPKWQ WKPNSFDTIT LLGGGTGITP LYQLVHHITQ
     NKEDKTKINL FYGSKTPSDI LLKKELDDLQ KKYPEQLNIQ YFVDKDDTGK FDGNKGFITK
     DFLAKNAPGP KEKTQVFVCG PPPFMDSLSG QKKSPMEQGD LTGALKDLGY SQDQVFKF
//