ID   MCR1_ASPNC              Reviewed;         322 AA.
AC   A2Q898;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=NADH-cytochrome b5 reductase 2;
DE            EC=1.6.2.2;
DE   AltName: Full=Mitochondrial cytochrome b reductase;
GN   Name=mcr1; ORFNames=An01g03570;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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; AM269959; CAK36895.1; -; Genomic_DNA.
DR   RefSeq; XP_001388787.1; XM_001388750.2.
DR   AlphaFoldDB; A2Q898; -.
DR   SMR; A2Q898; -.
DR   PaxDb; A2Q898; -.
DR   EnsemblFungi; CAK36895; CAK36895; An01g03570.
DR   GeneID; 4978482; -.
DR   KEGG; ang:ANI_1_468014; -.
DR   VEuPathDB; FungiDB:An01g03570; -.
DR   HOGENOM; CLU_003827_9_1_1; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..322
FT                   /note="NADH-cytochrome b5 reductase 2"
FT                   /id="PRO_0000330172"
FT   TRANSMEM        31..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          72..176
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         179..214
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   322 AA;  36090 MW;  831FC260D3A417AE CRC64;
     MFARQAFRCA QPLKQGFRKY STEAPKGKSS LAPIYAAVGI TGVGVGLYRY NSATAEAPAA
     VDRPKVFKGG DQGWFDLKLS EIEVLNHNTK RLRFEFEDKE ALSGLQVASA LLTKFKPADA
     KAVIRPYTPT SDEETPGYID LVVKVYPNGP MSEHLHSMNV GQRLDFKGPI VKYPWETNKH
     NHICLIAGGT GITPMYQLAR EIFKNPEDQT KVTLVFGNVK EEDILLKKEF EELENTYPRR
     FRAFYVLDNP PKEWTGGKGY ISKELLKTVL PEPKEENIKI FVCGPPGMYK AISGTKNSPT
     DQGELSGILK ELGYSKEQVF KF