(data stored in ACNUC7421 zone)

SWISSPROT: MCR1_ASHGO

ID   MCR1_ASHGO              Reviewed;         306 AA.
AC   Q75C62;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 94.
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=ACR054C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(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}.
DR   EMBL; AE016816; AAS51281.1; -; Genomic_DNA.
DR   RefSeq; NP_983457.1; NM_208810.1.
DR   SMR; Q75C62; -.
DR   STRING; 33169.AAS51281; -.
DR   EnsemblFungi; AAS51281; AAS51281; AGOS_ACR054C.
DR   GeneID; 4619582; -.
DR   KEGG; ago:AGOS_ACR054C; -.
DR   HOGENOM; HOG000175005; -.
DR   InParanoid; Q75C62; -.
DR   KO; K00326; -.
DR   OMA; KHDHIAL; -.
DR   Proteomes; UP000000591; Chromosome III.
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; IBA:GO_Central.
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   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
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;
DR   PRODOM; Q75C62.
DR   SWISS-2DPAGE; Q75C62.
KW   FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   NAD; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..306
FT                   /note="NADH-cytochrome b5 reductase 2"
FT                   /id="PRO_0000330169"
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          57..161
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   NP_BIND         164..199
FT                   /note="FAD"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   306 AA;  33771 MW;  AB7BECE740609D43 CRC64;
     MLSRITRSSK ALNFALGTTA VAAAGYLYAQ SRGNLSTSLN KGDVTGQAAA QTFTGDGQWH
     ALKIAKIEQV SHDTRRFTFA LPSQDHVTGL TTASALLAKY VTPKGSNVIR PYTPVSDNMA
     RGMFQLVIKH YDGGKFTTHL FGLKENDTVE FKGPIQKWRW DPNMFDSIVL MGAGTGITPL
     FQMMHHIAEN PTDNTKVHLL YGNKTPQDIL LRKELEELAS KYPDQVKVTY FVDKPEGDYK
     GEKGFITKDF LKQNLPTPGS NSHIFVCGPP PFMDAFSGNK VSPSDQGQVT GVLSELGYTK
     DHVYKF
//

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