ID   MCR1_PHANO              Reviewed;         336 AA.
AC   Q0U9W5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=SNOG_11449;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(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; CH445343; EAT81157.1; -; Genomic_DNA.
DR   RefSeq; XP_001801691.1; XM_001801639.1.
DR   AlphaFoldDB; Q0U9W5; -.
DR   SMR; Q0U9W5; -.
DR   STRING; 13684.SNOT_11449; -.
DR   PRIDE; Q0U9W5; -.
DR   EnsemblFungi; SNOT_11449; SNOT_11449; SNOG_11449.
DR   GeneID; 5978599; -.
DR   KEGG; pno:SNOG_11449; -.
DR   eggNOG; KOG0534; Eukaryota.
DR   HOGENOM; CLU_003827_9_1_1; -.
DR   InParanoid; Q0U9W5; -.
DR   OMA; NKHDHIA; -.
DR   OrthoDB; 1311668at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
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   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..336
FT                   /note="NADH-cytochrome b5 reductase 2"
FT                   /id="PRO_0000330187"
FT   TRANSMEM        28..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          84..189
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         192..227
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   336 AA;  37024 MW;  D6BDA6CF8E11601B CRC64;
     MFARQVIRPA RQLQQHVRRY ASEAPQSGGS SNGALYVGIG AAGLAGAYIY MRGGKPAAPL
     SEEANKVAAK VGGASKKAFT GGDQGFISLL LDKSEVVNHN TKKLTFKLPE PDMESGLPVT
     SAVITKYKGP EMEKPVIRPY TPVSDVDQQG TVDFIVKKYE KGPMSSHMHN MEPGQRLDIK
     GPIPKYPWSP NKHEHIALIA GGTGITPMWQ TARAIFKNPE DKTKVTLVFG NISEEDILLK
     KEWEHLENTY PQRFRAFYVL DNPPESWQGG KGFITKELLK TVLPEPKEGE KVKIFVCGPP
     GMYKAISGGK KSPSDQGELD GYLKELGYSK DQVYKF