ID A0A0B1P5E7_UNCNE Unreviewed; 324 AA.
AC A0A0B1P5E7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=NADH-cytochrome b5 reductase {ECO:0000256|RuleBase:RU361226};
DE EC=1.6.2.2 {ECO:0000256|RuleBase:RU361226};
GN ORFNames=EV44_g2954 {ECO:0000313|EMBL:KHJ32156.1};
OS Uncinula necator (Grape powdery mildew).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=52586 {ECO:0000313|EMBL:KHJ32156.1, ECO:0000313|Proteomes:UP000030854};
RN [1] {ECO:0000313|EMBL:KHJ32156.1, ECO:0000313|Proteomes:UP000030854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=c {ECO:0000313|Proteomes:UP000030854};
RX PubMed=25487071;
RA Jones L., Riaz S., Morales-Cruz A., Amrine K.C., McGuire B., Gubler W.D.,
RA Walker M.A., Cantu D.;
RT "Adaptive genomic structural variation in the grape powdery mildew
RT pathogen, Erysiphe necator.";
RL BMC Genomics 15:1081-1081(2014).
CC -!- FUNCTION: May mediate the reduction of outer membrane cytochrome b5.
CC {ECO:0000256|ARBA:ARBA00037464}.
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 Evidence={ECO:0000256|ARBA:ARBA00029341,
CC ECO:0000256|RuleBase:RU361226};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR601834-1, ECO:0000256|RuleBase:RU361226};
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004572}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004572}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000256|ARBA:ARBA00006105,
CC ECO:0000256|RuleBase:RU361226}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHJ32156.1}.
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DR EMBL; JNVN01002283; KHJ32156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B1P5E7; -.
DR STRING; 52586.A0A0B1P5E7; -.
DR HOGENOM; CLU_003827_9_1_1; -.
DR OMA; KGPEMQK; -.
DR OrthoDB; 979728at2759; -.
DR Proteomes; UP000030854; Unassembled WGS sequence.
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 CDD; cd06183; cyt_b5_reduct_like; 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-LIKE; 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 {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR601834-1};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR601834-
KW 1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00022787};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU361226};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361226};
KW Reference proteome {ECO:0000313|Proteomes:UP000030854}.
FT DOMAIN 72..177
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 126
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT BINDING 127
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT BINDING 128
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT BINDING 143
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT BINDING 145
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT BINDING 152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT BINDING 153
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
SQ SEQUENCE 324 AA; 36511 MW; 024E0327AC69547B CRC64;
MFRRQAFHGL RAFKSETRLY GTNSISNKSK LGSRAVTLVG SLAVLGGVTY WYWPEAVDTV
IAKKPNPAFT NQGYFDLKLD SVETINHNTK KFRFALPEKE QVSGLETASC LLTRYKGPDM
EKAVIRPYTP TSDEDEIGYL DLLVKKYPTG IMSSHFHEMM PGQTLEFKGP IVKYPWTANK
HNHIALIAGG TGIAPMYQLI RAIFKNPTDN TKVTLVFGNV TEEDILLRKE LQELENTYPQ
RFRAFYVLDN PPKSWSGEKG YISKHLLKTV LPEPKEENIK IFVCGPPPMY KAISGAKISA
SDQGELDGSI LEQLGYSKDQ VFKF
//
