NCB5R_MAGO7
ID NCB5R_MAGO7 Reviewed; 309 AA.
AC A4R935; G4N878;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=NADH-cytochrome b5 reductase 1;
DE EC=1.6.2.2 {ECO:0000250|UniProtKB:P38626};
DE AltName: Full=Microsomal cytochrome b reductase;
GN Name=CBR1; ORFNames=MGG_06289;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
CC -!- FUNCTION: NADH-dependent reductase for DPH3 and cytochrome b5. Required
CC for the first step of diphthamide biosynthesis, a post-translational
CC modification of histidine which occurs in elongation factor 2. DPH1 and
CC DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-
CC methionine (SAM) to a histidine residue, the reaction is assisted by a
CC reduction system comprising DPH3 and a NADH-dependent reductase,
CC predominantly CBR1. By reducing DPH3, also involved in the formation of
CC the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-
CC thiouridine), mediated by the elongator complex. The cytochrome b5/NADH
CC cytochrome b5 reductase electron transfer system supports the catalytic
CC activity of several sterol biosynthetic enzymes.
CC {ECO:0000250|UniProtKB:P38626}.
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:0000250|UniProtKB:P38626};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(3+)-[Dph3] + NADH = 2 Fe(2+)-[Dph3] + H(+) + NAD(+);
CC Xref=Rhea:RHEA:71231, Rhea:RHEA-COMP:18002, Rhea:RHEA-COMP:18003,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83228;
CC Evidence={ECO:0000250|UniProtKB:P38626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71232;
CC Evidence={ECO:0000250|UniProtKB:P38626};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC {ECO:0000250|UniProtKB:P38626}.
CC -!- SUBUNIT: Monomer. Component of the 2-(3-amino-3-carboxypropyl)histidine
CC synthase complex composed of DPH1, DPH2, DPH3 and a NADH-dependent
CC reductase, predominantly CBR1. {ECO:0000250|UniProtKB:P38626}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P38626}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000305}.
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DR EMBL; CM001234; EHA50979.1; -; Genomic_DNA.
DR RefSeq; XP_003717298.1; XM_003717250.1.
DR AlphaFoldDB; A4R935; -.
DR SMR; A4R935; -.
DR STRING; 318829.MGG_06289T0; -.
DR EnsemblFungi; MGG_06289T0; MGG_06289T0; MGG_06289.
DR GeneID; 2684444; -.
DR KEGG; mgr:MGG_06289; -.
DR VEuPathDB; FungiDB:MGG_06289; -.
DR eggNOG; KOG0534; Eukaryota.
DR HOGENOM; CLU_003827_9_0_1; -.
DR InParanoid; A4R935; -.
DR OMA; HFMANID; -.
DR OrthoDB; 1311668at2759; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000009058; Chromosome 4.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:0003954; F:NADH dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISS:UniProtKB.
DR GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; ISS:UniProtKB.
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; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..309
FT /note="NADH-cytochrome b5 reductase 1"
FT /id="PRO_0000330157"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 60..168
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 148..163
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 174..208
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 309 AA; 33630 MW; DB354E0C02610802 CRC64;
MAPPLSSKVY VDGVYIPAAL IVIGTAIVKR DWVVYSVALA LALGTWKFFQ LKPKKVLDPT
KFQEFELKEK TIISHNVAIY RIQLPSPSSI LGLPIGQHIS IGADIPQPDG SSKEVVRSYT
PISGDEQPGY VDLLIKSYPT GNISKYMAGL SVGQSIRVRG PKGAFVYQPN MVRHFGMIAG
GTGITPMLQV VRAIVRGRAA GDTTQVDLIF ANVTKEDILL KEDLDALAAE DKGFRVHYVL
DRPPEGWTGG VGFVTQDMIT KWLPKPADDV KILLCGPPPM VSGLKKATEA LGFKKARPVS
KLEDQVFAF
