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Database: UniProt
Entry: NCB5R_ASPNC
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Original site: NCB5R_ASPNC 
ID   NCB5R_ASPNC             Reviewed;         305 AA.
AC   A2QCV4;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   08-NOV-2023, entry version 89.
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=An02g04860;
OS   Aspergillus niger (strain ATCC MYA-4892 / 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=ATCC MYA-4892 / CBS 513.88 / FGSC A1513;
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: 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; AM270009; CAK47663.1; -; Genomic_DNA.
DR   RefSeq; XP_001399624.1; XM_001399587.2.
DR   AlphaFoldDB; A2QCV4; -.
DR   SMR; A2QCV4; -.
DR   EnsemblFungi; CAK47663; CAK47663; An02g04860.
DR   GeneID; 4978975; -.
DR   KEGG; ang:ANI_1_682024; -.
DR   VEuPathDB; FungiDB:An02g04860; -.
DR   HOGENOM; CLU_003827_9_0_1; -.
DR   OrthoDB; 979728at2759; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000006706; Chromosome 4R.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017183; P:protein histidyl modification to diphthamide; ISS:UniProtKB.
DR   GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; ISS:UniProtKB.
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:SF184; 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; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   NAD; Oxidoreductase; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..305
FT                   /note="NADH-cytochrome b5 reductase 1"
FT                   /id="PRO_5000219577"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          58..161
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         141..156
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         167..204
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   305 AA;  33480 MW;  A09CB317DE80134E CRC64;
     MSAFSPENIT GAFIPSALFV AGTFFFKQEL TPFAVALAAV LVGWKVFSNK PRKVLNPGDF
     QHFTLKEKND ISHNVTVYRF ALPRPTDILG LPIGQHISLA ATIGGKEVVR SYTPISSDNE
     AGYFDLLVKA YPQGNISKYL TTLEVGQTMK VRGPKGAMVY TPNMCRHIGM IAGGTGITPM
     YQIIKAIIRN RPRNGGNDTT QVDLIFANVN PDDILMKDEL EQLAKEDDGF RIYYVLNNPP
     EGWTGGVGFV TPDMIKERLP APSSDIKVLL CGPPPMVSAM KKATESLGYT KARPVSKLED
     QVFCF
//
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