NCB5R_ASPOR
ID NCB5R_ASPOR Reviewed; 292 AA.
AC Q2UFN3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 91.
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=AO090026000138;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE59632.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP007159; BAE59632.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001821634.2; XM_001821582.2.
DR AlphaFoldDB; Q2UFN3; -.
DR SMR; Q2UFN3; -.
DR STRING; 510516.Q2UFN3; -.
DR VEuPathDB; FungiDB:AO090026000138; -.
DR OMA; QAQHPNR; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000006564; Chromosome 3.
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..292
FT /note="NADH-cytochrome b5 reductase 1"
FT /id="PRO_0000330146"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 43..148
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 128..143
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 154..191
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 292 AA; 31925 MW; 15E3E5EA7D7E8A3D CRC64;
MSAFASENLT SALLVVGTAI FAVLVGAKFL GGSGKPRKVL NPTEFQNFVL KEKNEISHNV
AIYRFALPRP TDILGLPIGQ HISLAATIEG QPKEVVRSYT PISSDNEAGY FDLLVKAYPQ
GNISKYLTTL KIGDNMKVRG PKGAMVYTPN MCRHIGMIAG GTGITPMLQI IKAIIRNRPR
NGGNDTTQVD LIFANVNPED ILLKEELEQL VKEDDGFRVY YVLNNPPEGW TGGVGFVTPD
MIKERLPAPA QDIKIMLCGP PPMISAMKKA TESLGYTKAR PVSKLEDQVF CF
