ID   DHNA_FERAY              Reviewed;         519 AA.
AC   P26829;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   02-SEP-2026, entry version 139.
DE   RecName: Full=NADH dehydrogenase;
DE            EC=7.1.1.2;
DE   AltName: Full=Alkyl hydroperoxide reductase;
GN   Name=ahpF; Synonyms=ndh;
OS   Ferdinandcohnia aciditolerans (strain JCM 32973 / CCTCC AB 2017280 / YN-1)
OS   (Bacillus aciditolerans).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Fredinandcohnia.
OX   NCBI_TaxID=72581;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1917890; DOI=10.1093/oxfordjournals.jbchem.a123440;
RA   Xu X., Koyama N., Cui M., Yamagishi A., Nosoh Y., Oshima T.;
RT   "Nucleotide sequence of the gene encoding NADH dehydrogenase from an
RT   alkalophile, Bacillus sp. strain YN-1.";
RL   J. Biochem. 109:678-683(1991).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2760020; DOI=10.1093/oxfordjournals.jbchem.a122715;
RA   Xu X., Kanaya S., Koyama N., Sekiguchi T., Nosoh Y., Ohashi S., Tsuda K.;
RT   "Tryptic digestion of NADH dehydrogenase from alkalophilic Bacillus.";
RL   J. Biochem. 105:626-632(1989).
CC   -!- FUNCTION: Transfer of electrons from NADH to the respiratory chain. The
CC       immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + NADH + 5 H(+)(in) = a ubiquinol + NAD(+) + 4
CC         H(+)(out); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC         COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; D10701; BAA01545.1; -; Genomic_DNA.
DR   AlphaFoldDB; P26829; -.
DR   SMR; P26829; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IEA:UniProtKB-ARBA.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0102039; F:NADH-dependent peroxiredoxin activity; IEA:InterPro.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:UniProtKB-ARBA.
DR   GO; GO:0000302; P:response to reactive oxygen species; IEA:InterPro.
DR   CDD; cd03026; AhpF_NTD_C; 1.
DR   CDD; cd02974; AhpF_NTD_N; 1.
DR   FunFam; 3.50.50.60:FF:000007; Alkyl hydroperoxide reductase, F subunit; 1.
DR   Gene3D; 3.40.30.80; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR044141; AhpF_NTD_C.
DR   InterPro; IPR044142; AhpF_NTD_N.
DR   InterPro; IPR012081; Alkyl_hydroperoxide_Rdtase_suF.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR050097; Ferredoxin-NADP_redctase_2.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR03140; AhpF; 1.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF13192; Thioredoxin_3; 1.
DR   PIRSF; PIRSF000238; AhpF; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 2.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Disulfide bond;
KW   Electron transport; FAD; Flavoprotein; Membrane; NAD; Oxidoreductase;
KW   Redox-active center; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..519
FT                   /note="NADH dehydrogenase"
FT                   /id="PRO_0000166788"
FT   REGION          1..?183
FT                   /note="Membrane-binding"
FT   REGION          ?184..519
FT                   /note="Catalytic"
FT   BINDING         210..241
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         349..379
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         469..479
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        337..340
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   519 AA;  55830 MW;  054FA461B5A156C2 CRC64;
     MVLEPQIKSQ LNQYLQLMEG DVLLKVSAGN DKVSEDMLSL VDELASMSSR ITVEKTNLER
     TPSFSVNRPG EDTGIVFAGI PLGHEFTSLV LALLQVSGRA PKAEQNVIDQ IKNIEGEYHF
     ESYISLSCQN CPDVVQALNL MSVLNPGISH TMIDGAAFKD EVESKDIMAV PTVYLNGESF
     TSGRMTVEEI LAQLGSGPDA SELADKDPFD VLVVGGGPAG ASSAIYAARK GIRTGIVADR
     FGGQIMDTLS IENFISQKYT EGPKLAASLE EHVKEYDIDV MKLQRAKRLE KKDLIEIELE
     NGAVLKSKSV ILSTGARWRN VGVPGEQEFK NKGVAYCPHC DGPLFEGKDV AVIGGGNSGV
     EAAIDLAGIV NHVTVLEFMP ELKADEVLQE RLNSLPNVTV IKNAQTKEIT GDDKVNGISY
     MDRDTEEVHH IELAGVFVQI GLVPNTDWLD GTLERNRFGE IVVDSHGATN VPGVFAAGDC
     TNSAYKQIII SMGSGATAAL GAFDYLIRNT TPAESAAAK
//