ID   DHNA_BACSU              Reviewed;         509 AA.
AC   P42974;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   02-SEP-2026, entry version 176.
DE   RecName: Full=NADH dehydrogenase;
DE            EC=7.1.1.2;
DE   AltName: Full=Alkyl hydroperoxide reductase;
GN   Name=ahpF; Synonyms=ndh; OrderedLocusNames=BSU40100;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9205843; DOI=10.1093/dnares/4.2.155;
RA   Kasahara Y., Nakai S., Ogasawara N.;
RT   "Sequence analysis of the 36-kb region between gntZ and trnY genes of
RT   Bacillus subtilis genome.";
RL   DNA Res. 4:155-159(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-509.
RC   STRAIN=168 / JH642;
RX   PubMed=8125345; DOI=10.1016/0378-1119(94)90735-8;
RA   Zhang J., Aronson A.I.;
RT   "A Bacillus subtilis bglA gene encoding phospho-beta-glucosidase is
RT   inducible and closely linked to a NADH dehydrogenase-encoding gene.";
RL   Gene 140:85-90(1994).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-29.
RC   STRAIN=168 / YB886 / BG214;
RX   PubMed=8180695; DOI=10.1099/13500872-140-2-297;
RA   Hartford O.M., Dowds B.C.A.;
RT   "Isolation and characterization of a hydrogen peroxide resistant mutant of
RT   Bacillus subtilis.";
RL   Microbiology 140:297-304(1994).
CC   -!- FUNCTION: Transfer of electrons from NADH to the respiratory chain. The
CC       immediate electron acceptor for the enzyme is believed to be ubiquinone
CC       (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; D78193; BAA11269.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB16047.1; -; Genomic_DNA.
DR   EMBL; L19710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; G69583; G69583.
DR   RefSeq; NP_391890.1; NC_000964.3.
DR   RefSeq; WP_003243077.1; NC_000964.3.
DR   AlphaFoldDB; P42974; -.
DR   SMR; P42974; -.
DR   FunCoup; P42974; 17.
DR   IntAct; P42974; 1.
DR   MINT; P42974; -.
DR   STRING; 224308.BSU40100; -.
DR   TCDB; 5.B.17.1.1; the soluble nadh dehydrogenase (sndh) family.
DR   jPOST; P42974; -.
DR   PaxDb; 224308-BSU40100; -.
DR   EnsemblBacteria; CAB16047; CAB16047; BSU_40100.
DR   GeneID; 937717; -.
DR   KEGG; bsu:BSU40100; -.
DR   PATRIC; fig|224308.179.peg.4337; -.
DR   eggNOG; COG3634; Bacteria.
DR   InParanoid; P42974; -.
DR   OrthoDB; 9806179at2; -.
DR   PhylomeDB; P42974; -.
DR   BioCyc; BSUB:BSU40100-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P42974; -.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; Reference proteome; Translocase; Transport;
KW   Ubiquinone.
FT   CHAIN           1..509
FT                   /note="NADH dehydrogenase"
FT                   /id="PRO_0000166789"
FT   REGION          1..?183
FT                   /note="Membrane-binding"
FT   REGION          ?184..509
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"
FT   CONFLICT        29
FT                   /note="G -> E (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        227
FT                   /note="T -> D (in Ref. 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        393
FT                   /note="Y -> I (in Ref. 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   509 AA;  54874 MW;  487FFF089CA3A079 CRC64;
     MVLDANIKAQ LNQYMQLIEN DIVLKVSAGE DDTSKDMLAL VDELASMSSK ISVEKAELNR
     TPSFSVNRVG EDTGVTFAGI PLGHEFTSLV LALLQVSGRP PKVDQKVIDQ VKKISGEYHF
     ESYISLTCHN CPDVVQALNM MSVLNPNITH TMIDGAAYKA EVESKNIMAV PTVYLNGESF
     GSGRMTLEEI LAKMGSGTDA SEFADKEPFD VLVVGGGPAG ASAAIYTARK GIRTGVVAER
     FGGQVLDTMS IENFISVKAT EGPKLAASLE EHVKEYDIDV MNLQRAKRLE KKDLFELELE
     NGAVLKSKTV ILSTGARWRN VNVPGEQEFK NKGVAYCPHC DGPLFEGKDV AVIGGGNSGI
     EAAIDLAGIV NHVTVLEFAP ELKADEVLQK RLYSLPNVTV VKNAQTKEIT GDQSVNGITY
     VDRETGEEKH VELQGVFVQI GLVPNTEWLE GTVERNRMGE IIVDKHGATS VPGLFAAGDC
     TDSAYNQIII SMGSGATAAL GAFDYLIRN
//