DHNA_BACSU
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 03-AUG-2022, entry version 161.
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; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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 + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC NAD(+); 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; NZ_JNCM01000034.1.
DR AlphaFoldDB; P42974; -.
DR SMR; P42974; -.
DR IntAct; P42974; 1.
DR MINT; P42974; -.
DR STRING; 224308.BSU40100; -.
DR jPOST; P42974; -.
DR PaxDb; P42974; -.
DR PRIDE; P42974; -.
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 OMA; VTVFEFM; -.
DR PhylomeDB; P42974; -.
DR BioCyc; BSUB:BSU40100-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008785; F:alkyl hydroperoxide reductase activity; IEA:InterPro.
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:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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 Gene3D; 3.50.50.60; -; 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; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF13192; Thioredoxin_3; 1.
DR PIRSF; PIRSF000238; AhpF; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF52833; SSF52833; 2.
DR TIGRFAMs; TIGR03140; AhpF; 1.
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
