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   25-NOV-2008, entry version 78.
DE   RecName: Full=NADH dehydrogenase;
DE            EC=1.6.99.3;
DE   AltName: Full=Alkyl hydroperoxide reductase;
GN   Name=ahpF; Synonyms=ndh; OrderedLocusNames=BSU40100;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Kasahara Y., Nakai S., Yoshikawa H., Ogasawara N.;
RT   "36kb sequence between gntZ and trnY of B. subtilis genome.";
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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   MEDLINE=94171085; 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;
RX   MEDLINE=94236234; PubMed=8180695;
RA   Hartford O.M., Dowds B.C.A.;
RT   "Isolation and characterization of a hydrogen peroxide resistant
RT   mutant of Bacillus subtilis.";
RL   Microbiology 140:297-304(1994).
CC   -!- FUNCTION: Transfer of electrons from NADH to the respiratory
CC       chain. The immediate electron acceptor for the enzyme is believed
CC       to be ubiquinone (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; D78193; BAA11269.1; -; Genomic_DNA.
DR   EMBL; Z99124; CAB16047.1; -; Genomic_DNA.
DR   EMBL; L19710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; G69583; G69583.
DR   RefSeq; NP_391890.1; -.
DR   HSSP; P35340; 1FL2.
DR   GeneID; 937717; -.
DR   GenomeReviews; AL009126_GR; BSU40100.
DR   KEGG; bsu:BSU40100; -.
DR   NMPDR; fig|224308.1.peg.4016; -.
DR   SubtiList; BG11204; ahpF.
DR   HOGENOM; P42974; -.
DR   BioCyc; BSUB224308:BSU4007-MON; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IEA:EC.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000759; Adrndx_reductase.
DR   InterPro; IPR012081; Alkyl_hydroperoxide_Rdtase_suF.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 2.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PIRSF; PIRSF000238; AhpF; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
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; Complete proteome; Direct protein sequencing;
KW   Electron transport; FAD; Flavoprotein; Membrane; NAD; Oxidoreductase;
KW   Redox-active center; Transport; Ubiquinone.
FT   CHAIN         1    509       NADH dehydrogenase.
FT                                /FTId=PRO_0000166789.
FT   NP_BIND     210    241       FAD (By similarity).
FT   NP_BIND     349    379       NAD (By similarity).
FT   NP_BIND     469    479       FAD (By similarity).
FT   REGION        1   ?183       Membrane-binding.
FT   REGION     ?184    509       Catalytic.
FT   DISULFID    337    340       Redox-active (By similarity).
FT   CONFLICT     29     29       G -> E (in Ref. 4; AA sequence).
FT   CONFLICT    227    227       T -> D (in Ref. 3).
FT   CONFLICT    393    393       Y -> I (in Ref. 3).
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
//