ID   DHNA_BACYN              Reviewed;         519 AA.
AC   P26829;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-NOV-2008, entry version 75.
DE   RecName: Full=NADH dehydrogenase;
DE            EC=1.6.99.3;
DE   AltName: Full=Alkyl hydroperoxide reductase;
GN   Name=ahpF; Synonyms=ndh;
OS   Bacillus sp. (strain YN-1).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=72581;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92011449; PubMed=1917890;
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   MEDLINE=89340392; PubMed=2760020;
RA   Xu X., Kanaya S., Koyama N., Sekiguchi T., Nosoh Y., Ohashi S.,
RA   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
CC       chain. The immediate electron acceptor for the enzyme is believed
CC       to be ubiquinone.
CC   -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; D10701; BAA01545.1; -; Genomic_DNA.
DR   HSSP; P35340; 1FL2.
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; Direct protein sequencing; Electron transport; FAD;
KW   Flavoprotein; Membrane; NAD; Oxidoreductase; Redox-active center;
KW   Transport; Ubiquinone.
FT   CHAIN         1    519       NADH dehydrogenase.
FT                                /FTId=PRO_0000166788.
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    519       Catalytic.
FT   DISULFID    337    340       Redox-active (By similarity).
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
//