ID   DHNA_HAEIN              Reviewed;         444 AA.
AC   P44856;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-NOV-2008, entry version 61.
DE   RecName: Full=NADH dehydrogenase;
DE            EC=1.6.99.3;
GN   Name=ndh; OrderedLocusNames=HI0747;
OS   Haemophilus influenzae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=727;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   MEDLINE=95350630; PubMed=7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
RA   Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA   Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA   Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA   Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA   Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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. Does not couple the redox reaction to proton
CC       translocation (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane (By similarity).
CC   -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
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DR   EMBL; L42023; AAC22405.1; -; Genomic_DNA.
DR   PIR; C64090; C64090.
DR   RefSeq; NP_438906.1; -.
DR   GeneID; 949772; -.
DR   GenomeReviews; L42023_GR; HI0747.
DR   KEGG; hin:HI0747; -.
DR   TIGR; HI0747; -.
DR   HOGENOM; P44856; -.
DR   BioCyc; HINF71421:HI_0747-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:0003954; F:NADH dehydrogenase activity; IEA:EC.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   Pfam; PF00070; Pyr_redox; 2.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Electron transport; FAD;
KW   Flavoprotein; Membrane; NAD; Oxidoreductase; Transport; Ubiquinone.
FT   CHAIN         1    444       NADH dehydrogenase.
FT                                /FTId=PRO_0000079891.
FT   NP_BIND       3     38       FAD (By similarity).
FT   NP_BIND     181    218       NAD (By similarity).
SQ   SEQUENCE   444 AA;  48778 MW;  B0EFE3613FE6B78B CRC64;
     MKNVVIVGGG AGGIELATFL GNKLGRQKQA KVTLVDRNAT HLWKPLLHEI ATGVMDDGVD
     SLSYRAHGKN HFFSFEQGSI IRINREQKYV ELAPVYGQEG DMLVIARRIP YDYLVIAIGS
     KSNDFNTKGV ADNCIFLDSS KQALRFQHKL LELFLKFSEN RALDDIGEEE FKQKLVDENK
     VNIAIVGGGA TGVELTAELY HAAEDLSSYG YGKIDSSCLQ VTLVEAGTRL LPALPENLSA
     AVLDELKEMG TNVQLNTMIT EAQPNTLITK DGGEIKADLI VWAAGVRAST VTQQFDGLEI
     NRINQLVVKD TLQTTVDDSI FAIGDCAALI QSNGKLVPPR AQAAHQMAKA CAKNIFALFE
     NKPLKSFKYN DKGTLVSLSN FTALGSLTNK FGKNPLTVQG KFAQFAYVSL YRMHQHALHG
     CIKIGLIILV DKLNRYLKPR LKLH
//