NDH_HAEIN
ID NDH_HAEIN Reviewed; 444 AA.
AC P44856;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Type II NADH:quinone oxidoreductase {ECO:0000250|UniProtKB:P00393};
DE EC=1.6.5.9 {ECO:0000250|UniProtKB:P00393};
DE AltName: Full=NADH dehydrogenase-2 {ECO:0000250|UniProtKB:P00393};
DE Short=NADH dh II {ECO:0000250|UniProtKB:P00393};
DE Short=NDH-2 {ECO:0000250|UniProtKB:P00393};
DE AltName: Full=NADH-quinone reductase {ECO:0000250|UniProtKB:P00393};
DE Short=NQR {ECO:0000250|UniProtKB:P00393};
GN Name=ndh; OrderedLocusNames=HI_0747;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.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., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Alternative, nonproton pumping NADH:quinone oxidoreductase
CC that delivers electrons to the respiratory chain by oxidation of NADH
CC and reduction of quinones (By similarity). Utilizes NADH exclusively,
CC and electron flow from NADH to ubiquinone does not generate an
CC electrochemical gradient (By similarity).
CC {ECO:0000250|UniProtKB:P00393}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.9;
CC Evidence={ECO:0000250|UniProtKB:P00393};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + H(+) + NADH = a ubiquinol + NAD(+);
CC Xref=Rhea:RHEA:23152, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000250|UniProtKB:P00393};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P00393};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P00393};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P00393}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P00393}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P00393}. Note=Membrane-bound (By similarity).
CC Interaction with the membrane is probably mediated by amphipathic
CC helices and electrostatic interactions (By similarity).
CC {ECO:0000250|UniProtKB:P00393}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR EMBL; L42023; AAC22405.1; -; Genomic_DNA.
DR PIR; C64090; C64090.
DR RefSeq; NP_438906.1; NC_000907.1.
DR RefSeq; WP_005693148.1; NC_000907.1.
DR AlphaFoldDB; P44856; -.
DR SMR; P44856; -.
DR STRING; 71421.HI_0747; -.
DR EnsemblBacteria; AAC22405; AAC22405; HI_0747.
DR KEGG; hin:HI_0747; -.
DR PATRIC; fig|71421.8.peg.784; -.
DR eggNOG; COG1252; Bacteria.
DR HOGENOM; CLU_021377_7_0_6; -.
DR OMA; DHCIFLD; -.
DR PhylomeDB; P44856; -.
DR BioCyc; HINF71421:G1GJ1-785-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR045024; NDH-2.
DR PANTHER; PTHR43706; PTHR43706; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Electron transport; FAD; Flavoprotein;
KW Membrane; NAD; Oxidoreductase; Reference proteome; Transport; Ubiquinone.
FT CHAIN 1..444
FT /note="Type II NADH:quinone oxidoreductase"
FT /id="PRO_0000079891"
FT BINDING 8..12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00393"
FT BINDING 38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00393"
FT BINDING 120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00393"
FT BINDING 186..191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00393"
FT BINDING 285
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00393"
FT BINDING 325
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00393"
FT BINDING 341
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00393"
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
