NQO8_PARDE
ID NQO8_PARDE Reviewed; 345 AA.
AC P29920;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=NADH-quinone oxidoreductase subunit 8;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunit H;
DE AltName: Full=NDH-1 subunit 8;
GN Name=nqo8 {ECO:0000303|PubMed:8422400};
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13543 / NRRL B-3784 / NRC 449;
RX PubMed=8422400; DOI=10.1021/bi00054a030;
RA Xu X., Matsuno-Yagi A., Yagi T.;
RT "DNA sequencing of the seven remaining structural genes of the gene cluster
RT encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus
RT denitrificans.";
RL Biochemistry 32:968-981(1993).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC -!- SUBUNIT: NDH-1 is composed of at least 14 different subunits, Nqo1 to
CC Nqo14. The complex has a L-shaped structure, with the hydrophobic arm
CC (subunits Nqo7, Nqo8, Nqo10 to Nqo14) embedded in the inner membrane
CC and the hydrophilic peripheral arm (subunits Nqo1 to Nqo6, Nqo9)
CC protruding into the bacterial cytoplasm. The hydrophilic domain
CC contains all the redox centers.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. {ECO:0000305}.
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DR EMBL; L02354; AAA25592.1; -; Genomic_DNA.
DR PIR; C45456; C45456.
DR AlphaFoldDB; P29920; -.
DR SMR; P29920; -.
DR TCDB; 3.D.1.2.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR HAMAP; MF_01350; NDH1_NuoH; 1.
DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO.
DR InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS.
DR PANTHER; PTHR11432; PTHR11432; 1.
DR Pfam; PF00146; NADHdh; 1.
DR PROSITE; PS00667; COMPLEX1_ND1_1; 1.
DR PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW Transmembrane; Transmembrane helix; Ubiquinone.
FT CHAIN 1..345
FT /note="NADH-quinone oxidoreductase subunit 8"
FT /id="PRO_0000117521"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 345 AA; 38751 MW; E33B667E569506B4 CRC64;
MAEFWASPYG FALSMLLQGL AVIAFVMGSL IFMVYGDRKI WAAVQMRRGP NVVGPWGLLQ
TFADALKYIV KEIVIPAGAD KFVYFLAPFL SMMLALFAFV VIPFDEGWVM ANINVGILFI
FAASSLEVYG VIMGGWASNS KYPFLASLRS AAQMISYEVS LGLIIIGIII STGSMNLTAI
VEAHGGDYGL LNWYWLPHLP MVVLFFVSAL AECNRPPFDL VEAESELVAG FMTEYSSTPY
LLFMAGEYIA MYLMCALLSL LFFGGWLSPV PFIADGWWWM VIKMWFWFYM FAMVKAIVPR
YRYDQLMRIG WKVFLPLSLG WVVLVAILAR YEILGGFWAR FAVGG