ID   NQO10_PARDE             Reviewed;         200 AA.
AC   P29922;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=NADH-quinone oxidoreductase chain 10;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I, chain 10;
DE   AltName: Full=NDH-1, chain 10;
GN   Name=nqo10 {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 6 family. {ECO:0000305}.
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DR   EMBL; L02354; AAA25596.1; -; Genomic_DNA.
DR   PIR; F45456; F45456.
DR   RefSeq; WP_041529947.1; NZ_PPGA01000003.1.
DR   AlphaFoldDB; P29922; -.
DR   SMR; P29922; -.
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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.1200; -; 1.
DR   InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6.
DR   InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ.
DR   Pfam; PF00499; Oxidored_q3; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW   Transmembrane; Transmembrane helix; Ubiquinone.
FT   CHAIN           1..200
FT                   /note="NADH-quinone oxidoreductase chain 10"
FT                   /id="PRO_0000118368"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   200 AA;  21819 MW;  9D3B421C33F4ACAE CRC64;
     MMTFAFYLFA ISACVAGFMV VIGRNPVHSV LWLILAFLSA AGLFVLQGAE FVAMLLVVVY
     VGAVAVLFLF VVMMLDVDFA ELKGELARYL PLALVIGVVL LAQLGIAFSG WTPSDQAESL
     RAAPVDAAVE NTLGLGLVLY DRYVLMFQLA GLVLLVAMIG AIVLTMRHRK DVKRQNVLEQ
     MWRDPAKTME LKDVKPGQGL