NQO11_THET8
ID NQO11_THET8 Reviewed; 95 AA.
AC Q56226; Q5SM49;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=NADH-quinone oxidoreductase subunit 11;
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01456};
DE AltName: Full=NADH dehydrogenase I chain 11;
DE AltName: Full=NDH-1 subunit 11;
GN Name=nqo11; OrderedLocusNames=TTHA0094;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=9020134; DOI=10.1074/jbc.272.7.4201;
RA Yano T., Chu S.S., Sled' V.D., Ohnishi T., Yagi T.;
RT "The proton-translocating NADH-quinone oxidoreductase (NDH-1) of
RT thermophilic bacterium Thermus thermophilus HB-8. Complete DNA sequence of
RT the gene cluster and thermostable properties of the expressed NQO2
RT subunit.";
RL J. Biol. Chem. 272:4201-4211(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 menaquinone.
CC Couples the redox reaction to proton translocation (for every two
CC electrons transferred, four hydrogen ions are translocated across the
CC cytoplasmic membrane), and thus conserves the redox energy in a proton
CC gradient required for the synthesis of ATP.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01456};
CC -!- SUBUNIT: NDH-1 is composed of 15 different subunits, Nqo1 to Nqo15. The
CC complex has a L-shaped structure, with the hydrophobic arm (subunits
CC Nqo7, Nqo8 and Nqo10 to Nqo14) embedded in the membrane and the
CC hydrophilic peripheral arm (subunits Nqo1 to Nqo6, Nqo9 and Nqo15)
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 4L family.
CC {ECO:0000255|HAMAP-Rule:MF_01456}.
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DR EMBL; U52917; AAA97948.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD69917.1; -; Genomic_DNA.
DR PIR; T11908; T11908.
DR RefSeq; WP_011227704.1; NC_006461.1.
DR RefSeq; YP_143360.1; NC_006461.1.
DR PDB; 4HE8; X-ray; 3.30 A; E/K=1-95.
DR PDB; 4HEA; X-ray; 3.30 A; K/S=1-95.
DR PDB; 6I0D; X-ray; 3.60 A; K/S=1-95.
DR PDB; 6I1P; X-ray; 3.21 A; K/S=1-95.
DR PDB; 6Q8O; X-ray; 3.60 A; K/S=1-95.
DR PDB; 6Q8W; X-ray; 3.40 A; K/S=1-95.
DR PDB; 6Q8X; X-ray; 3.51 A; K/S=1-95.
DR PDB; 6Y11; X-ray; 3.11 A; K/S=1-95.
DR PDB; 6ZIY; EM; 4.25 A; K=1-95.
DR PDB; 6ZJL; EM; 4.30 A; K=1-95.
DR PDB; 6ZJN; EM; 6.10 A; K=1-95.
DR PDB; 6ZJY; EM; 5.50 A; K=1-95.
DR PDBsum; 4HE8; -.
DR PDBsum; 4HEA; -.
DR PDBsum; 6I0D; -.
DR PDBsum; 6I1P; -.
DR PDBsum; 6Q8O; -.
DR PDBsum; 6Q8W; -.
DR PDBsum; 6Q8X; -.
DR PDBsum; 6Y11; -.
DR PDBsum; 6ZIY; -.
DR PDBsum; 6ZJL; -.
DR PDBsum; 6ZJN; -.
DR PDBsum; 6ZJY; -.
DR AlphaFoldDB; Q56226; -.
DR SMR; Q56226; -.
DR DIP; DIP-59269N; -.
DR IntAct; Q56226; 1.
DR STRING; 300852.55771476; -.
DR TCDB; 3.D.1.3.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAD69917; BAD69917; BAD69917.
DR GeneID; 3169648; -.
DR KEGG; ttj:TTHA0094; -.
DR PATRIC; fig|300852.9.peg.92; -.
DR eggNOG; COG0713; Bacteria.
DR HOGENOM; CLU_144724_0_0_0; -.
DR OMA; NFVAFSY; -.
DR PhylomeDB; Q56226; -.
DR Proteomes; UP000000532; Chromosome.
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:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR HAMAP; MF_01456; NDH1_NuoK; 1.
DR InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K.
DR InterPro; IPR039428; NUOK/Mnh_C1-like.
DR PANTHER; PTHR11434; PTHR11434; 1.
DR Pfam; PF00420; Oxidored_q2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..95
FT /note="NADH-quinone oxidoreductase subunit 11"
FT /id="PRO_0000118523"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT HELIX 2..20
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 24..49
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 52..78
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:6Y11"
SQ SEQUENCE 95 AA; 9996 MW; ED9D2A80D2E96592 CRC64;
MSYLLTSALL FALGVYGVLT RRTAILVFLS IELMLNAANL SLVGFARAYG LDGQVAALMV
IAVAAAEVAV GLGLIVAIFR HRESTAVDDL SELRG
