ID NQO10_THET8 Reviewed; 176 AA. AC Q56225; Q5SM50; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 120. DE RecName: Full=NADH-quinone oxidoreductase subunit 10; DE EC=7.1.1.-; DE AltName: Full=NADH dehydrogenase I chain 10; DE AltName: Full=NDH-1 subunit 10; GN Name=nqo10; OrderedLocusNames=TTHA0093; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Deinococcota; 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 -!- 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 6 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U52917; AAA97947.1; -; Genomic_DNA. DR EMBL; AP008226; BAD69916.1; -; Genomic_DNA. DR PIR; T11907; T11907. DR RefSeq; WP_011227703.1; NC_006461.1. DR RefSeq; YP_143359.1; NC_006461.1. DR PDB; 4HE8; X-ray; 3.30 A; D/J=1-176. DR PDB; 4HEA; X-ray; 3.30 A; J/R=1-176. DR PDB; 6I0D; X-ray; 3.60 A; J/R=1-176. DR PDB; 6I1P; X-ray; 3.21 A; J/R=1-176. DR PDB; 6Q8O; X-ray; 3.60 A; J/R=1-176. DR PDB; 6Q8W; X-ray; 3.40 A; J/R=1-176. DR PDB; 6Q8X; X-ray; 3.51 A; J/R=1-176. DR PDB; 6Y11; X-ray; 3.11 A; J/R=1-176. DR PDB; 6ZIY; EM; 4.25 A; J=1-176. DR PDB; 6ZJL; EM; 4.30 A; J=1-176. DR PDB; 6ZJN; EM; 6.10 A; J=1-176. DR PDB; 6ZJY; EM; 5.50 A; J=1-176. 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; Q56225; -. DR EMDB; EMD-11231; -. DR EMDB; EMD-11235; -. DR EMDB; EMD-11237; -. DR EMDB; EMD-11238; -. DR SMR; Q56225; -. DR DIP; DIP-59268N; -. DR IntAct; Q56225; 15. DR TCDB; 3.D.1.3.1; the h+ or na+-translocating nadh dehydrogenase (ndh) family. DR EnsemblBacteria; BAD69916; BAD69916; BAD69916. DR GeneID; 3169626; -. DR KEGG; ttj:TTHA0093; -. DR PATRIC; fig|300852.9.peg.91; -. DR eggNOG; COG0839; Bacteria. DR HOGENOM; CLU_085957_4_1_0; -. DR Proteomes; UP000000532; Chromosome. 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; NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ; 1. DR InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6. DR InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ. DR PANTHER; PTHR33269:SF5; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 6, CHLOROPLASTIC; 1. DR PANTHER; PTHR33269; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 6; 1. DR Pfam; PF00499; Oxidored_q3; 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. FT CHAIN 1..176 FT /note="NADH-quinone oxidoreductase subunit 10" FT /id="PRO_0000118369" FT TRANSMEM 2..22 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 26..46 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 56..76 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 91..111 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 137..157 FT /note="Helical" FT /evidence="ECO:0000255" FT HELIX 2..21 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 25..45 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 49..57 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 58..62 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 63..73 FT /evidence="ECO:0007829|PDB:6Y11" FT STRAND 76..79 FT /evidence="ECO:0007829|PDB:4HE8" FT HELIX 89..108 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 124..131 FT /evidence="ECO:0007829|PDB:6Y11" FT TURN 132..135 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 136..157 FT /evidence="ECO:0007829|PDB:6Y11" SQ SEQUENCE 176 AA; 18551 MW; 802325655FE3AAB1 CRC64; MSLLEGLALF LLLLSGVLVV TLRNAIHAAL ALILNFLVLA GVYVALDARF LGFIQVIVYA GAIVVLFLFV IMLLFAAQGE IGFDPLVRSR PLAALLALGV AGILAAGLWG LDLAFTQDLK GGLPQALGPL LYGDWLFVLL AVGFLLMAAT VVAVALVEPG KASRAKEAEK REEVAR //