ID NQO6_THET8 Reviewed; 181 AA. AC Q56218; Q5SM58; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 16-JUN-2009, entry version 63. DE RecName: Full=NADH-quinone oxidoreductase subunit 6; DE EC=1.6.99.5; DE AltName: Full=NADH dehydrogenase I subunit 6; DE AltName: Full=NDH-1 subunit 6; GN Name=nqo6; OrderedLocusNames=TTHA0085; OS Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=97172490; 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 RT sequence of the gene cluster and thermostable properties of the RT expressed NQO2 subunit."; RL J. Biol. Chem. 272:4201-4211(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., RA Shibata T., 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. RN [3] RP PROTEIN SEQUENCE OF 2-9, IDENTIFICATION BY MASS SPECTROMETRY, EPR RP SPECTROSCOPY, AND SUBUNIT. RX PubMed=16584177; DOI=10.1021/bi0600998; RA Hinchliffe P., Carroll J., Sazanov L.A.; RT "Identification of a novel subunit of respiratory complex I from RT Thermus thermophilus."; RL Biochemistry 45:4413-4420(2006). RN [4] RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS), SUBUNIT, AND ELECTRON TRANSFER RP MECHANISM. RX PubMed=16469879; DOI=10.1126/science.1123809; RA Sazanov L.A., Hinchliffe P.; RT "Structure of the hydrophilic domain of respiratory complex I from RT Thermus thermophilus."; RL Science 311:1430-1436(2006). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC menaquinone. Couples the redox reaction to proton translocation CC (for every two electrons transferred, four hydrogen ions are CC translocated across the cytoplasmic membrane), and thus conserves CC the redox energy in a proton gradient required for the synthesis CC of ATP. CC -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. This 4Fe-4S cluster CC is referred to as N2. CC -!- SUBUNIT: NDH-1 is composed of 15 different subunits, nqo1 to CC nqo15. The complex has a L-shaped structure, with the hydrophobic CC arm (subunits nqo7, nqo8 and nqo10 to nqo14) embedded in the CC membrane and the hydrophilic peripheral arm (subunits nqo1 to CC nqo6, nqo9 and nqo15) protruding into the bacterial cytoplasm. The CC hydrophilic domain contains all the redox centers. Subunit nqo6 CC interacts extensively with nqo4. CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; CC Cytoplasmic side. CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U52917; AAA97939.1; -; Genomic_DNA. DR EMBL; AP008226; BAD69908.1; -; Genomic_DNA. DR PIR; T11899; T11899. DR RefSeq; YP_143351.1; -. DR PDB; 2FUG; X-ray; 3.30 A; 6/F/O/X=1-181. DR PDBsum; 2FUG; -. DR TCDB; 3.D.1.3.1; proton-translocating NADH dehydrogenase (NDH) family. DR GeneID; 3168381; -. DR GenomeReviews; AP008226_GR; TTHA0085. DR KEGG; ttj:TTHA0085; -. DR HOGENOM; Q56218; -. DR OMA; Q56218; LINWART. DR BioCyc; TTHE300852:TTHA0085-MON; -. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:HAMAP. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:HAMAP. DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:HAMAP. DR HAMAP; MF_01356; -; 1. DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa. DR InterPro; IPR006138; NADH_UbQ_OxRdtase_su-20kDa. DR InterPro; IPR014406; NiFe_hyd_3_ssu/Q_oxred_NuoB. DR PANTHER; PTHR11995:SF2; NADH_DH_20kDa; 1. DR PANTHER; PTHR11995; NiFe_hyd_3_ssu/Q_oxred_NuoB; 1. DR Pfam; PF01058; Oxidored_q6; 1. DR TIGRFAMs; TIGR01957; nuoB_fam; 1. DR PROSITE; PS01150; COMPLEX1_20K; 1. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Cell membrane; Complete proteome; KW Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding; KW NAD; Oxidoreductase; Quinone. FT INIT_MET 1 1 Removed. FT CHAIN 2 181 NADH-quinone oxidoreductase subunit 6. FT /FTId=PRO_0000118763. FT METAL 45 45 Iron-sulfur (4Fe-4S). FT METAL 46 46 Iron-sulfur (4Fe-4S). FT METAL 111 111 Iron-sulfur (4Fe-4S). FT METAL 140 140 Iron-sulfur (4Fe-4S). FT HELIX 19 34 FT HELIX 45 49 FT HELIX 51 53 FT STRAND 78 82 FT TURN 86 88 FT HELIX 89 97 FT STRAND 105 108 FT HELIX 109 113 FT HELIX 127 129 FT STRAND 134 137 FT HELIX 144 159 FT STRAND 165 167 SQ SEQUENCE 181 AA; 20239 MW; A1E030366E6692F1 CRC64; MALKDLFERD VQELEREGIL FTTLEKLVAW GRSNSLWPAT FGLACCAIEM MASTDARNDL ARFGSEVFRA SPRQADVMIV AGRLSKKMAP VMRRVWEQMP DPKWVISMGA CASSGGMFNN YAIVQNVDSV VPVDVYVPGC PPRPEALIYA VMQLQKKVRG QAYNERGERL PPVAAWKRTR G //