ID NQO12_THET8 Reviewed; 606 AA. AC Q56227; Q5SM48; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 129. DE RecName: Full=NADH-quinone oxidoreductase subunit 12; DE EC=7.1.1.-; DE AltName: Full=NADH dehydrogenase I chain 12; DE AltName: Full=NDH-1 subunit 12; GN Name=nqo12; OrderedLocusNames=TTHA0095; 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 5 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; AAA97949.1; -; Genomic_DNA. DR EMBL; AP008226; BAD69918.1; -; Genomic_DNA. DR PIR; T11909; T11909. DR RefSeq; WP_011227705.1; NC_006461.1. DR RefSeq; YP_143361.1; NC_006461.1. DR PDB; 4HE8; X-ray; 3.30 A; F/L=1-606. DR PDB; 4HEA; X-ray; 3.30 A; L/T=1-606. DR PDB; 6I0D; X-ray; 3.60 A; L/T=1-606. DR PDB; 6I1P; X-ray; 3.21 A; L/T=1-606. DR PDB; 6Q8O; X-ray; 3.60 A; L/T=1-606. DR PDB; 6Q8W; X-ray; 3.40 A; L/T=1-606. DR PDB; 6Q8X; X-ray; 3.51 A; L/T=1-606. DR PDB; 6Y11; X-ray; 3.11 A; L/T=1-606. DR PDB; 6ZIY; EM; 4.25 A; L=1-606. DR PDB; 6ZJL; EM; 4.30 A; L=1-606. DR PDB; 6ZJN; EM; 6.10 A; L=1-606. DR PDB; 6ZJY; EM; 5.50 A; L=1-606. 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; Q56227; -. DR EMDB; EMD-11231; -. DR EMDB; EMD-11235; -. DR EMDB; EMD-11237; -. DR EMDB; EMD-11238; -. DR SMR; Q56227; -. DR DIP; DIP-59270N; -. DR IntAct; Q56227; 1. DR TCDB; 3.D.1.3.1; the h+ or na+-translocating nadh dehydrogenase (ndh) family. DR EnsemblBacteria; BAD69918; BAD69918; BAD69918. DR GeneID; 3169613; -. DR KEGG; ttj:TTHA0095; -. DR PATRIC; fig|300852.9.peg.93; -. DR eggNOG; COG1009; Bacteria. DR HOGENOM; CLU_007100_6_0_0; -. DR PhylomeDB; Q56227; -. 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 GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR Gene3D; 1.20.5.2700; -; 1. DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr. DR InterPro; IPR001750; ND/Mrp_mem. DR InterPro; IPR003945; NU5C-like. DR InterPro; IPR001516; Proton_antipo_N. DR NCBIfam; TIGR01974; NDH_I_L; 1. DR PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1. DR PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR Pfam; PF00662; Proton_antipo_N; 1. DR PRINTS; PR01434; NADHDHGNASE5. DR PRINTS; PR01435; NPOXDRDTASE5. 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..606 FT /note="NADH-quinone oxidoreductase subunit 12" FT /id="PRO_0000118212" FT TRANSMEM 1..21 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 29..49 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 75..95 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 104..124 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 126..146 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 165..185 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 206..226 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 234..254 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 266..286 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 303..323 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 325..345 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 364..384 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 397..417 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 441..461 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 492..512 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 584..604 FT /note="Helical" FT /evidence="ECO:0000255" FT HELIX 2..19 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 27..49 FT /evidence="ECO:0007829|PDB:6Y11" FT STRAND 53..57 FT /evidence="ECO:0007829|PDB:6Y11" FT STRAND 65..69 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 71..94 FT /evidence="ECO:0007829|PDB:6Y11" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:6I1P" FT HELIX 101..119 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 124..142 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 150..178 FT /evidence="ECO:0007829|PDB:6Y11" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:4HE8" FT HELIX 185..192 FT /evidence="ECO:0007829|PDB:6Y11" FT STRAND 193..195 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 199..216 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 222..225 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 227..231 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 234..241 FT /evidence="ECO:0007829|PDB:6Y11" FT STRAND 244..246 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 247..255 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 257..261 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 264..283 FT /evidence="ECO:0007829|PDB:6Y11" FT TURN 284..287 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 291..311 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 315..342 FT /evidence="ECO:0007829|PDB:6Y11" FT TURN 356..358 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 362..374 FT /evidence="ECO:0007829|PDB:6Y11" FT STRAND 377..379 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 380..394 FT /evidence="ECO:0007829|PDB:6Y11" FT STRAND 395..397 FT /evidence="ECO:0007829|PDB:4HE8" FT HELIX 400..425 FT /evidence="ECO:0007829|PDB:6Y11" FT STRAND 426..428 FT /evidence="ECO:0007829|PDB:4HE8" FT HELIX 440..455 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 457..459 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 469..473 FT /evidence="ECO:0007829|PDB:6Y11" FT TURN 474..476 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 489..514 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 519..529 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 531..533 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 534..541 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 543..580 FT /evidence="ECO:0007829|PDB:6Y11" FT HELIX 586..603 FT /evidence="ECO:0007829|PDB:6Y11" SQ SEQUENCE 606 AA; 65141 MW; 47318E8F2665295C CRC64; MALLGTILLP LLGFALLGLF GKRMREPLPG VLASGLVLAS FLLGAGLLLS GGARFQAEWL PGIPFSLLLD NLSGFMLLIV TGVGFLIHVY AIGYMGGDPG YSRFFAYFNL FIAMMLTLVL ADSYPVMFIG WEGVGLASFL LIGFWYKNPQ YADSARKAFI VNRIGDLGFM LGMAILWALY GTLSISELKE AMEGPLKNPD LLALAGLLLF LGAVGKSAQI PLMVWLPDAM AGPTPVSALI HAATMVTAGV YLIARSSFLY SVLPDVSYAI AVVGLLTAAY GALSAFGQTD IKKIVAYSTI SQLGYMFLAA GVGAYWVALF HVFTHAFFKA LLFLASGSVI HALGGEQDVR KMGGLWKHLP QTRWHALIGA LALGGLPLLS GFWSKDAILA ATLTYPFGGV GFYVGALLVA VLTAMYAMRW FVLVFLGEER GHHHPHEAPP VMLWPNHLLA LGSVLAGYLA LPHPLPNVLE PFLKPALAEV EAHHLSLGAE WGLIALSAAV ALLGLWAGFV FFQRKVFPAW YLAFEAASRE AFYVDRAYNA LIVNPLKALA EALFYGDRGL LSGYFGLGGA ARSLGQGLAR LQTGYLRVYA LLFVLGALLL LGVMRW //