ID NQO2_THET8 Reviewed; 181 AA. AC Q56221; Q5SM55; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 161. DE RecName: Full=NADH-quinone oxidoreductase subunit 2; DE EC=7.1.1.-; DE AltName: Full=NADH dehydrogenase I chain 2; DE AltName: Full=NDH-1 subunit 2; GN Name=nqo2; OrderedLocusNames=TTHA0088; 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], AND CHARACTERIZATION. 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. RN [3] RP PROTEIN SEQUENCE OF 2-9, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, EPR RP SPECTROSCOPY, AND SUBUNIT. RC STRAIN=ATCC 27634 / DSM 579 / HB8; 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 Thermus RT thermophilus."; RL Biochemistry 45:4413-4420(2006). RN [4] RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF ENZYME HYDROPHILIC DOMAIN IN RP COMPLEX WITH 2FE-2S CLUSTER, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, RP DOMAIN, ELECTRON TRANSFER MECHANISM, AND DISULFIDE BOND. 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 Thermus RT thermophilus."; RL Science 311:1430-1436(2006). 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 -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000269|PubMed:16469879}; CC Note=Binds 1 [2Fe-2S] cluster. This [2Fe-2S] cluster is referred to as CC N1a. {ECO:0000269|PubMed:16469879}; 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. {ECO:0000269|PubMed:16469879, CC ECO:0000269|PubMed:16584177}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:16469879}; CC Peripheral membrane protein {ECO:0000305|PubMed:16469879}; Cytoplasmic CC side {ECO:0000305|PubMed:16469879}. CC -!- DOMAIN: The subunit can be divided into two domains: an N-terminal CC four-helical bundle (residues 2 to 74) involved in interactions with CC subunits Nqo1 and Nqo3, and a thioredoxin-like C-terminal domain CC (residues 75 to 180) that coordinates the binuclear cluster N1a. CC {ECO:0000269|PubMed:16469879}. CC -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family. CC {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; AAA97942.1; -; Genomic_DNA. DR EMBL; AP008226; BAD69911.1; -; Genomic_DNA. DR PIR; T11902; T11902. DR RefSeq; WP_011174268.1; NC_006461.1. DR RefSeq; YP_143354.1; NC_006461.1. DR PDB; 2FUG; X-ray; 3.30 A; 2/B/K/T=1-181. DR PDB; 2YBB; EM; 19.00 A; 2=1-181. DR PDB; 3I9V; X-ray; 3.10 A; 2/B=1-181. DR PDB; 3IAM; X-ray; 3.10 A; 2/B=1-181. DR PDB; 3IAS; X-ray; 3.15 A; 2/B/K/T=1-181. DR PDB; 3M9S; X-ray; 4.50 A; 2/B=1-181. DR PDB; 4HEA; X-ray; 3.30 A; 2/C=1-181. DR PDB; 6I0D; X-ray; 3.60 A; 2/C=1-181. DR PDB; 6I1P; X-ray; 3.21 A; 2/C=1-181. DR PDB; 6Q8O; X-ray; 3.60 A; 2/C=1-181. DR PDB; 6Q8W; X-ray; 3.40 A; 2/C=1-181. DR PDB; 6Q8X; X-ray; 3.51 A; 2/C=1-181. DR PDB; 6Y11; X-ray; 3.11 A; 2/C=1-181. DR PDB; 6ZIY; EM; 4.25 A; 2=1-181. DR PDB; 6ZJL; EM; 4.30 A; 2=1-181. DR PDB; 6ZJN; EM; 6.10 A; 2=1-181. DR PDB; 6ZJY; EM; 5.50 A; 2=1-181. DR PDBsum; 2FUG; -. DR PDBsum; 2YBB; -. DR PDBsum; 3I9V; -. DR PDBsum; 3IAM; -. DR PDBsum; 3IAS; -. DR PDBsum; 3M9S; -. 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; Q56221; -. DR EMDB; EMD-11231; -. DR EMDB; EMD-11235; -. DR EMDB; EMD-11237; -. DR EMDB; EMD-11238; -. DR EMDB; EMD-1876; -. DR SMR; Q56221; -. DR DIP; DIP-59260N; -. DR IntAct; Q56221; 1. DR TCDB; 3.D.1.3.1; the h+ or na+-translocating nadh dehydrogenase (ndh) family. DR EnsemblBacteria; BAD69911; BAD69911; BAD69911. DR GeneID; 3168326; -. DR KEGG; ttj:TTHA0088; -. DR PATRIC; fig|300852.9.peg.86; -. DR eggNOG; COG1905; Bacteria. DR HOGENOM; CLU_054362_2_0_0; -. DR PhylomeDB; Q56221; -. DR EvolutionaryTrace; Q56221; -. DR Proteomes; UP000000532; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR CDD; cd03064; TRX_Fd_NuoE; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR Gene3D; 1.10.10.1590; NADH-quinone oxidoreductase subunit E; 1. DR InterPro; IPR002023; NuoE-like. DR InterPro; IPR042128; NuoE_dom. DR InterPro; IPR041921; NuoE_N. DR InterPro; IPR036249; Thioredoxin-like_sf. DR NCBIfam; TIGR01958; nuoE_fam; 1. DR PANTHER; PTHR10371:SF3; NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 2, MITOCHONDRIAL; 1. DR PANTHER; PTHR10371; NADH DEHYDROGENASE UBIQUINONE FLAVOPROTEIN 2, MITOCHONDRIAL; 1. DR Pfam; PF01257; 2Fe-2S_thioredx; 1. DR PIRSF; PIRSF000216; NADH_DH_24kDa; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS01099; COMPLEX1_24K; 1. PE 1: Evidence at protein level; KW 2Fe-2S; 3D-structure; Cell membrane; Direct protein sequencing; KW Disulfide bond; Iron; Iron-sulfur; Membrane; Metal-binding; NAD; Quinone; KW Reference proteome; Translocase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:16584177" FT CHAIN 2..181 FT /note="NADH-quinone oxidoreductase subunit 2" FT /id="PRO_0000118686" FT BINDING 83 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000269|PubMed:16469879" FT BINDING 87 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000269|PubMed:16469879" FT BINDING 88 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000269|PubMed:16469879" FT BINDING 124 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000269|PubMed:16469879" FT BINDING 128 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000269|PubMed:16469879" FT DISULFID 144..172 FT /evidence="ECO:0000269|PubMed:16469879" FT TURN 4..6 FT /evidence="ECO:0007829|PDB:3I9V" FT HELIX 8..15 FT /evidence="ECO:0007829|PDB:3I9V" FT HELIX 24..26 FT /evidence="ECO:0007829|PDB:3I9V" FT HELIX 27..38 FT /evidence="ECO:0007829|PDB:3I9V" FT HELIX 43..53 FT /evidence="ECO:0007829|PDB:3I9V" FT HELIX 57..64 FT /evidence="ECO:0007829|PDB:3I9V" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:6Y11" FT STRAND 77..83 FT /evidence="ECO:0007829|PDB:3I9V" FT HELIX 86..89 FT /evidence="ECO:0007829|PDB:3I9V" FT TURN 90..92 FT /evidence="ECO:0007829|PDB:3I9V" FT HELIX 93..104 FT /evidence="ECO:0007829|PDB:3I9V" FT STRAND 108..111 FT /evidence="ECO:0007829|PDB:6Y11" FT STRAND 117..123 FT /evidence="ECO:0007829|PDB:3I9V" FT HELIX 128..130 FT /evidence="ECO:0007829|PDB:3I9V" FT STRAND 132..135 FT /evidence="ECO:0007829|PDB:3IAM" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:3I9V" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:3IAM" FT HELIX 147..158 FT /evidence="ECO:0007829|PDB:3I9V" FT HELIX 163..165 FT /evidence="ECO:0007829|PDB:3I9V" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:3I9V" SQ SEQUENCE 181 AA; 20286 MW; 484FE09245C613EE CRC64; MGFFDDKQDF LEETFAKYPP EGRRAAIMPL LRRVQQEEGW IRPERIEEIA RLVGTTPTEV MGVASFYSYY QFVPTGKYHL QVCATLSCKL AGAEELWDYL TETLGIGPGE VTPDGLFSVQ KVECLGSCHT APVIQVNDEP YVECVTRARL EALLAGLRAG KRLEEIELPG KCGHHVHEVE V //