NQO2_THET8
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 03-AUG-2022, entry version 153.
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; Deinococcus-Thermus; 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}.
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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 SMR; Q56221; -.
DR DIP; DIP-59260N; -.
DR IntAct; Q56221; 1.
DR STRING; 300852.55771470; -.
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 OMA; VGKFHVQ; -.
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; 1.10.10.1590; -; 1.
DR InterPro; IPR002023; NuoE-like.
DR InterPro; IPR042128; NuoE_dom.
DR InterPro; IPR041921; NuoE_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PIRSF; PIRSF000216; NADH_DH_24kDa; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01958; nuoE_fam; 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
