NQO15_THET8
ID NQO15_THET8 Reviewed; 129 AA.
AC Q5SKZ7;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=NADH-quinone oxidoreductase subunit 15;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I chain 15;
DE AltName: Full=NDH-1 subunit 15;
GN Name=nqo15; OrderedLocusNames=TTHA0496;
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 [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 [2]
RP PROTEIN SEQUENCE OF 2-9, CHARACTERIZATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, 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 [3]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF ENZYME HYDROPHILIC DOMAIN,
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, 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 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. The Nqo15 subunit has
CC probably a role in complex stabilization, and may be also involved in
CC the storage of iron for iron-sulfur cluster regeneration in the
CC complex. {ECO:0000269|PubMed:16469879, ECO:0000269|PubMed:16584177}.
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. Nqo15 is bound to the side of the
CC complex near the N-terminus of Nqo3, where it interacts with subunits
CC Nqo3, Nqo2, Nqo1, Nqo9 and Nqo4. {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: Has a similar fold to the mitochondrial iron chaperone
CC frataxin. {ECO:0000305|PubMed:16469879}.
CC -!- SIMILARITY: Belongs to the complex I Nqo15 family. {ECO:0000305}.
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DR EMBL; AP008226; BAD70319.1; -; Genomic_DNA.
DR RefSeq; WP_011227977.1; NC_006461.1.
DR RefSeq; YP_143762.1; NC_006461.1.
DR PDB; 2FUG; X-ray; 3.30 A; 7/H/Q/Z=1-129.
DR PDB; 2YBB; EM; 19.00 A; 7=1-129.
DR PDB; 3I9V; X-ray; 3.10 A; 7/H=1-129.
DR PDB; 3IAM; X-ray; 3.10 A; 7/H=1-129.
DR PDB; 3IAS; X-ray; 3.15 A; 7/H/Q/Z=1-129.
DR PDB; 3M9S; X-ray; 4.50 A; 7/J=1-129.
DR PDB; 4HEA; X-ray; 3.30 A; 7/I=1-129.
DR PDB; 6I0D; X-ray; 3.60 A; 7/I=1-129.
DR PDB; 6I1P; X-ray; 3.21 A; 7/I=1-129.
DR PDB; 6Q8O; X-ray; 3.60 A; 7/I=1-129.
DR PDB; 6Q8W; X-ray; 3.40 A; 7/I=1-129.
DR PDB; 6Q8X; X-ray; 3.51 A; 7/I=1-129.
DR PDB; 6Y11; X-ray; 3.11 A; 7/I=1-129.
DR PDB; 6ZIY; EM; 4.25 A; 7=1-129.
DR PDB; 6ZJL; EM; 4.30 A; 7=1-129.
DR PDB; 6ZJN; EM; 6.10 A; 7=1-129.
DR PDB; 6ZJY; EM; 5.50 A; 7=1-129.
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; Q5SKZ7; -.
DR SMR; Q5SKZ7; -.
DR DIP; DIP-59273N; -.
DR IntAct; Q5SKZ7; 1.
DR STRING; 300852.55771878; -.
DR TCDB; 3.D.1.3.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAD70319; BAD70319; BAD70319.
DR GeneID; 3169322; -.
DR KEGG; ttj:TTHA0496; -.
DR PATRIC; fig|300852.9.peg.494; -.
DR eggNOG; ENOG50325PM; Bacteria.
DR HOGENOM; CLU_132697_0_0_0; -.
DR OMA; RMERPYD; -.
DR EvolutionaryTrace; Q5SKZ7; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR Gene3D; 3.30.920.80; -; 1.
DR InterPro; IPR036524; Frataxin/CyaY_sf.
DR InterPro; IPR021093; NADH_quinone_OxRdtase_su15.
DR InterPro; IPR038458; NADH_quinone_OxRdtase_su15_sf.
DR Pfam; PF11497; NADH_Oxid_Nqo15; 1.
DR SUPFAM; SSF55387; SSF55387; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Membrane; NAD;
KW Quinone; Reference proteome; Translocase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16584177"
FT CHAIN 2..129
FT /note="NADH-quinone oxidoreductase subunit 15"
FT /id="PRO_0000233014"
FT HELIX 5..26
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 112..126
FT /evidence="ECO:0007829|PDB:3I9V"
SQ SEQUENCE 129 AA; 14788 MW; A944E174C0DE152C CRC64;
MSASSERELY EAWVELLSWM REYAQAKGVR FEKEADFPDF IYRMERPYDL PTTIMTASLS
DGLGEPFLLA DVSPRHAKLK RIGLRLPRAH IHLHAHYEPG KGLVTGKIPL TKERFFALAD
RAREALAFA
