NQO4_THET8
ID NQO4_THET8 Reviewed; 409 AA.
AC Q56220; Q5SM56;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=NADH-quinone oxidoreductase subunit 4;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I chain 4;
DE AltName: Full=NDH-1 subunit 4;
GN Name=nqo4; OrderedLocusNames=TTHA0087;
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].
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 1-8, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND
RP 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,
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND ELECTRON TRANSFER 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 Nqo4 subunit may
CC contain the quinone-binding site. {ECO:0000269|PubMed:16469879,
CC 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. This subunit interacts extensively with
CC Nqo6. {ECO:0000269|PubMed:16469879, 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 -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; U52917; AAA97941.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD69910.1; -; Genomic_DNA.
DR PIR; T11901; T11901.
DR RefSeq; WP_011227699.1; NC_006461.1.
DR RefSeq; YP_143353.1; NC_006461.1.
DR PDB; 2FUG; X-ray; 3.30 A; 4/D/M/V=1-409.
DR PDB; 2YBB; EM; 19.00 A; 4=1-409.
DR PDB; 3I9V; X-ray; 3.10 A; 4/D=1-409.
DR PDB; 3IAM; X-ray; 3.10 A; 4/D=1-409.
DR PDB; 3IAS; X-ray; 3.15 A; 4/D/M/V=1-409.
DR PDB; 3M9S; X-ray; 4.50 A; 4/D=1-409.
DR PDB; 4HEA; X-ray; 3.30 A; 4/E=1-409.
DR PDB; 6I0D; X-ray; 3.60 A; 4/E=1-409.
DR PDB; 6I1P; X-ray; 3.21 A; 4/E=1-409.
DR PDB; 6Q8O; X-ray; 3.60 A; 4/E=1-409.
DR PDB; 6Q8W; X-ray; 3.40 A; 4/E=1-409.
DR PDB; 6Q8X; X-ray; 3.51 A; 4/E=1-409.
DR PDB; 6Y11; X-ray; 3.11 A; 4/E=1-409.
DR PDB; 6ZIY; EM; 4.25 A; 4=1-409.
DR PDB; 6ZJL; EM; 4.30 A; 4=1-409.
DR PDB; 6ZJN; EM; 6.10 A; 4=1-409.
DR PDB; 6ZJY; EM; 5.50 A; 4=1-409.
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; Q56220; -.
DR SMR; Q56220; -.
DR DIP; DIP-59262N; -.
DR IntAct; Q56220; 1.
DR STRING; 300852.55771469; -.
DR TCDB; 3.D.1.3.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PRIDE; Q56220; -.
DR EnsemblBacteria; BAD69910; BAD69910; BAD69910.
DR GeneID; 3168206; -.
DR KEGG; ttj:TTHA0087; -.
DR PATRIC; fig|300852.9.peg.85; -.
DR eggNOG; COG0649; Bacteria.
DR HOGENOM; CLU_015134_1_2_0; -.
DR OMA; IMGTSME; -.
DR PhylomeDB; Q56220; -.
DR EvolutionaryTrace; Q56220; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.645.10; -; 1.
DR HAMAP; MF_01358; NDH1_NuoD; 1.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR InterPro; IPR022885; NDH1_su_D/H.
DR InterPro; IPR029014; NiFe-Hase_large.
DR PANTHER; PTHR11993; PTHR11993; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; SSF56762; 1.
DR TIGRFAMs; TIGR01962; NuoD; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Membrane; NAD;
KW Quinone; Reference proteome; Translocase; Transport.
FT CHAIN 1..409
FT /note="NADH-quinone oxidoreductase subunit 4"
FT /id="PRO_0000118617"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:3IAM"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:6I1P"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:3IAM"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:3IAM"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3IAM"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 91..105
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 111..139
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 144..164
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 186..209
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 214..218
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 272..295
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 314..318
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 321..332
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 351..359
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 377..385
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 404..408
FT /evidence="ECO:0007829|PDB:3I9V"
SQ SEQUENCE 409 AA; 46371 MW; 161AA0C796D62ED3 CRC64;
MREEFLEEIP LDAPPEEAKE LRTEVMTLNV GPQHPSTHGV LRLMVTLSGE EVLEVVPHIG
YLHTGFEKTM EHRTYLQNIT YTPRMDYLHS FAHDLAYALA VEKLLGAVVP PRAETIRVIL
NELSRLASHL VFLGTGLLDL GALTPFFYAF RERETILDLF EWVTGQRFHH NYIRIGGVKE
DLPEEFVPEL KKLLEVLPHR IDEYEALFAE SPIFYERARG VGVIPPEVAI DLGLTGGSLR
ASGVNYDVRK AYPYSGYETY TFDVPLGERG DVFDRMLVRI REMRESVKII KQALERLEPG
PVRDPNPQIT PPPRHLLETS MEAVIYHFKH YTEGFHPPKG EVYVPTESAR GELGYYIVSD
GGSMPYRVKV RAPSFVNLQS LPYACKGEQV PDMVAIIASL DPVMGDVDR
