NQO13_THET8
ID NQO13_THET8 Reviewed; 469 AA.
AC Q56228; Q5SM47;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=NADH-quinone oxidoreductase subunit 13;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I chain 13;
DE AltName: Full=NDH-1 subunit 13;
GN Name=nqo13; OrderedLocusNames=TTHA0096;
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.
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 4 family. {ECO:0000305}.
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DR EMBL; U52917; AAA97950.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD69919.1; -; Genomic_DNA.
DR PIR; T11910; T11910.
DR RefSeq; WP_011227706.1; NC_006461.1.
DR RefSeq; YP_143362.1; NC_006461.1.
DR PDB; 4HE8; X-ray; 3.30 A; G/M=1-469.
DR PDB; 4HEA; X-ray; 3.30 A; M/U=1-469.
DR PDB; 6I0D; X-ray; 3.60 A; M/U=1-469.
DR PDB; 6I1P; X-ray; 3.21 A; M/U=1-469.
DR PDB; 6Q8O; X-ray; 3.60 A; M/U=1-469.
DR PDB; 6Q8W; X-ray; 3.40 A; M/U=1-469.
DR PDB; 6Q8X; X-ray; 3.51 A; M/U=1-469.
DR PDB; 6Y11; X-ray; 3.11 A; M/U=1-469.
DR PDB; 6ZIY; EM; 4.25 A; M=1-469.
DR PDB; 6ZJL; EM; 4.30 A; M=1-469.
DR PDB; 6ZJN; EM; 6.10 A; M=1-469.
DR PDB; 6ZJY; EM; 5.50 A; M=1-469.
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; Q56228; -.
DR SMR; Q56228; -.
DR DIP; DIP-59271N; -.
DR IntAct; Q56228; 1.
DR STRING; 300852.55771478; -.
DR TCDB; 3.D.1.3.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAD69919; BAD69919; BAD69919.
DR GeneID; 3169618; -.
DR KEGG; ttj:TTHA0096; -.
DR PATRIC; fig|300852.9.peg.94; -.
DR eggNOG; COG1008; Bacteria.
DR HOGENOM; CLU_007100_4_4_0; -.
DR OMA; ITRWGNQ; -.
DR PhylomeDB; Q56228; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR PANTHER; PTHR43507; PTHR43507; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
DR TIGRFAMs; TIGR01972; NDH_I_M; 1.
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..469
FT /note="NADH-quinone oxidoreductase subunit 13"
FT /id="PRO_0000118038"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 166
FT /note="A -> D (in Ref. 1; AAA97950)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="A -> D (in Ref. 1; AAA97950)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="A -> D (in Ref. 1; AAA97950)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="A -> D (in Ref. 1; AAA97950)"
FT /evidence="ECO:0000305"
FT HELIX 2..17
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 23..40
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 69..87
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 96..111
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:6I1P"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 141..168
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 190..203
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:6Q8W"
FT HELIX 214..220
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 250..277
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 281..301
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 305..336
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 354..366
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 373..387
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 389..395
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 399..413
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:4HE8"
FT HELIX 427..445
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 447..453
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 454..463
FT /evidence="ECO:0007829|PDB:6Y11"
SQ SEQUENCE 469 AA; 49219 MW; 5FD2D14713790224 CRC64;
MVVLAVLLPV VFGALLLLGL PRALGVLGAG LSFLLNLYLF LTHPGGVAHA FQAPLLPGAG
VYWAFGLDGL SALFFLTIAL TVFLGALVAR VEGRFLGLAL LMEGLLLGLF AARDLLVFYV
FFEAALIPAL LMLYLYGGEG RTRALYTFVL FTLVGSLPML AAVLGARLLS GSPTFLLEDL
LAHPLQEEAA FWVFLGFALA FAIKTPLFPL HAWLPPFHQE NHPSGLADAL GTLYKVGVFA
FFRFAIPLAP EGFAQAQGLL LFLAALSALY GAWVAFAAKD FKTLLAYAGL SHMGVAALGV
FSGTPEGAMG GLYLLAASGV YTGGLFLLAG RLYERTGTLE IGRYRGLAQS APGLAALALI
LFLAMVGLPG LSGFPGEFLT LLGAYKASPW LAALAFLSVI ASAAYALTAF QKTFWEEGGS
GVKDLAGAEW GFALLSVLAL LLMGVFPGYF ARGLHPLAEA FAKLLGGGA
