NQO12_THET8
ID NQO12_THET8 Reviewed; 606 AA.
AC Q56227; Q5SM48;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=NADH-quinone oxidoreductase subunit 12;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I chain 12;
DE AltName: Full=NDH-1 subunit 12;
GN Name=nqo12; OrderedLocusNames=TTHA0095;
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 5 family. {ECO:0000305}.
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DR EMBL; U52917; AAA97949.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD69918.1; -; Genomic_DNA.
DR PIR; T11909; T11909.
DR RefSeq; WP_011227705.1; NC_006461.1.
DR RefSeq; YP_143361.1; NC_006461.1.
DR PDB; 4HE8; X-ray; 3.30 A; F/L=1-606.
DR PDB; 4HEA; X-ray; 3.30 A; L/T=1-606.
DR PDB; 6I0D; X-ray; 3.60 A; L/T=1-606.
DR PDB; 6I1P; X-ray; 3.21 A; L/T=1-606.
DR PDB; 6Q8O; X-ray; 3.60 A; L/T=1-606.
DR PDB; 6Q8W; X-ray; 3.40 A; L/T=1-606.
DR PDB; 6Q8X; X-ray; 3.51 A; L/T=1-606.
DR PDB; 6Y11; X-ray; 3.11 A; L/T=1-606.
DR PDB; 6ZIY; EM; 4.25 A; L=1-606.
DR PDB; 6ZJL; EM; 4.30 A; L=1-606.
DR PDB; 6ZJN; EM; 6.10 A; L=1-606.
DR PDB; 6ZJY; EM; 5.50 A; L=1-606.
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; Q56227; -.
DR SMR; Q56227; -.
DR DIP; DIP-59270N; -.
DR IntAct; Q56227; 1.
DR STRING; 300852.55771477; -.
DR TCDB; 3.D.1.3.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAD69918; BAD69918; BAD69918.
DR GeneID; 3169613; -.
DR KEGG; ttj:TTHA0095; -.
DR PATRIC; fig|300852.9.peg.93; -.
DR eggNOG; COG1009; Bacteria.
DR HOGENOM; CLU_007100_6_0_0; -.
DR OMA; LIGFWQH; -.
DR PhylomeDB; Q56227; -.
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; IPR018393; NADHpl_OxRdtase_5_subgr.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
DR PANTHER; PTHR42829; PTHR42829; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR TIGRFAMs; TIGR01974; NDH_I_L; 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..606
FT /note="NADH-quinone oxidoreductase subunit 12"
FT /id="PRO_0000118212"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 2..19
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 27..49
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 71..94
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6I1P"
FT HELIX 101..119
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 124..142
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 150..178
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:4HE8"
FT HELIX 185..192
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 199..216
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 234..241
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 264..283
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 291..311
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 315..342
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 362..374
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 380..394
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:4HE8"
FT HELIX 400..425
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:4HE8"
FT HELIX 440..455
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 469..473
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 489..514
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 519..529
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 534..541
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 543..580
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 586..603
FT /evidence="ECO:0007829|PDB:6Y11"
SQ SEQUENCE 606 AA; 65141 MW; 47318E8F2665295C CRC64;
MALLGTILLP LLGFALLGLF GKRMREPLPG VLASGLVLAS FLLGAGLLLS GGARFQAEWL
PGIPFSLLLD NLSGFMLLIV TGVGFLIHVY AIGYMGGDPG YSRFFAYFNL FIAMMLTLVL
ADSYPVMFIG WEGVGLASFL LIGFWYKNPQ YADSARKAFI VNRIGDLGFM LGMAILWALY
GTLSISELKE AMEGPLKNPD LLALAGLLLF LGAVGKSAQI PLMVWLPDAM AGPTPVSALI
HAATMVTAGV YLIARSSFLY SVLPDVSYAI AVVGLLTAAY GALSAFGQTD IKKIVAYSTI
SQLGYMFLAA GVGAYWVALF HVFTHAFFKA LLFLASGSVI HALGGEQDVR KMGGLWKHLP
QTRWHALIGA LALGGLPLLS GFWSKDAILA ATLTYPFGGV GFYVGALLVA VLTAMYAMRW
FVLVFLGEER GHHHPHEAPP VMLWPNHLLA LGSVLAGYLA LPHPLPNVLE PFLKPALAEV
EAHHLSLGAE WGLIALSAAV ALLGLWAGFV FFQRKVFPAW YLAFEAASRE AFYVDRAYNA
LIVNPLKALA EALFYGDRGL LSGYFGLGGA ARSLGQGLAR LQTGYLRVYA LLFVLGALLL
LGVMRW
