ID   NUOH_ACIC1              Reviewed;         451 AA.
AC   A0LRI8;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=NADH-quinone oxidoreductase subunit H {ECO:0000255|HAMAP-Rule:MF_01350};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01350};
DE   AltName: Full=NADH dehydrogenase I subunit H {ECO:0000255|HAMAP-Rule:MF_01350};
DE   AltName: Full=NDH-1 subunit H {ECO:0000255|HAMAP-Rule:MF_01350};
GN   Name=nuoH {ECO:0000255|HAMAP-Rule:MF_01350}; OrderedLocusNames=Acel_0274;
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
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 believed to be
CC       ubiquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient. This subunit may bind ubiquinone.
CC       {ECO:0000255|HAMAP-Rule:MF_01350}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01350};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoA, H,
CC       J, K, L, M, N constitute the membrane sector of the complex.
CC       {ECO:0000255|HAMAP-Rule:MF_01350}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01350};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01350}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01350}.
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DR   EMBL; CP000481; ABK52048.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0LRI8; -.
DR   SMR; A0LRI8; -.
DR   STRING; 351607.Acel_0274; -.
DR   EnsemblBacteria; ABK52048; ABK52048; Acel_0274.
DR   KEGG; ace:Acel_0274; -.
DR   eggNOG; COG1005; Bacteria.
DR   HOGENOM; CLU_015134_0_0_11; -.
DR   OMA; WSGWASN; -.
DR   Proteomes; UP000008221; 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:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_01350; NDH1_NuoH; 1.
DR   InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO.
DR   InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS.
DR   PANTHER; PTHR11432; PTHR11432; 1.
DR   Pfam; PF00146; NADHdh; 1.
DR   PROSITE; PS00667; COMPLEX1_ND1_1; 1.
DR   PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; NAD; Quinone; Reference proteome; Translocase;
KW   Transmembrane; Transmembrane helix; Ubiquinone.
FT   CHAIN           1..451
FT                   /note="NADH-quinone oxidoreductase subunit H"
FT                   /id="PRO_0000298786"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        336..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ   SEQUENCE   451 AA;  48976 MW;  D5C539FDBA893F83 CRC64;
     MTVTTLGHPL APVFAAAPLS PPTHRDIWWL IIVKTLGVFA FLVLATLFMI WAERRVVARM
     QQRIGPNRVG PFGLLQSLAD GLKLALKEDI VPTLADKAVF ILAPVISATP AFLAFAVIPF
     GPTVSIAGHH TNLQLTDLPV AVLFVLAMSS LGVYGIVLAG WSSGSPYPLL GGVRSAAQVV
     SYEIAMGLSF VGVFLYSGSL STSDIVAAQA HRWGILWAGV SFAVYAIAMV GETNRAPFDL
     PEGETEIVGG FHTEYTSLKF ALFYLAEYIN MVTVSALMTT LFLGGWRAPW PLSLWSQANV
     GWWPVLWFLI KLGIVLFVFI WLRGTLPRFR YDQFMQFGWK VLIPVNLTWI LVEAAIRVVN
     VSNWRVWVIP FAIFLALVAV GTYVADLVRQ RSEVGDGGPI LGPALVPNPD SPYPIPPLPG
     QRPLVGVLEA RTDDFPVGSA AEPRNGGDGD A