ID   NUOH_NITSB              Reviewed;         330 AA.
AC   A6Q1Q1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=NIS_0296;
OS   Nitratiruptor sp. (strain SB155-2).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC   Nitratiruptoraceae; Nitratiruptor; unclassified Nitratiruptor.
OX   NCBI_TaxID=387092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB155-2;
RX   PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA   Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA   Horikoshi K.;
RT   "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT   emergence of pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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 inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01350}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       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; AP009178; BAF69410.1; -; Genomic_DNA.
DR   RefSeq; WP_012081673.1; NC_009662.1.
DR   AlphaFoldDB; A6Q1Q1; -.
DR   SMR; A6Q1Q1; -.
DR   STRING; 387092.NIS_0296; -.
DR   EnsemblBacteria; BAF69410; BAF69410; NIS_0296.
DR   KEGG; nis:NIS_0296; -.
DR   eggNOG; COG1005; Bacteria.
DR   HOGENOM; CLU_015134_0_1_7; -.
DR   OMA; WSGWASN; -.
DR   OrthoDB; 1559067at2; -.
DR   Proteomes; UP000001118; 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.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Ubiquinone.
FT   CHAIN           1..330
FT                   /note="NADH-quinone oxidoreductase subunit H"
FT                   /id="PRO_1000086945"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ   SEQUENCE   330 AA;  36200 MW;  5938A45E23EF5C29 CRC64;
     MDAAFVIATI IKILIVLGLF SALAGFGTYV ERKVLAFMQR RLGPMHVGPY GLLQVLADGI
     KLFTKEDFIP QGAVRPVFMI APVITAATAF IAMAAIPMFP EFTIGGYTVK PIISDINVGL
     LFVLGVMAAG LYGPLLAGMS SGNKWALLGA ARTAIQFLSY EVVTGLSVLA PVMIVGSISL
     VDFNNYQAGG MGNWLIWKQP LAFVLFLIAG YAETNRTPFD LLEHEAEVIS GYATEYSGMR
     WGMFFIGEYA NMFTIGFLVS LIFLGGFNDW GFIPGAIAIL IKVFFFFFLF LWTRASWPHV
     RPDQLMWLCW KVLMPLAVIN VVITGIVMSI