ID   NUOH_COXB2              Reviewed;         340 AA.
AC   B6IZ52;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=CbuG_0567;
OS   Coxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=434923;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CbuG_Q212;
RX   PubMed=19047403; DOI=10.1128/iai.01141-08;
RA   Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA   Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA   Heinzen R.A.;
RT   "Comparative genomics reveal extensive transposon-mediated genomic
RT   plasticity and diversity among potential effector proteins within the genus
RT   Coxiella.";
RL   Infect. Immun. 77:642-656(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 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; CP001019; ACJ17980.1; -; Genomic_DNA.
DR   RefSeq; WP_012569820.1; NC_011527.1.
DR   AlphaFoldDB; B6IZ52; -.
DR   SMR; B6IZ52; -.
DR   KEGG; cbg:CbuG_0567; -.
DR   HOGENOM; CLU_015134_0_1_6; -.
DR   OMA; MYVGMGI; -.
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 inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW   Transmembrane; Transmembrane helix; Ubiquinone.
FT   CHAIN           1..340
FT                   /note="NADH-quinone oxidoreductase subunit H"
FT                   /id="PRO_1000143586"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        221..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        245..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ   SEQUENCE   340 AA;  38027 MW;  8A6D9A55D63FAAF4 CRC64;
     MTDQLITLIW IIIKIVLILV PLLVAVAFIT LAERKVIGYM QSRVGPNRVG FRGLAQPIAD
     IFKLLLKEVI IPTASSRYLY LIAPILSLVP ALAAWAVIPF AQGWMLANVN AGLLFLFAMT
     SLGVYGILVA GWASNSKYAF FGALRSAAQV VSYEIPMGFA LVGVLLAAGT MNLQGIVLRQ
     SGGLWHWFWL PLLPLFVTYW ITAVAETNRA PFDVAEGESE IVAGFHVEYA GVTFALFFLA
     EYANMVLVSA IATVIFLGGW LSPFQGIPGL ESLFAWVPGI VWFVLKLSLF IFTYFWMRAT
     FPRYRYDQIM RLCWKVLIPV TLVWIIILAL AIEFHWTHWL