ID   NUOH_MYCBP              Reviewed;         410 AA.
AC   A1KNE8;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=BCG_3175;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(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       menaquinone. 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 (By similarity).
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; AM408590; CAL73164.1; -; Genomic_DNA.
DR   RefSeq; WP_003416445.1; NC_008769.1.
DR   AlphaFoldDB; A1KNE8; -.
DR   SMR; A1KNE8; -.
DR   PRIDE; A1KNE8; -.
DR   GeneID; 45427139; -.
DR   KEGG; mbb:BCG_3175; -.
DR   HOGENOM; CLU_015134_0_0_11; -.
DR   OMA; WSGWASN; -.
DR   Proteomes; UP000001472; 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; Translocase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..410
FT                   /note="NADH-quinone oxidoreductase subunit H"
FT                   /id="PRO_0000298827"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   REGION          376..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   410 AA;  44658 MW;  8D3B863AA0B48BBD CRC64;
     MTTFGHDTWW LVAAKAIAVF VFLMLTVLVA ILAERKLLGR MQLRPGPNRV GPKGALQSLA
     DGIKLALKES ITPGGIDRFV YFVAPIISVI PAFTAFAFIP FGPEVSVFGH RTPLQITDLP
     VAVLFILGLS AIGVYGIVLG GWASGSTYPL LGGVRSTAQV ISYEVAMGLS FATVFLMAGT
     MSTSQIVAAQ DGVWYAFLLL PSFVIYLISM VGETNRAPFD LPEAEGELVA GFHTEYSSLK
     FAMFMLAEYV NMTTVSALAA TLFFGGWHAP WPLNMWASAN TGWWPLIWFT AKVWGFLFIY
     FWLRATLPRL RYDQFMALGW KLLIPVSLVW VMVAAIIRSL RNQGYQYWTP TLVFSSIVVA
     AAMVLLLRKP LSAPGARASA RQRGDEGTSP EPAFPTPPLL AGATKENAGG