ID   NUOH_LEPBJ              Reviewed;         346 AA.
AC   Q04V66;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=LBJ_0507;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB197;
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA   Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA   Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000350; ABJ75204.1; -; Genomic_DNA.
DR   RefSeq; WP_002735619.1; NC_008510.1.
DR   AlphaFoldDB; Q04V66; -.
DR   SMR; Q04V66; -.
DR   EnsemblBacteria; ABJ75204; ABJ75204; LBJ_0507.
DR   GeneID; 61172704; -.
DR   KEGG; lbj:LBJ_0507; -.
DR   HOGENOM; CLU_015134_0_1_12; -.
DR   OMA; MYVGMGI; -.
DR   Proteomes; UP000000656; Chromosome 1.
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; 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..346
FT                   /note="NADH-quinone oxidoreductase subunit H"
FT                   /id="PRO_0000298820"
FT   TRANSMEM        6..26
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        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ   SEQUENCE   346 AA;  39039 MW;  76852B49ABCF2272 CRC64;
     MNWNEILFWL LKSGLFFFIL ITACAYYTLA ERKVAGFIQD RKGPNRAGIW GLLQPLADGI
     KFLTKEEVFP TQVNKIMYLI APAISMTCAI MAWSVVPLGG RIPLPQWLQD RTGLVFLDLQ
     IANPDTGILF LFAISSLAVY GIIIAGWASN NKYSLLGAIR STAQMISYEL PLSMSVVSIV
     ILTGSLKLTD ISASQAGLWN IFKLPGFIAF CLFVVAMFAE TNRLPFDLAE AESELVVGFH
     TEYGAFKFAL FFIAEYMNMI TMSCVVTLLF FGGYQVPFGI LEGHVLQSLF GLFFFLGKVL
     FFTFLFVWVR WTLPRFRYDQ LMSLGWKKLI PWAVLNILIA SLYIQF