ID   NUOH_VEREI              Reviewed;         360 AA.
AC   A1WLN7;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=Veis_2806;
OS   Verminephrobacter eiseniae (strain EF01-2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Verminephrobacter.
OX   NCBI_TaxID=391735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF01-2;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000542; ABM58544.1; -; Genomic_DNA.
DR   RefSeq; WP_011810541.1; NC_008786.1.
DR   AlphaFoldDB; A1WLN7; -.
DR   SMR; A1WLN7; -.
DR   STRING; 391735.Veis_2806; -.
DR   EnsemblBacteria; ABM58544; ABM58544; Veis_2806.
DR   KEGG; vei:Veis_2806; -.
DR   eggNOG; COG1005; Bacteria.
DR   HOGENOM; CLU_015134_0_1_4; -.
DR   OMA; MYVGMGI; -.
DR   OrthoDB; 1559067at2; -.
DR   Proteomes; UP000000374; 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 inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Ubiquinone.
FT   CHAIN           1..360
FT                   /note="NADH-quinone oxidoreductase subunit H"
FT                   /id="PRO_0000298856"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        130..150
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        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        297..317
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"
SQ   SEQUENCE   360 AA;  39568 MW;  4E9444E0176C43DC CRC64;
     MIDALYQAGL QLLPGGWWTG MVWPVLWILL KIVALLIPLM GAVAYLTLWE RKLLGFMQVR
     HGPNRVGPWG LLQPIADALK LLTKEIIQPT AASRGLFVLG PVMAIMPALA AWVVIPFGPD
     VALANVNAGL LLVMAITSIE VYGVIIAGWA SNSKYAFLGA LRASAQMVSY EIAMGFCLLI
     VIMVSGSMNL TEIVLAQGRG VAAANGIGFL SWNWLPLLPV FLVYLISGVA ETNRHPFDVV
     EGEAEIVAGH MVEYSGMGFA IFFLAEYASM WLVSILAALM FLGGWLPPVD SASLHWIPGW
     IWLGIKTCLV VSMFIWIRAT FPRFRYDQIM RLGWKIFIPV TLACLLIAGG WLLSPWNIWK