NUOH_CUPMC
ID NUOH_CUPMC Reviewed; 354 AA.
AC Q1LPV6;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=Rmet_0934;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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; CP000352; ABF07820.1; -; Genomic_DNA.
DR RefSeq; WP_008643351.1; NC_007973.1.
DR AlphaFoldDB; Q1LPV6; -.
DR SMR; Q1LPV6; -.
DR STRING; 266264.Rmet_0934; -.
DR EnsemblBacteria; ABF07820; ABF07820; Rmet_0934.
DR GeneID; 60825421; -.
DR KEGG; rme:Rmet_0934; -.
DR eggNOG; COG1005; Bacteria.
DR HOGENOM; CLU_015134_0_1_4; -.
DR OMA; WSGWASN; -.
DR OrthoDB; 1559067at2; -.
DR Proteomes; UP000002429; 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; 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..354
FT /note="NADH-quinone oxidoreductase subunit H"
FT /id="PRO_0000298845"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ SEQUENCE 354 AA; 39832 MW; 050437429E602684 CRC64;
MIDWITSQGH DIFGMYWTPL WILIRAVLIV VPVLLCVAYL ILWERKLIGW MHVRIGPNRV
GPLGLLQPIA DVLKLLLKEV MFPSQINRGM YLVAPLMVLM PAVAVWAVIP FQAEVVMADI
NAGLLYVMAI SSVGVYGVIL AGWASNSKYA FIGAMRAAAQ MVSYEIAMGF ALVTVLMVSG
SLNLSHIVNA QNTGYFANMG LNLLSWNWLP LLPMFGVYFI SGVAETNRHP FDVVEGESEI
VAGHMIEYSG MTFALFFLAE YINMIIISTM TSLMFLGGWA PPFSSALTNA IPGFFWLVIK
VFLLLSVFIW IRASFPRYRY DQIMRLGWKI FIPLTVAWLI IVAIWIKSPW NIWH
