NUOH_LEGPH
ID NUOH_LEGPH Reviewed; 340 AA.
AC Q5ZRU5;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=lpg2782;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
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; AE017354; AAU28832.1; -; Genomic_DNA.
DR RefSeq; WP_010948471.1; NC_002942.5.
DR RefSeq; YP_096779.1; NC_002942.5.
DR AlphaFoldDB; Q5ZRU5; -.
DR SMR; Q5ZRU5; -.
DR STRING; 272624.lpg2782; -.
DR PaxDb; Q5ZRU5; -.
DR PRIDE; Q5ZRU5; -.
DR DNASU; 3079953; -.
DR EnsemblBacteria; AAU28832; AAU28832; lpg2782.
DR GeneID; 66491954; -.
DR KEGG; lpn:lpg2782; -.
DR PATRIC; fig|272624.6.peg.2963; -.
DR eggNOG; COG1005; Bacteria.
DR HOGENOM; CLU_015134_0_1_6; -.
DR OMA; MYVGMGI; -.
DR Proteomes; UP000000609; 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..340
FT /note="NADH-quinone oxidoreductase subunit H"
FT /id="PRO_0000240083"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 78..98
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 151..171
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 244..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; 37996 MW; 7F11A8E72E0DE83B CRC64;
MLHTIGILIW IIIKILVIVV PLLISVAYLT YAERKVIGYI QVRIGPNRVG LKGLLQPFAD
LLKLITKEII VPTRSNKYLF VIAPLFALVP SLVGWAVIPF QEGIVLANIN AGVLYLFAMS
SLGVYGVLIA GWASNSKYAM FGALRSTAQT VSYEIAMGFA LVGVLLAAGS MNLTDIVNSQ
KGGMLHWWFI PLLPLFLVFW ISGIAETNRA PFDLAEGESE IVAGFHVEYS GIGFALFFLS
EYASMILIST VLAILFMGGW LSPFEGITFL DQIFFIVPGF VWLLLKISFF LFVYLWVRAT
FPRYRYDQLM RLGWKVLIPV TIVWLIVTAL MVVAHVKPWF
