NUOH_SALTY
ID NUOH_SALTY Reviewed; 325 AA.
AC Q60010;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 129.
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=STM2322;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=F98;
RX PubMed=9371470; DOI=10.1128/jb.179.22.7186-7190.1997;
RA Zhang-Barber L.Z., Turner A.K., Martin G., Fraenkel G., Dougan G.,
RA Barrow P.A.;
RT "Influence of genes encoding proton-translocating enzymes on suppression of
RT Salmonella typhimurium growth and colonization.";
RL J. Bacteriol. 179:7186-7190(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 13 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; L42521; AAC37140.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21223.1; -; Genomic_DNA.
DR RefSeq; NP_461264.1; NC_003197.2.
DR RefSeq; WP_000118515.1; NC_003197.2.
DR AlphaFoldDB; Q60010; -.
DR SMR; Q60010; -.
DR STRING; 99287.STM2322; -.
DR PaxDb; Q60010; -.
DR EnsemblBacteria; AAL21223; AAL21223; STM2322.
DR GeneID; 1253844; -.
DR GeneID; 66756771; -.
DR KEGG; stm:STM2322; -.
DR PATRIC; fig|99287.12.peg.2459; -.
DR HOGENOM; CLU_015134_0_1_6; -.
DR OMA; WSGWASN; -.
DR PhylomeDB; Q60010; -.
DR BioCyc; SENT99287:STM2322-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
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 GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
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..325
FT /note="NADH-quinone oxidoreductase subunit H"
FT /id="PRO_0000117525"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 50..69
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT CONFLICT 117
FT /note="L -> W (in Ref. 1; AAC37140)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="Q -> H (in Ref. 1; AAC37140)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="A -> T (in Ref. 1; AAC37140)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 36292 MW; 85A7F3A941EA873D CRC64;
MSWITPDLIE ILLSILKAVV ILLVVVTCGA FMSFGERRLL GLFQNRYGPN RVGWGGSLQL
VADMIKMFFK EDWIPKFSDR VIFTLAPMIA FTSLLLSFAI VPVSPNWVVA DLNIGILFFL
MMAGLAVYAV LFAGWSSNNK YSLLGAMRAS AQTVSYEVFL GLSLMGVVAQ AGSFNMTDIV
NNQAHLWNVI PQFFGFVTFA IAGVAVCHRH PFDQPEAEQE LADGYHIEYS GMKFGLFFVG
EYIGIVTVSA LMVTLFFGGW HGPFLPPFVW FALKTAFFMM MFILIRASLP RPRYDQVMSF
GWKVCLPLTL INLLVTAAVI LWQAQ
