NUOH_ECOLI
ID NUOH_ECOLI Reviewed; 325 AA.
AC P0AFD4; P33603; P78307;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=NADH-quinone oxidoreductase subunit H;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunit H;
DE AltName: Full=NDH-1 subunit H;
DE AltName: Full=NUO8;
GN Name=nuoH; OrderedLocusNames=b2282, JW2277;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / AN387;
RX PubMed=7690854; DOI=10.1006/jmbi.1993.1488;
RA Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H.;
RT "The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase
RT in Escherichia coli. Organization of the 14 genes and relationship between
RT the derived proteins and subunits of mitochondrial complex I.";
RL J. Mol. Biol. 233:109-122(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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 -!- 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 -!- 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 -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. {ECO:0000305}.
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DR EMBL; X68301; CAA48367.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75342.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16110.1; -; Genomic_DNA.
DR PIR; H64999; H64999.
DR RefSeq; NP_416785.1; NC_000913.3.
DR RefSeq; WP_000118507.1; NZ_STEB01000008.1.
DR PDB; 7NYH; EM; 3.60 A; H=1-325.
DR PDB; 7NYR; EM; 3.30 A; H=1-325.
DR PDB; 7NYU; EM; 3.80 A; H=1-325.
DR PDB; 7NYV; EM; 3.70 A; H=1-325.
DR PDBsum; 7NYH; -.
DR PDBsum; 7NYR; -.
DR PDBsum; 7NYU; -.
DR PDBsum; 7NYV; -.
DR AlphaFoldDB; P0AFD4; -.
DR SMR; P0AFD4; -.
DR BioGRID; 4260511; 40.
DR ComplexPortal; CPX-243; Respiratory chain complex I.
DR IntAct; P0AFD4; 1.
DR STRING; 511145.b2282; -.
DR TCDB; 3.D.1.1.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR jPOST; P0AFD4; -.
DR PaxDb; P0AFD4; -.
DR PRIDE; P0AFD4; -.
DR DNASU; 946761; -.
DR EnsemblBacteria; AAC75342; AAC75342; b2282.
DR EnsemblBacteria; BAA16110; BAA16110; BAA16110.
DR GeneID; 67416712; -.
DR GeneID; 946761; -.
DR KEGG; ecj:JW2277; -.
DR KEGG; eco:b2282; -.
DR PATRIC; fig|1411691.4.peg.4454; -.
DR EchoBASE; EB2012; -.
DR eggNOG; COG1005; Bacteria.
DR HOGENOM; CLU_015134_0_1_6; -.
DR InParanoid; P0AFD4; -.
DR OMA; WSGWASN; -.
DR PhylomeDB; P0AFD4; -.
DR BioCyc; EcoCyc:NUOH-MON; -.
DR BioCyc; MetaCyc:NUOH-MON; -.
DR PRO; PR:P0AFD4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0030964; C:NADH dehydrogenase complex; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IDA:EcoCyc.
DR GO; GO:0045271; C:respiratory chain complex I; IC:ComplexPortal.
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; IMP:EcoCyc.
DR GO; GO:0022904; P:respiratory electron transport chain; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000117523"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 35..36
FT /note="GE -> AK (in Ref. 1; CAA48367)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="G -> A (in Ref. 1; CAA48367)"
FT /evidence="ECO:0000305"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 81..96
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:7NYR"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 140..156
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 159..171
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:7NYR"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:7NYR"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:7NYR"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 232..255
FT /evidence="ECO:0007829|PDB:7NYR"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 267..288
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 294..299
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 305..320
FT /evidence="ECO:0007829|PDB:7NYR"
SQ SEQUENCE 325 AA; 36219 MW; 0648FD831E1B8FB0 CRC64;
MSWISPELIE ILLTILKAVV ILLVVVTCGA FMSFGERRLL GLFQNRYGPN RVGWGGSLQL
VADMIKMFFK EDWIPKFSDR VIFTLAPMIA FTSLLLAFAI VPVSPGWVVA DLNIGILFFL
MMAGLAVYAV LFAGWSSNNK YSLLGAMRAS AQTLSYEVFL GLSLMGVVAQ AGSFNMTDIV
NSQAHVWNVI PQFFGFITFA IAGVAVCHRH PFDQPEAEQE LADGYHIEYS GMKFGLFFVG
EYIGIVTISA LMVTLFFGGW QGPLLPPFIW FALKTAFFMM MFILIRASLP RPRYDQVMSF
GWKICLPLTL INLLVTAAVI LWQAQ
