NUOI_ECOLI
ID NUOI_ECOLI Reviewed; 180 AA.
AC P0AFD6; P33604; P76488; P78183;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=NADH-quinone oxidoreductase subunit I;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunit I;
DE AltName: Full=NDH-1 subunit I;
DE AltName: Full=NUO9;
GN Name=nuoI; OrderedLocusNames=b2281, JW2276;
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 PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP PROTEIN SEQUENCE OF 1-4.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7607227; DOI=10.1111/j.1432-1033.1995.tb20594.x;
RA Leif H., Sled V.D., Ohnishi T., Weiss H., Friedrich T.;
RT "Isolation and characterization of the proton-translocating NADH:
RT ubiquinone oxidoreductase from Escherichia coli.";
RL Eur. J. Biochem. 230:538-548(1995).
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.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250};
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X68301; CAA48368.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75341.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16109.2; -; Genomic_DNA.
DR PIR; G64999; G64999.
DR RefSeq; NP_416784.1; NC_000913.3.
DR RefSeq; WP_000172749.1; NZ_STEB01000008.1.
DR PDB; 7NYR; EM; 3.30 A; I=1-180.
DR PDB; 7NYU; EM; 3.80 A; I=1-180.
DR PDB; 7NYV; EM; 3.70 A; I=1-180.
DR PDB; 7NZ1; EM; 2.10 A; I=1-180.
DR PDBsum; 7NYR; -.
DR PDBsum; 7NYU; -.
DR PDBsum; 7NYV; -.
DR PDBsum; 7NZ1; -.
DR AlphaFoldDB; P0AFD6; -.
DR SMR; P0AFD6; -.
DR BioGRID; 4260510; 80.
DR ComplexPortal; CPX-243; Respiratory chain complex I.
DR DIP; DIP-35918N; -.
DR IntAct; P0AFD6; 8.
DR STRING; 511145.b2281; -.
DR TCDB; 3.D.1.1.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR jPOST; P0AFD6; -.
DR PaxDb; P0AFD6; -.
DR PRIDE; P0AFD6; -.
DR EnsemblBacteria; AAC75341; AAC75341; b2281.
DR EnsemblBacteria; BAA16109; BAA16109; BAA16109.
DR GeneID; 67416711; -.
DR GeneID; 946757; -.
DR KEGG; ecj:JW2276; -.
DR KEGG; eco:b2281; -.
DR PATRIC; fig|511145.12.peg.2374; -.
DR EchoBASE; EB2013; -.
DR eggNOG; COG1143; Bacteria.
DR HOGENOM; CLU_067218_4_3_6; -.
DR InParanoid; P0AFD6; -.
DR OMA; RGDLYYT; -.
DR PhylomeDB; P0AFD6; -.
DR BioCyc; EcoCyc:NUOI-MON; -.
DR BioCyc; MetaCyc:NUOI-MON; -.
DR PRO; PR:P0AFD6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; 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_01351; NDH1_NuoI; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR PANTHER; PTHR10849; PTHR10849; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR TIGRFAMs; TIGR01971; NuoI; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding; NAD;
KW Quinone; Reference proteome; Repeat; Translocase; Ubiquinone.
FT CHAIN 1..180
FT /note="NADH-quinone oxidoreductase subunit I"
FT /id="PRO_0000118722"
FT DOMAIN 50..80
FT /note="4Fe-4S ferredoxin-type 1"
FT DOMAIN 90..119
FT /note="4Fe-4S ferredoxin-type 2"
FT BINDING 60
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 24..29
FT /note="AFAKRE -> GSPNQ (in Ref. 1; CAA48368)"
FT /evidence="ECO:0000305"
FT CONFLICT 165..175
FT /note="EAENEAKPIDV -> DRRTKPSLSTF (in Ref. 1; CAA48368)"
FT /evidence="ECO:0000305"
FT HELIX 24..28
FT /evidence="ECO:0007829|PDB:7NYR"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:7NZ1"
SQ SEQUENCE 180 AA; 20538 MW; B31860402432C171 CRC64;
MTLKELLVGF GTQVRSIWMI GLHAFAKRET RMYPEEPVYL PPRYRGRIVL TRDPDGEERC
VACNLCAVAC PVGCISLQKA ETKDGRWYPE FFRINFSRCI FCGLCEEACP TTAIQLTPDF
EMGEYKRQDL VYEKEDLLIS GPGKYPEYNF YRMAGMAIDG KDKGEAENEA KPIDVKSLLP
