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 02-SEP-2026, entry version 146. 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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; 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 + NADH + 5 H(+)(in) = a quinol + NAD(+) + 4 CC H(+)(out); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC 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_CP009789.1. DR PDB; 7AWT; EM; 2.73 A; I=1-180. 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 PDB; 7P61; EM; 3.20 A; I=34-180. DR PDB; 7P62; EM; 3.60 A; I=37-180. DR PDB; 7P63; EM; 3.40 A; I=1-180. DR PDB; 7P64; EM; 2.50 A; I=1-180. DR PDB; 7P69; EM; 3.00 A; I=36-180. DR PDB; 7P7C; EM; 2.40 A; I=1-180. DR PDB; 7P7E; EM; 2.70 A; I=36-180. DR PDB; 7P7J; EM; 2.70 A; I=1-180. DR PDB; 7P7K; EM; 3.10 A; I=32-180. DR PDB; 7P7L; EM; 3.00 A; I=1-180. DR PDB; 7P7M; EM; 3.20 A; I=1-180. DR PDB; 7Z7R; EM; 3.36 A; I=1-180. DR PDB; 7Z7S; EM; 2.40 A; I=1-180. DR PDB; 7Z7T; EM; 3.10 A; I=1-180. DR PDB; 7Z7V; EM; 2.29 A; I=1-180. DR PDB; 7Z80; EM; 2.93 A; I=1-180. DR PDB; 7Z83; EM; 2.88 A; I=1-180. DR PDB; 7Z84; EM; 2.87 A; I=1-180. DR PDB; 7ZC5; EM; 3.00 A; I=1-180. DR PDB; 7ZCI; EM; 2.69 A; I=1-180. DR PDB; 9Q8I; EM; 2.35 A; I=1-180. DR PDB; 9TAJ; EM; 3.00 A; I=1-180. DR PDB; 9TAL; EM; 2.66 A; I=1-180. DR PDB; 9TAM; EM; 2.96 A; I=1-180. DR PDB; 9TAN; EM; 2.59 A; I=1-180. DR AlphaFoldDB; P0AFD6; -. DR EMDB; EMD-12653; -. DR EMDB; EMD-12654; -. DR EMDB; EMD-12655; -. DR EMDB; EMD-12661; -. DR EMDB; EMD-52895; -. DR SMR; P0AFD6; -. DR BioGRID; 4260510; 86. DR ComplexPortal; CPX-243; Respiratory chain complex I. DR DIP; DIP-35918N; -. DR FunCoup; P0AFD6; 670. 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; 511145-b2281; -. DR EnsemblBacteria; AAC75341; AAC75341; b2281. DR GeneID; 67176149; -. DR GeneID; 89517116; -. DR GeneID; 946757; -. DR KEGG; ecj:JW2276; -. DR KEGG; eco:b2281; -. DR KEGG; ecoc:C3026_12730; -. 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; WYPDFFR; -. DR OrthoDB; 9808559at2; -. DR PhylomeDB; P0AFD6; -. DR BioCyc; EcoCyc:NUOI-MONOMER; -. DR BioCyc; MetaCyc:NUOI-MONOMER; -. DR PRO; PR:P0AFD6; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P0AFD6; -. 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:0045271; C:respiratory chain complex I; IDA:EcoCyc. 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) (non-electrogenic) activity; IEA:UniProtKB-UniRule. DR GO; GO:0009060; P:aerobic respiration; IMP:EcoCyc. DR GO; GO:0022904; P:respiratory electron transport chain; IDA:ComplexPortal. DR DisProt; DP03502; -. DR FunFam; 3.30.70.3270:FF:000002; NADH-quinone oxidoreductase subunit I; 1. DR Gene3D; 3.30.70.3270; -; 1. 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 NCBIfam; TIGR01971; NuoI; 1. DR NCBIfam; NF004536; PRK05888.1-1; 1. DR PANTHER; PTHR10849:SF20; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1. DR PANTHER; PTHR10849; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1. DR Pfam; PF12838; Fer4_7; 1. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. DR PDBsum; 7AWT; -. DR PDBsum; 7NYR; -. DR PDBsum; 7NYU; -. DR PDBsum; 7NYV; -. DR PDBsum; 7NZ1; -. DR PDBsum; 7P61; -. DR PDBsum; 7P62; -. DR PDBsum; 7P63; -. DR PDBsum; 7P64; -. DR PDBsum; 7P69; -. DR PDBsum; 7P7C; -. DR PDBsum; 7P7E; -. DR PDBsum; 7P7J; -. DR PDBsum; 7P7K; -. DR PDBsum; 7P7L; -. DR PDBsum; 7P7M; -. DR PDBsum; 7Z7R; -. DR PDBsum; 7Z7S; -. DR PDBsum; 7Z7T; -. DR PDBsum; 7Z7V; -. DR PDBsum; 7Z80; -. DR PDBsum; 7Z83; -. DR PDBsum; 7Z84; -. DR PDBsum; 7ZC5; -. DR PDBsum; 7ZCI; -. DR PDBsum; 9Q8I; -. DR PDBsum; 9TAJ; -. DR PDBsum; 9TAL; -. DR PDBsum; 9TAM; -. DR PDBsum; 9TAN; -. 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 3..24 FT /evidence="ECO:0007829|PDB:7Z7V" FT HELIX 30..32 FT /evidence="ECO:0007829|PDB:7NYR" FT TURN 33..35 FT /evidence="ECO:0007829|PDB:7Z7V" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:7Z7V" 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 83..85 FT /evidence="ECO:0007829|PDB:7AWT" 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 120..122 FT /evidence="ECO:0007829|PDB:7AWT" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:7Z7V" 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" FT STRAND 154..156 FT /evidence="ECO:0007829|PDB:7P7J" FT HELIX 170..172 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 //