ID NUOB_ECOLI Reviewed; 220 AA. AC P0AFC7; P33598; P78090; P78186; P78187; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 02-SEP-2026, entry version 141. DE RecName: Full=NADH-quinone oxidoreductase subunit B {ECO:0000255|HAMAP-Rule:MF_01356}; DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01356}; DE AltName: Full=NADH dehydrogenase I subunit B {ECO:0000255|HAMAP-Rule:MF_01356}; DE AltName: Full=NDH-1 subunit B {ECO:0000255|HAMAP-Rule:MF_01356}; DE AltName: Full=NUO2; GN Name=nuoB {ECO:0000255|HAMAP-Rule:MF_01356}; GN OrderedLocusNames=b2287, JW5875; 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], AND SEQUENCE REVISION. 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 1-6. 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 ubiquinone. Couples CC the redox reaction to proton translocation (for every two electrons CC transferred, four hydrogen ions are translocated across the cytoplasmic CC membrane), and thus conserves the redox energy 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; Evidence={ECO:0000255|HAMAP-Rule:MF_01356}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01356}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01356}; CC -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits NuoB, CD, CC E, F, and G constitute the peripheral sector of the complex. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; CC Cytoplasmic side. CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family. CC {ECO:0000255|HAMAP-Rule:MF_01356}. 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; CAA48361.1; -; Genomic_DNA. DR EMBL; U00096; AAC75347.1; -; Genomic_DNA. DR EMBL; AP009048; BAA16121.2; -; Genomic_DNA. DR PIR; E65000; E65000. DR RefSeq; NP_416790.1; NC_000913.3. DR RefSeq; WP_000386733.1; NZ_CP009789.1. DR RefSeq; WP_046608242.1; NZ_LN832404.1. DR PDB; 7AWT; EM; 2.73 A; B=1-220. DR PDB; 7NYR; EM; 3.30 A; B=1-220. DR PDB; 7NYU; EM; 3.80 A; B=1-220. DR PDB; 7NYV; EM; 3.70 A; B=1-220. DR PDB; 7NZ1; EM; 2.10 A; B=1-220. DR PDB; 7P61; EM; 3.20 A; B=1-220. DR PDB; 7P62; EM; 3.60 A; B=1-220. DR PDB; 7P63; EM; 3.40 A; B=1-220. DR PDB; 7P64; EM; 2.50 A; B=1-220. DR PDB; 7P69; EM; 3.00 A; B=1-220. DR PDB; 7P7C; EM; 2.40 A; B=1-220. DR PDB; 7P7E; EM; 2.70 A; B=1-220. DR PDB; 7P7J; EM; 2.70 A; B=1-220. DR PDB; 7P7K; EM; 3.10 A; B=1-220. DR PDB; 7P7L; EM; 3.00 A; B=1-220. DR PDB; 7P7M; EM; 3.20 A; B=1-220. DR PDB; 7Z7R; EM; 3.36 A; B=1-220. DR PDB; 7Z7S; EM; 2.40 A; B=1-220. DR PDB; 7Z7T; EM; 3.10 A; B=1-220. DR PDB; 7Z7V; EM; 2.29 A; B=1-220. DR PDB; 7Z80; EM; 2.93 A; B=1-220. DR PDB; 7Z83; EM; 2.88 A; B=1-220. DR PDB; 7Z84; EM; 2.87 A; B=1-220. DR PDB; 7ZC5; EM; 3.00 A; B=1-220. DR PDB; 7ZCI; EM; 2.69 A; B=1-220. DR PDB; 9Q8I; EM; 2.35 A; B=1-220. DR PDB; 9TAJ; EM; 3.00 A; B=1-220. DR PDB; 9TAK; EM; 2.80 A; B=1-220. DR PDB; 9TAL; EM; 2.66 A; B=1-220. DR PDB; 9TAM; EM; 2.96 A; B=1-220. DR PDB; 9TAN; EM; 2.59 A; B=1-220. DR AlphaFoldDB; P0AFC7; -. DR EMDB; EMD-12653; -. DR EMDB; EMD-12654; -. DR EMDB; EMD-12655; -. DR EMDB; EMD-12661; -. DR EMDB; EMD-52895; -. DR SMR; P0AFC7; -. DR BioGRID; 4262975; 66. DR ComplexPortal; CPX-243; Respiratory chain complex I. DR FunCoup; P0AFC7; 569. DR IntAct; P0AFC7; 1. DR STRING; 511145.b2287; -. DR TCDB; 3.D.1.1.1; the h+ or na+-translocating nadh dehydrogenase (ndh) family. DR jPOST; P0AFC7; -. DR PaxDb; 511145-b2287; -. DR EnsemblBacteria; AAC75347; AAC75347; b2287. DR GeneID; 67176143; -. DR GeneID; 93774887; -. DR GeneID; 946738; -. DR KEGG; ecj:JW5875; -. DR KEGG; eco:b2287; -. DR KEGG; ecoc:C3026_12760; -. DR PATRIC; fig|1411691.4.peg.4449; -. DR EchoBASE; EB2008; -. DR eggNOG; COG0377; Bacteria. DR HOGENOM; CLU_055737_7_3_6; -. DR InParanoid; P0AFC7; -. DR OMA; CGGPYWE; -. DR OrthoDB; 9786737at2; -. DR PhylomeDB; P0AFC7; -. DR BioCyc; EcoCyc:NUOB-MONOMER; -. DR BioCyc; MetaCyc:NUOB-MONOMER; -. DR PRO; PR:P0AFC7; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P0AFC7; -. 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:EcoliWiki. DR GO; GO:0045271; C:respiratory chain complex I; IDA:EcoCyc. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IMP: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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:InterPro. DR GO; GO:0009060; P:aerobic respiration; IMP:EcoCyc. DR GO; GO:0015990; P:electron transport coupled proton transport; IMP:EcoCyc. DR GO; GO:0022904; P:respiratory electron transport chain; IDA:ComplexPortal. DR DisProt; DP03500; -. DR FunFam; 3.40.50.12280:FF:000002; NADH-quinone oxidoreductase subunit B; 1. DR Gene3D; 3.40.50.12280; -; 1. DR HAMAP; MF_01356; NDH1_NuoB; 1. DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa. DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su. DR NCBIfam; TIGR01957; nuoB_fam; 1. DR NCBIfam; NF005012; PRK06411.1; 1. DR PANTHER; PTHR11995; NADH DEHYDROGENASE; 1. DR PANTHER; PTHR11995:SF14; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7, MITOCHONDRIAL; 1. DR Pfam; PF01058; Oxidored_q6; 1. DR SUPFAM; SSF56770; HydA/Nqo6-like; 1. DR PROSITE; PS01150; COMPLEX1_20K; 1. 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; 9TAK; -. 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; Translocase; Transport; Ubiquinone. FT CHAIN 1..220 FT /note="NADH-quinone oxidoreductase subunit B" FT /id="PRO_0000118765" FT BINDING 63 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356" FT BINDING 64 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356" FT BINDING 129 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356" FT BINDING 158 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356" FT CONFLICT 71 FT /note="S -> L (in Ref. 1; CAA48361)" FT /evidence="ECO:0000305" FT STRAND 3..6 FT /evidence="ECO:0007829|PDB:7Z7V" FT STRAND 16..18 FT /evidence="ECO:0007829|PDB:7Z7S" FT STRAND 20..25 FT /evidence="ECO:0007829|PDB:7Z7S" FT HELIX 38..51 FT /evidence="ECO:0007829|PDB:7Z7V" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:7NZ1" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:7NZ1" FT HELIX 65..70 FT /evidence="ECO:0007829|PDB:7NZ1" FT HELIX 71..73 FT /evidence="ECO:0007829|PDB:7AWT" FT TURN 74..76 FT /evidence="ECO:0007829|PDB:7Z7V" FT HELIX 78..81 FT /evidence="ECO:0007829|PDB:7Z7V" FT STRAND 87..89 FT /evidence="ECO:0007829|PDB:7Z7V" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:7P7C" FT STRAND 94..98 FT /evidence="ECO:0007829|PDB:7NZ1" FT TURN 104..106 FT /evidence="ECO:0007829|PDB:7NZ1" FT HELIX 107..116 FT /evidence="ECO:0007829|PDB:7NZ1" FT STRAND 122..127 FT /evidence="ECO:0007829|PDB:7NZ1" FT HELIX 128..131 FT /evidence="ECO:0007829|PDB:7NZ1" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:7P7M" FT HELIX 145..147 FT /evidence="ECO:0007829|PDB:7NZ1" FT STRAND 152..155 FT /evidence="ECO:0007829|PDB:7NZ1" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:7NZ1" FT HELIX 162..176 FT /evidence="ECO:0007829|PDB:7NZ1" FT STRAND 178..180 FT /evidence="ECO:0007829|PDB:7P61" FT STRAND 183..188 FT /evidence="ECO:0007829|PDB:7Z7V" FT TURN 193..197 FT /evidence="ECO:0007829|PDB:7NZ1" FT HELIX 200..203 FT /evidence="ECO:0007829|PDB:7NZ1" FT HELIX 205..209 FT /evidence="ECO:0007829|PDB:7NZ1" SQ SEQUENCE 220 AA; 25056 MW; EBD6268505993880 CRC64; MDYTLTRIDP NGENDRYPLQ KQEIVTDPLE QEVNKNVFMG KLNDMVNWGR KNSIWPYNFG LSCCYVEMVT SFTAVHDVAR FGAEVLRASP RQADLMVVAG TCFTKMAPVI QRLYDQMLEP KWVISMGACA NSGGMYDIYS VVQGVDKFIP VDVYIPGCPP RPEAYMQALM LLQESIGKER RPLSWVVGDQ GVYRANMQSE RERKRGERIA VTNLRTPDEI //