ID NUOB_COXBU Reviewed; 161 AA. AC Q83BQ6; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 124. 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}; GN Name=nuoB {ECO:0000255|HAMAP-Rule:MF_01356}; GN OrderedLocusNames=CBU_1447; OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae; OC Coxiella. OX NCBI_TaxID=227377; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSA 493 / Nine Mile phase I; RX PubMed=12704232; DOI=10.1073/pnas.0931379100; RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., RA Fraser C.M., Heidelberg J.F.; RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur CC (Fe-S) centers, to quinones in the respiratory chain. Couples the redox CC reaction to proton translocation (for every two electrons transferred, CC four hydrogen ions are translocated across the cytoplasmic membrane), CC and thus conserves the redox energy in a proton gradient (By CC similarity). {ECO:0000250}. 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_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 14 different subunits. Subunits NuoB, C, CC D, E, F, and G constitute the peripheral sector of the complex. CC {ECO:0000255|HAMAP-Rule:MF_01356}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01356}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01356}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01356}. 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; AE016828; AAO90944.1; -; Genomic_DNA. DR RefSeq; NP_820430.1; NC_002971.3. DR RefSeq; WP_005769074.1; NZ_CDBG01000001.1. DR AlphaFoldDB; Q83BQ6; -. DR SMR; Q83BQ6; -. DR STRING; 227377.CBU_1447; -. DR DNASU; 1209354; -. DR EnsemblBacteria; AAO90944; AAO90944; CBU_1447. DR GeneID; 1209354; -. DR KEGG; cbu:CBU_1447; -. DR PATRIC; fig|227377.7.peg.1447; -. DR eggNOG; COG0377; Bacteria. DR HOGENOM; CLU_055737_7_3_6; -. DR OrthoDB; 9786737at2; -. DR Proteomes; UP000002671; Chromosome. DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central. DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central. 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 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. PE 3: Inferred from homology; KW 4Fe-4S; Cell inner membrane; Cell membrane; Iron; Iron-sulfur; Membrane; KW Metal-binding; NAD; Quinone; Reference proteome; Translocase; Transport; KW Ubiquinone. FT CHAIN 1..161 FT /note="NADH-quinone oxidoreductase subunit B" FT /id="PRO_0000358395" FT BINDING 36 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356" FT BINDING 37 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356" FT BINDING 102 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356" FT BINDING 132 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356" SQ SEQUENCE 161 AA; 18160 MW; 4720682912477297 CRC64; MQQLLTKEGF LLTSLDDLMR WARSGSLWPM TFGLACCAVE MMQCASSRYD LDRFGAGLFR PSPRQSDVMI VAGTLCNKMA PALRKVYDQM AEPRWVISMG SCANGGGYYH YAYSVVRGCD RIVPVDVYVP GCPPTAEALF YGIMQLRNKI RYRNIFDRKD A //