ID A0A105LBI9_9BURK Unreviewed; 167 AA. AC A0A105LBI9; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 03-MAY-2023, entry version 31. DE RecName: Full=NADH-quinone oxidoreductase subunit B {ECO:0000256|HAMAP-Rule:MF_01356}; DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01356}; DE AltName: Full=NADH dehydrogenase I subunit B {ECO:0000256|HAMAP-Rule:MF_01356}; DE AltName: Full=NDH-1 subunit B {ECO:0000256|HAMAP-Rule:MF_01356}; GN Name=nuoB {ECO:0000256|HAMAP-Rule:MF_01356}; GN ORFNames=BGV49_17345 {ECO:0000313|EMBL:OJA85656.1}, BW685_16520 GN {ECO:0000313|EMBL:OMG72316.1}, WJ33_12185 GN {ECO:0000313|EMBL:KVG76848.1}, WK95_24140 GN {ECO:0000313|EMBL:KVW35758.1}, WL29_09160 GN {ECO:0000313|EMBL:KWA69569.1}, WL60_25825 GN {ECO:0000313|EMBL:KWD28475.1}, WL80_22155 GN {ECO:0000313|EMBL:KWE84690.1}; OS Burkholderia ubonensis. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=101571 {ECO:0000313|EMBL:KVW35758.1, ECO:0000313|Proteomes:UP000067565}; RN [1] {ECO:0000313|Proteomes:UP000060630, ECO:0000313|Proteomes:UP000064029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSMB1346WGS {ECO:0000313|EMBL:KVW35758.1, RC ECO:0000313|Proteomes:UP000067565}, MSMB2036 RC {ECO:0000313|EMBL:KVG76848.1, ECO:0000313|Proteomes:UP000064029}, RC MSMB2087WGS {ECO:0000313|EMBL:KWA69569.1, RC ECO:0000313|Proteomes:UP000060630}, MSMB2188WGS RC {ECO:0000313|EMBL:KWD28475.1, ECO:0000313|Proteomes:UP000066241}, and RC MSMB2205WGS {ECO:0000313|EMBL:KWE84690.1, RC ECO:0000313|Proteomes:UP000067740}; RA Sahl J., Keim P., Wagner D.; RT "Expanding the genomic diversity of Burkholderia species for the RT development of highly accurate diagnostics."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000183092} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSMB0170 {ECO:0000313|Proteomes:UP000183092}; RA Price E.P., Currie B.J., Wagner D.M.; RT "Population biology and virulence potential of Burkholderia ubonensis."; RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:OJA85656.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MSMB0170 {ECO:0000313|EMBL:OJA85656.1}; RA Price E.P., Currie B.J., Wagner D.M.; RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:OMG72316.1, ECO:0000313|Proteomes:UP000187194} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A21 {ECO:0000313|EMBL:OMG72316.1, RC ECO:0000313|Proteomes:UP000187194}; RA Price E.P., Sarovich D.S., Webb J.R., Hall C.M., Sahl J.W., Kaestli M., RA Mayo M., Harrington G., Baker A.L., Sidak-Loftis L.C., Lummis M., RA Schupp J.M., Gillece J.D., Tuanyok A., Warner J., Busch J.D., Keim P., RA Currie B.J., Wagner D.M.; RT "Phylogeographic, genomic and meropenem susceptibility analysis of RT Burkholderia ubonensis."; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. 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. CC {ECO:0000256|ARBA:ARBA00025189}. 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. {ECO:0000256|HAMAP-Rule:MF_01356}. 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:0000256|HAMAP-Rule:MF_01356}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01356}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01356}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01356}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01356}; CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01356}. CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family. CC {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KVW35758.1}. 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; LOXM01000007; KVG76848.1; -; Genomic_DNA. DR EMBL; LPFE01000063; KVW35758.1; -; Genomic_DNA. DR EMBL; LPHD01000222; KWA69569.1; -; Genomic_DNA. DR EMBL; LPIK01000005; KWD28475.1; -; Genomic_DNA. DR EMBL; LPJL01000097; KWE84690.1; -; Genomic_DNA. DR EMBL; MEBC01000020; OJA85656.1; -; Genomic_DNA. DR EMBL; MTJZ01000018; OMG72316.1; -; Genomic_DNA. DR RefSeq; WP_045564217.1; NZ_MTJZ01000018.1. DR AlphaFoldDB; A0A105LBI9; -. DR EnsemblBacteria; KVG76848; KVG76848; WJ33_12185. DR EnsemblBacteria; KVW35758; KVW35758; WK95_24140. DR EnsemblBacteria; KWA69569; KWA69569; WL29_09160. DR EnsemblBacteria; KWE84690; KWE84690; WL80_22155. DR EnsemblBacteria; OMG72316; OMG72316; BW685_16520. DR OrthoDB; 9786737at2; -. DR Proteomes; UP000060630; Unassembled WGS sequence. DR Proteomes; UP000064029; Unassembled WGS sequence. DR Proteomes; UP000066241; Unassembled WGS sequence. DR Proteomes; UP000067565; Unassembled WGS sequence. DR Proteomes; UP000067740; Unassembled WGS sequence. DR Proteomes; UP000183092; Unassembled WGS sequence. DR Proteomes; UP000187194; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. 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 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 TIGRFAMs; TIGR01957; nuoB_fam; 1. DR PROSITE; PS01150; COMPLEX1_20K; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01356}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01356, KW ECO:0000256|RuleBase:RU004464}; Membrane {ECO:0000256|HAMAP-Rule:MF_01356}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01356, KW ECO:0000256|RuleBase:RU004464}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01356}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01356}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01356}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01356}. FT DOMAIN 40..148 FT /note="NADH:ubiquinone oxidoreductase-like 20kDa subunit" FT /evidence="ECO:0000259|Pfam:PF01058" FT BINDING 39 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" FT BINDING 40 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" FT BINDING 104 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" FT BINDING 134 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" SQ SEQUENCE 167 AA; 18685 MW; BB55826BE7807E4C CRC64; MIDQPFTLEK DGFVVTSLEA VLAAARTNSL WYMTFGLACC AVEMMHAAGA RYDMDRFGMI PRASPRQCDL MIVSGTLTNK MAPAMRKVYD QMAEPRYVVS MGSCANGGGY YHYSYSVVRG CDRIVPVDVY VPGCPPTAEA LIYGLMQLQR KIMEQSTHSQ PRVFERR //