ID A0A105LBI9_9BURK Unreviewed; 167 AA. AC A0A105LBI9; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 27-SEP-2017, entry version 11. DE RecName: Full=NADH-quinone oxidoreductase subunit B {ECO:0000256|HAMAP-Rule:MF_01356}; DE EC=1.6.5.11 {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=BW685_16520 {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}, WL80_22155 GN {ECO:0000313|EMBL:KWE84690.1}; OS Burkholderia ubonensis. OC Bacteria; Proteobacteria; 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, ECO:0000313|Proteomes:UP000067565} 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}, and MSMB2205WGS RC {ECO:0000313|EMBL:KWE84690.1, 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|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., RA Kaestli M., Mayo M., Harrington G., Baker A.L., Sidak-Loftis L.C., RA Lummis M., Schupp J.M., Gillece J.D., Tuanyok A., Warner J., RA Busch J.D., Keim P., 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- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC believed to be ubiquinone. Couples the redox reaction to proton CC translocation (for every two electrons transferred, four hydrogen CC ions are translocated across the cytoplasmic membrane), and thus CC conserves the redox energy in a proton gradient. CC {ECO:0000256|HAMAP-Rule:MF_01356}. CC -!- CATALYTIC ACTIVITY: NADH + a quinone = NAD(+) + a quinol. CC {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 CC NuoB, C, D, E, F, and G constitute the peripheral sector of the CC complex. {ECO:0000256|HAMAP-Rule:MF_01356}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01356}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01356}; Cytoplasmic side {ECO:0000256|HAMAP- CC 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 CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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; LPJL01000097; KWE84690.1; -; Genomic_DNA. DR EMBL; MTJZ01000018; OMG72316.1; -; Genomic_DNA. DR RefSeq; WP_045564217.1; NZ_MTJZ01000018.1. 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 GeneID; 29889710; -. DR Proteomes; UP000060630; Unassembled WGS sequence. DR Proteomes; UP000064029; Unassembled WGS sequence. DR Proteomes; UP000067565; Unassembled WGS sequence. DR Proteomes; UP000067740; 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 GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.700; -; 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 Pfam; PF01058; Oxidored_q6; 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, KW ECO:0000256|RuleBase:RU004464}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01356}; KW Complete proteome {ECO:0000313|Proteomes:UP000060630, KW ECO:0000313|Proteomes:UP000064029, ECO:0000313|Proteomes:UP000067565, KW ECO:0000313|Proteomes:UP000067740}; 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}; KW 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 Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01356, KW ECO:0000256|RuleBase:RU004464}; KW Quinone {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 Oxidored_q6. {ECO:0000259|Pfam:PF01058}. FT METAL 39 39 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01356}. FT METAL 40 40 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01356}. FT METAL 104 104 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01356}. FT METAL 134 134 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT 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 //