ID Q1Q759_9BACT Unreviewed; 212 AA. AC Q1Q759; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 29-OCT-2014, entry version 45. DE RecName: Full=NADH-quinone oxidoreductase subunit B {ECO:0000256|HAMAP-Rule:MF_01356}; DE EC=1.6.99.5 {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 ECO:0000313|EMBL:CAJ73410.1}; GN ORFNames=kuste2661 {ECO:0000313|EMBL:CAJ73410.1}; OS Candidatus Kuenenia stuttgartiensis. OC Bacteria; Planctomycetes; Planctomycetia; Candidatus Brocadiales; OC Candidatus Brocadiaceae; Candidatus Kuenenia. OX NCBI_TaxID=174633 {ECO:0000313|EMBL:CAJ73410.1}; RN [1] {ECO:0000313|EMBL:CAJ73410.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16598256; DOI=10.1038/nature04647; RA Strous M., Pelletier E., Mangenot S., Rattei T., Lehner A., RA Taylor M.W., Horn M., Daims H., Bartol-Mavel D., Wincker P., Barbe V., RA Fonknechten N., Vallenet D., Segurens B., Schenowitz-Truong C., RA Medigue C., Collingro A., Snel B., Dutilh B.E., OpDenCamp H.J.M., RA vanDerDrift C., Cirpus I., vanDePas-Schoonen K.T., Harhangi H.R., RA vanNiftrik L., Schmid M., Keltjens J., vanDeVossenberg J., Kartal B., RA Meier H., Frishman D., Huynen M.A., Mewes H., Weissenbach J., RA Jetten M.S.M., Wagner M., LePaslier D.; RT "Deciphering the evolution and metabolism of an anammox bacterium from RT a community genome."; RL Nature 440:790-794(2006). RN [2] {ECO:0000313|EMBL:CAJ73410.1} RP NUCLEOTIDE SEQUENCE. RA Genoscope; RL Submitted (JAN-2006) 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 + quinone = NAD(+) + quinol. CC {ECO:0000256|HAMAP-Rule:MF_01356}. CC -!- COFACTOR: Binds 1 4Fe-4S cluster. {ECO:0000256|HAMAP- CC 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 --------------------------------------------------------------------------- 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; CT573071; CAJ73410.1; -; Genomic_DNA. DR ProteinModelPortal; Q1Q759; -. DR PRIDE; Q1Q759; -. 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-HAMAP. 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 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 METAL 55 55 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01356}. FT METAL 56 56 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01356}. FT METAL 121 121 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01356}. FT METAL 150 150 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01356}. SQ SEQUENCE 212 AA; 23999 MW; DDEFE4E029A19CBF CRC64; MKWWLTKSSD QTKTVSGTSS FEEAVQKTVV LCNLQNLIAW GRKNSLWPFN FGLSCCYVEM ATSLTSKYDI ARFGAEVIRG TPREADVMIT AGTIFIKMAP IIKRLYEQMM EPRWIISMGS CSNSGGMYDI YSVVQGVDKF MPVDVYVPGC PPRPDAFMEG LLMLRDSVGK EKRPLSWFTG PQGITRMDPV SMKELKHENR MKMTKIKPPS EI //