ID Q1Q759_KUEST Unreviewed; 212 AA. AC Q1Q759; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 07-OCT-2020, entry version 67. 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 ECO:0000313|EMBL:CAJ73410.1}; GN ORFNames=KSMBR1_3989 {ECO:0000313|EMBL:SOH06461.1}, kuste2661 GN {ECO:0000313|EMBL:CAJ73410.1}; OS Kuenenia stuttgartiensis. OC Bacteria; Planctomycetes; Candidatus Brocadiae; 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., Taylor M.W., RA Horn M., Daims H., Bartol-Mavel D., Wincker P., Barbe V., Fonknechten N., RA Vallenet D., Segurens B., Schenowitz-Truong C., Medigue C., Collingro A., RA Snel B., Dutilh B.E., OpDenCamp H.J.M., vanDerDrift C., Cirpus I., RA vanDePas-Schoonen K.T., Harhangi H.R., vanNiftrik L., Schmid M., RA Keltjens J., vanDeVossenberg J., Kartal B., Meier H., Frishman D., RA Huynen M.A., Mewes H., Weissenbach J., Jetten M.S.M., Wagner M., RA LePaslier D.; RT "Deciphering the evolution and metabolism of an anammox bacterium from a RT 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. RN [3] {ECO:0000313|EMBL:SOH06461.1, ECO:0000313|Proteomes:UP000221734} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Kuenenia_mbr1_ru-nijmegen {ECO:0000313|EMBL:SOH06461.1}; RA Banno H., Chua N.-H.; RL Submitted (OCT-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. 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 --------------------------------------------------------------------------- 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 EMBL; LT934425; SOH06461.1; -; Genomic_DNA. DR KEGG; kst:KSMBR1_3989; -. DR KO; K00331; -. DR Proteomes; UP000221734; Chromosome kuenenia_stuttgartiensis_mbr1. 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 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, 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 Oxidoreductase {ECO:0000313|EMBL:CAJ73410.1}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01356}; KW Reference proteome {ECO:0000313|Proteomes:UP000221734}; 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 56..163 FT /note="Oxidored_q6" FT /evidence="ECO:0000259|Pfam:PF01058" FT METAL 55 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" FT METAL 56 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" FT METAL 121 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" FT METAL 150 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-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 //