ID D7GIX6_PROFC Unreviewed; 185 AA. AC D7GIX6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 02-JUN-2021, entry version 60. 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:CBL56048.1}; GN OrderedLocusNames=PFREUD_05170 {ECO:0000313|EMBL:CBL56048.1}; OS Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM OS 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1). OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Propionibacterium. OX NCBI_TaxID=754252 {ECO:0000313|EMBL:CBL56048.1, ECO:0000313|Proteomes:UP000000936}; RN [1] {ECO:0000313|EMBL:CBL56048.1, ECO:0000313|Proteomes:UP000000936} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1 RC {ECO:0000313|Proteomes:UP000000936}; RX PubMed=20668525; DOI=10.1371/journal.pone.0011748; RA Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S., RA Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P., RA Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., Gaillardin C., RA Lortal S.; RT "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a hardy RT actinobacterium with food and probiotic applications."; RL PLoS ONE 5:E11748-E11748(2010). 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 a CC menaquinone. 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; FN806773; CBL56048.1; -; Genomic_DNA. DR RefSeq; WP_013160439.1; NC_014215.1. DR STRING; 754252.PFREUD_05170; -. DR EnsemblBacteria; CBL56048; CBL56048; PFREUD_05170. DR GeneID; 61222779; -. DR KEGG; pfr:PFREUD_05170; -. DR eggNOG; COG0377; Bacteria. DR HOGENOM; CLU_055737_7_3_11; -. DR OMA; RIIITYE; -. DR OrthoDB; 1904620at2; -. DR Proteomes; UP000000936; Chromosome. 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:CBL56048.1}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01356}; KW Reference proteome {ECO:0000313|Proteomes:UP000000936}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01356}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01356}. FT DOMAIN 61..145 FT /note="Oxidored_q6" FT /evidence="ECO:0000259|Pfam:PF01058" FT METAL 37 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" FT METAL 38 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" FT METAL 103 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" FT METAL 132 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" SQ SEQUENCE 185 AA; 20311 MW; 45AE72FD45294C58 CRC64; MGIEEKLPAG IFLTTVEQVQ GWMRQASFWP LTMGLACCAI EMISYGGPRA DCSRWGQEIF RASPRQADLM IVAGRVGQKL APVVRQLWDQ MPNPKWCIAM GACASSGGVF NNYAVVQGVD HIVPVDMYLP GCPPRPDMLI DAVFKLKKGK VQHTTMGAHR VQEVAELEQK ALAAPATIEQ KGLMR //