ID D7GIX6_PROFR Unreviewed; 185 AA. AC D7GIX6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 05-OCT-2010, entry version 2. DE RecName: Full=NADH-quinone oxidoreductase subunit B; DE EC=1.6.99.5; DE AltName: Full=NADH dehydrogenase I subunit B; DE AltName: Full=NDH-1 subunit B; GN Name=nuoB; ORFNames=PFREUD_05170; OS Propionibacterium freudenreichii subsp. shermanii CIRM-BIA1. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=754252; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIRM-B1AI; 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., RA Gaillardin C., Lortal S.; RT "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a RT hardy 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- 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 a menaquinone. 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 (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol. CC -!- COFACTOR: Binds 1 4Fe-4S cluster (By similarity). 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 (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; CC Cytoplasmic side (By similarity). CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family. 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; YP_003687492.1; -. DR GeneID; 9283963; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; 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 InterPro; IPR014406; NiFe_hyd_3_ssu/Q_oxred_NuoB. DR PANTHER; PTHR11995:SF2; NADH_DH_20kDa; 1. DR PANTHER; PTHR11995; NiFe_hyd_3_ssu/Q_oxred_NuoB; 1. 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; Cell membrane; Iron; Iron-sulfur; Membrane; Metal-binding; KW NAD; Oxidoreductase; Quinone; Transport. FT METAL 37 37 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 38 38 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 103 103 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 132 132 Iron-sulfur (4Fe-4S) (By similarity). 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 //