ID NUOB_BUCAI Reviewed; 224 AA. AC P57253; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 25-NOV-2008, entry version 43. 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; OrderedLocusNames=BU155; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum OS symbiotic bacterium). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=118099; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tokyo 1998; RX MEDLINE=20445173; PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids RT Buchnera sp. APS."; RL Nature 407:81-86(2000). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. CC Couples the redox reaction to proton translocation (for every two CC electrons transferred, four hydrogen ions are translocated across CC the cytoplasmic membrane), and thus conserves the redox energy in CC a proton gradient (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol. CC -!- COFACTOR: Binds 1 4Fe-4S cluster (Potential). CC -!- SUBUNIT: Composed of 13 different subunits (By similarity). CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000003; BAB12873.1; -; Genomic_DNA. DR RefSeq; NP_239987.1; -. DR GeneID; 1109599; -. DR GenomeReviews; BA000003_GR; BU155. DR KEGG; buc:BU155; -. DR HOGENOM; P57253; -. DR BioCyc; BSP107806:BU155-MON; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to u...; IEA:InterPro. DR InterPro; IPR006138; NADH_DHase_20kDa_su. DR InterPro; IPR014406; NiFe_hyd_3_ssu/Q_oxred_NuoB. DR InterPro; IPR006137; OxRdtase_q6. 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; Complete proteome; Iron; Iron-sulfur; Metal-binding; NAD; KW Oxidoreductase; Quinone. FT CHAIN 1 224 NADH-quinone oxidoreductase subunit B. FT /FTId=PRO_0000118769. FT METAL 67 67 Iron-sulfur (4Fe-4S) (Potential). FT METAL 68 68 Iron-sulfur (4Fe-4S) (Potential). FT METAL 133 133 Iron-sulfur (4Fe-4S) (Potential). FT METAL 162 162 Iron-sulfur (4Fe-4S) (Potential). SQ SEQUENCE 224 AA; 25597 MW; BB450B102C87CD7B CRC64; MNYTLTKADS DNNNKKYPKQ TIESVSDPLE EYLKKNIFMG KITQLLHKLV NWGRKNSLWP YNFGLSCCYV EMVSAFTSVH DVARFGSEVL RASPRQADVM VIAGTPFIKM APVIQRLYDQ MLEPKWVISM GACANSGGMY DIYSVVQGVD KFLPVDIYIP GCPPRPEAYM QALILLQKLI NEERRPLSWV IGEQGVYHKK MPSERVQKRS KRINIINLST SEKI //