ID NUOB_BRUA1 Reviewed; 193 AA.
AC B2S544;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 01-MAY-2013, entry version 37.
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=BAbS19_I07670;
OS Brucella abortus (strain S19).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Brucellaceae; Brucella.
OX NCBI_TaxID=430066;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S19;
RX PubMed=18478107; DOI=10.1371/journal.pone.0002193;
RA Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C.,
RA Martino-Catt S., Bricker B., Yu G., Du L., Sobral B.W.;
RT "Genome sequence of Brucella abortus vaccine strain S19 compared to
RT virulent strains yields candidate virulence genes.";
RL PLoS ONE 3:E2193-E2193(2008).
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 (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 inner membrane; Peripheral membrane
CC protein; Cytoplasmic side (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; CP000887; ACD72291.1; -; Genomic_DNA.
DR RefSeq; YP_001934765.1; NC_010742.1.
DR ProteinModelPortal; B2S544; -.
DR STRING; 430066.BAbS19_I07670; -.
DR EnsemblBacteria; ACD72291; ACD72291; BAbS19_I07670.
DR GeneID; 6327929; -.
DR KEGG; bmc:BAbS19_I07670; -.
DR PATRIC; 17818584; VBIBruAbo38055_2062.
DR eggNOG; COG0377; -.
DR HOGENOM; HOG000228249; -.
DR KO; K00331; -.
DR OMA; HYDNERF; -.
DR ProtClustDB; PRK06411; -.
DR BioCyc; BABO430066:GHI6-759-MONOMER; -.
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: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:0019684; P:photosynthesis, light reaction; IEA:HAMAP.
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 InterPro; IPR014406; NiFe-hyd_3_ssu/Q_oxred_NuoB.
DR PANTHER; PTHR11995; PTHR11995; 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 inner membrane; Cell membrane; Complete proteome; Iron;
KW Iron-sulfur; Membrane; Metal-binding; NAD; Oxidoreductase; Quinone;
KW Transport; Ubiquinone.
FT CHAIN 1 193 NADH-quinone oxidoreductase subunit B.
FT /FTId=PRO_0000358357.
FT METAL 72 72 Iron-sulfur (4Fe-4S) (Potential).
FT METAL 73 73 Iron-sulfur (4Fe-4S) (Potential).
FT METAL 137 137 Iron-sulfur (4Fe-4S) (Potential).
FT METAL 167 167 Iron-sulfur (4Fe-4S) (Potential).
SQ SEQUENCE 193 AA; 21036 MW; F85E7FEDA4E09A25 CRC64;
MGLTGTNTTL VAPQPKGILD PRTGKTVGSD DAFFNDLNGE LSDKGFIVTS ADALITWART
GSLMWMTFGL ACCAVEMMHI SMPRYDAERF GIAPRASPRQ SDVMIVAGTL TNKMAPALRK
VYDQMPEPRY VISMGSCANG GGYYHYSYSV VRGCDRVVPV DIYVPGCPPT AEALLYGILL
LQKKIRRTGT IER
//
