ID   NUOB_AQUAE              Reviewed;         179 AA.
AC   O67334;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 57.
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=aq_1312;
OS   Aquifex aeolicus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=63363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
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.
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DR   EMBL; AE000657; AAC07297.1; -; Genomic_DNA.
DR   PIR; C70413; C70413.
DR   RefSeq; NP_213898.1; -.
DR   GeneID; 1192772; -.
DR   GenomeReviews; AE000657_GR; aq_1312.
DR   KEGG; aae:aq_1312; -.
DR   NMPDR; fig|224324.1.peg.913; -.
DR   HOGENOM; O67334; -.
DR   OMA; O67334; HYDNERF.
DR   BioCyc; AAEO224324:AQ_1312-MON; -.
DR   BRENDA; 1.6.99.5; 189781.
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:0055114; P:oxidation reduction; IEA:HAMAP.
DR   GO; GO:0019684; P:photosynthesis, light reaction; IEA:HAMAP.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   HAMAP; MF_01356; -; 1.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR006138; NADH_UbQ_OxRdtase_su-20kDa.
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 inner membrane; Cell membrane; Complete proteome; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; NAD; Oxidoreductase; Quinone;
KW   Transport; Ubiquinone.
FT   CHAIN         1    179       NADH-quinone oxidoreductase subunit B.
FT                                /FTId=PRO_0000118764.
FT   METAL        35     35       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL        36     36       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       100    100       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       129    129       Iron-sulfur (4Fe-4S) (Potential).
SQ   SEQUENCE   179 AA;  19880 MW;  239D68B6AF828B77 CRC64;
     MVAINSNGFV TTTVEELLRW GRRNSLWPVT IGLACCAIEM MHTAASRFDL DRLGVIFRAS
     PRQADVLIVA GTVVNKVAPM LKLIWDQMPD PKWCISMGGC ASAGGPFPTY STLQGVDRII
     PVDVYIPGCP PTPQGLIYGI LQLQRKIKEQ GITKYDKLFA DFNREIEKEG IFVPRELKV
//