(data stored in SCRATCH zone)

SWISSPROT: NUOB_NOCSJ

ID   NUOB_NOCSJ              Reviewed;         184 AA.
AC   A1SE28;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   11-DEC-2019, entry version 81.
DE   RecName: Full=NADH-quinone oxidoreductase subunit B {ECO:0000255|HAMAP-Rule:MF_01356};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01356};
DE   AltName: Full=NADH dehydrogenase I subunit B {ECO:0000255|HAMAP-Rule:MF_01356};
DE   AltName: Full=NDH-1 subunit B {ECO:0000255|HAMAP-Rule:MF_01356};
GN   Name=nuoB {ECO:0000255|HAMAP-Rule:MF_01356}; OrderedLocusNames=Noca_0521;
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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:0000255|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:0000255|HAMAP-Rule:MF_01356};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01356};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01356}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01356};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01356};
CC       Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01356}.
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01356}.
DR   EMBL; CP000509; ABL80063.1; -; Genomic_DNA.
DR   RefSeq; WP_011754013.1; NC_008699.1.
DR   SMR; A1SE28; -.
DR   STRING; 196162.Noca_0521; -.
DR   EnsemblBacteria; ABL80063; ABL80063; Noca_0521.
DR   KEGG; nca:Noca_0521; -.
DR   eggNOG; ENOG4105ES3; Bacteria.
DR   eggNOG; COG0377; LUCA.
DR   HOGENOM; HOG000228249; -.
DR   KO; K00331; -.
DR   OMA; HYSYSVT; -.
DR   OrthoDB; 1904620at2; -.
DR   Proteomes; UP000000640; 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;
DR   PRODOM; A1SE28.
DR   SWISS-2DPAGE; A1SE28.
KW   4Fe-4S; Cell membrane; Iron; Iron-sulfur; Membrane; Metal-binding; NAD;
KW   Quinone; Reference proteome; Translocase; Transport.
FT   CHAIN           1..184
FT                   /note="NADH-quinone oxidoreductase subunit B"
FT                   /id="PRO_0000376294"
FT   METAL           37
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT   METAL           38
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT   METAL           103
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT   METAL           132
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
SQ   SEQUENCE   184 AA;  20057 MW;  DAFAEF8BD0E90210 CRC64;
     MGIEEKLPSG VLLSTVEGLA GYMRKASFWP ASFGLACCAI EMMTSGGPKH DLGRFGMEVF
     RASPRQADVM IVAGRVSQKM APVLRQIYDQ MPEPKWVLAM GVCASSGGMF NNYAVVQGVD
     HVVPVDMYLP GCPPRPQMLI DAILKLHDKV QHTKMGAHRA AEIEELETAA LRALPTSEMK
     GQLR
//

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