NUOB_SULNB
ID NUOB_SULNB Reviewed; 172 AA.
AC A6QCG2;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=SUN_2231;
OS Sulfurovum sp. (strain NBC37-1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Sulfurovum; unclassified Sulfurovum.
OX NCBI_TaxID=387093;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBC37-1;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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
CC ubiquinone. 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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01356}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01356}; 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}.
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; AP009179; BAF73171.1; -; Genomic_DNA.
DR RefSeq; WP_012084008.1; NC_009663.1.
DR AlphaFoldDB; A6QCG2; -.
DR SMR; A6QCG2; -.
DR STRING; 387093.SUN_2231; -.
DR EnsemblBacteria; BAF73171; BAF73171; SUN_2231.
DR KEGG; sun:SUN_2231; -.
DR eggNOG; COG0377; Bacteria.
DR HOGENOM; CLU_055737_7_3_7; -.
DR OMA; AGWVRKS; -.
DR OrthoDB; 1904620at2; -.
DR Proteomes; UP000006378; 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.
PE 3: Inferred from homology;
KW 4Fe-4S; Cell inner membrane; Cell membrane; Iron; Iron-sulfur; Membrane;
KW Metal-binding; NAD; Quinone; Reference proteome; Translocase; Transport;
KW Ubiquinone.
FT CHAIN 1..172
FT /note="NADH-quinone oxidoreductase subunit B"
FT /id="PRO_0000376393"
FT BINDING 42
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 43
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 107
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 136
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
SQ SEQUENCE 172 AA; 19174 MW; 1129689F7322950B CRC64;
MAQHQVNYAS AAGLPIALTS VDKLVNWGRS NSLWPLTYGL ACCAIEMMAS GASRYDFDRM
GTIFRASPRQ ADVMILAGTL SKKHSEFARR LYDQMTEPKW VISMGSCANT GGMFNTYATV
QGVDRIIPVD IYLPGCAPRP ETLQYALMML QKKIRRESAN MNNNTKQNLR LV