NUOB_PARDP
ID NUOB_PARDP Reviewed; 175 AA.
AC A1B497;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=NADH dehydrogenase I, subunit 6;
DE AltName: Full=NADH-quinone oxidoreductase subunit 6;
DE Short=NQO6;
DE AltName: Full=NDH-1 subunit B {ECO:0000255|HAMAP-Rule:MF_01356};
DE AltName: Full=NDH-1, subunit 6;
GN Name=nuoB {ECO:0000255|HAMAP-Rule:MF_01356};
GN Synonyms=nqo6 {ECO:0000303|PubMed:14610094}; OrderedLocusNames=Pden_2249;
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
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 Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION IN NADH OXIDASE SUPERCOMPLEX, FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=14610094; DOI=10.1074/jbc.m309505200;
RA Stroh A., Anderka O., Pfeiffer K., Yagi T., Finel M., Ludwig B.,
RA Schagger H.;
RT "Assembly of respiratory complexes I, III, and IV into NADH oxidase
RT supercomplex stabilizes complex I in Paracoccus denitrificans.";
RL J. Biol. Chem. 279:5000-5007(2004).
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 ECO:0000305|PubMed:14610094}.
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 at least 14 different subunits, Nqo1 to
CC Nqo14. The complex has a L-shaped structure, with the hydrophobic arm
CC (subunits Nqo7, Nqo8, Nqo10 to Nqo14) embedded in the inner membrane
CC and the hydrophilic peripheral arm (subunits Nqo1 to Nqo6, Nqo9)
CC protruding into the bacterial cytoplasm. The hydrophilic domain
CC contains all the redox centers (By similarity). NADH-quinone
CC oxidoreductase forms a supercomplex with ubiquinol-cytochrome c
CC reductase complex (complex III or cytochrome b-c1 complex) and
CC cytochrome c oxidase (complex IV), which stabilizes the NADH-quinone
CC oxidoreductase complex (PubMed:14610094). {ECO:0000250,
CC ECO:0000269|PubMed:14610094}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:14610094}; Peripheral membrane protein
CC {ECO:0000305|PubMed:14610094}; Cytoplasmic side
CC {ECO:0000305|PubMed:14610094}.
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; CP000489; ABL70341.1; -; Genomic_DNA.
DR AlphaFoldDB; A1B497; -.
DR SMR; A1B497; -.
DR STRING; 318586.Pden_2249; -.
DR PRIDE; A1B497; -.
DR EnsemblBacteria; ABL70341; ABL70341; Pden_2249.
DR KEGG; pde:Pden_2249; -.
DR eggNOG; COG0377; Bacteria.
DR HOGENOM; CLU_055737_7_0_5; -.
DR OMA; GPYWEHG; -.
DR Proteomes; UP000000361; Chromosome 1.
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 1: Evidence at protein level;
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..175
FT /note="NADH-quinone oxidoreductase subunit B"
FT /id="PRO_0000358441"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 119
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 149
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
SQ SEQUENCE 175 AA; 19505 MW; 8233131871D66E8B CRC64;
MMTGLNTAGA DRDLATAELN RELQDKGFLL TTTEDIINWA RNGSLHWMTF GLACCAVEMM
QTSMPRYDLE RFGTAPRASP RQSDLMIVAG TLTNKMAPAL RKVYDQMPEP RYVISMGSCA
NGGGYYHYSY SVVRGCDRIV PVDIYVPGCP PTAEALLYGI LQLQRRIRRT GTLVR
