NUOJ_BUCAI
ID NUOJ_BUCAI Reviewed; 170 AA.
AC P57260;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=NADH-quinone oxidoreductase subunit J;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunit J;
DE AltName: Full=NDH-1 subunit J;
GN Name=nuoJ; OrderedLocusNames=BU162;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC reaction to proton translocation (for every two electrons transferred,
CC four hydrogen ions are translocated across the cytoplasmic membrane),
CC and thus conserves the redox energy in a proton gradient (By
CC similarity). {ECO:0000250}.
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 -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoA, H, J, K, L,
CC M, N constitute the membrane sector of the complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the complex I subunit 6 family. {ECO:0000305}.
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DR EMBL; BA000003; BAB12880.1; -; Genomic_DNA.
DR RefSeq; NP_239994.1; NC_002528.1.
DR RefSeq; WP_009874118.1; NC_002528.1.
DR AlphaFoldDB; P57260; -.
DR SMR; P57260; -.
DR STRING; 107806.10038845; -.
DR EnsemblBacteria; BAB12880; BAB12880; BAB12880.
DR KEGG; buc:BU162; -.
DR PATRIC; fig|107806.10.peg.172; -.
DR eggNOG; COG0839; Bacteria.
DR HOGENOM; CLU_085957_0_1_6; -.
DR OMA; WVLPFEA; -.
DR Proteomes; UP000001806; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.1200; -; 1.
DR InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6.
DR InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ.
DR Pfam; PF00499; Oxidored_q3; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; NAD; Quinone; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..170
FT /note="NADH-quinone oxidoreductase subunit J"
FT /id="PRO_0000118374"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 170 AA; 19088 MW; EA1FE307DB7AF878 CRC64;
MEFVFYVCSF AAVVSTFFVI IQKNAVYSLV YLIISLLSIA GVFFSLGAFF AGSLEVIIYA
GAIIVLFVFV IMMLNISDKY NLEEAHYLKP RFWIGPSILS LILLLSMTYA IFFLRDKKID
GFLIDSKIVG INLFGPYVFL VELSSILLLS ALVVIFHIGT EKNVDKNKVL
