ID G6EIM8_9SPHN Unreviewed; 205 AA.
AC G6EIM8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=NADH-quinone oxidoreductase subunit J {ECO:0000256|RuleBase:RU004429};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN ORFNames=NSU_4199 {ECO:0000313|EMBL:EHJ58970.1};
OS Novosphingobium pentaromativorans US6-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1088721 {ECO:0000313|EMBL:EHJ58970.1, ECO:0000313|Proteomes:UP000004030};
RN [1] {ECO:0000313|EMBL:EHJ58970.1, ECO:0000313|Proteomes:UP000004030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=US6-1 {ECO:0000313|EMBL:EHJ58970.1,
RC ECO:0000313|Proteomes:UP000004030};
RX PubMed=22275104; DOI=10.1128/JB.06476-11;
RA Luo Y.R., Kang S.G., Kim S.J., Kim M.R., Li N., Lee J.H., Kwon K.K.;
RT "Genome sequence of benzo(a)pyrene-degrading bacterium Novosphingobium
RT pentaromativorans US6-1.";
RL J. Bacteriol. 194:907-907(2012).
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.
CC {ECO:0000256|RuleBase:RU004429}.
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:0000256|RuleBase:RU004429};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU004429};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU004429}.
CC -!- SIMILARITY: Belongs to the complex I subunit 6 family.
CC {ECO:0000256|ARBA:ARBA00005698, ECO:0000256|RuleBase:RU004429}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHJ58970.1}.
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DR EMBL; AGFM01000064; EHJ58970.1; -; Genomic_DNA.
DR RefSeq; WP_007015107.1; NZ_CP009291.1.
DR AlphaFoldDB; G6EIM8; -.
DR STRING; 1088721.JI59_02955; -.
DR KEGG; npn:JI59_02955; -.
DR PATRIC; fig|1088721.3.peg.4136; -.
DR eggNOG; COG0839; Bacteria.
DR OrthoDB; 9795409at2; -.
DR Proteomes; UP000004030; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.1200; NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ; 1.
DR InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6.
DR InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ.
DR PANTHER; PTHR33269; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 6; 1.
DR PANTHER; PTHR33269:SF17; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 6; 1.
DR Pfam; PF00499; Oxidored_q3; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU004429};
KW Membrane {ECO:0000256|RuleBase:RU004429};
KW NAD {ECO:0000256|RuleBase:RU004429};
KW Quinone {ECO:0000256|RuleBase:RU004429};
KW Reference proteome {ECO:0000313|Proteomes:UP000004030};
KW Transmembrane {ECO:0000256|RuleBase:RU004429};
KW Transmembrane helix {ECO:0000256|RuleBase:RU004429}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 31..47
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 53..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 90..112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 146..167
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
SQ SEQUENCE 205 AA; 21941 MW; 2410618387B8100A CRC64;
MIHVFAFYLF AVITIASAVT TITARNPVHS VLWLILAFFN AAGLMVLTGA EFIAMLLVIV
YVGAVAVLFL FVVMMLDIDF AELRAGFVRN FPLGLLVAIV LLAEMVLGIG AYRAGAMDLG
SPDGTAATPA GASNIEAIGG LLYSRYLFLF EAAGIILLVA MIGAIVLTHR QRSDTRGQKI
SKQIMRRPDE ATVNVKPEVG KGVQL
//
