ID A0A1F9YH49_9BACT Unreviewed; 163 AA.
AC A0A1F9YH49;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 28-JUN-2023, entry version 13.
DE RecName: Full=NADH-quinone oxidoreductase subunit J {ECO:0000256|RuleBase:RU004429};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN ORFNames=A2506_05835 {ECO:0000313|EMBL:OGS38934.1};
OS Elusimicrobia bacterium RIFOXYD12_FULL_66_9.
OC Bacteria; Elusimicrobiota.
OX NCBI_TaxID=1797972 {ECO:0000313|EMBL:OGS38934.1, ECO:0000313|Proteomes:UP000176958};
RN [1] {ECO:0000313|EMBL:OGS38934.1, ECO:0000313|Proteomes:UP000176958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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|RuleBase:RU004429}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:OGS38934.1}.
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DR EMBL; MGVR01000347; OGS38934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F9YH49; -.
DR Proteomes; UP000176958; 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 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 Transmembrane {ECO:0000256|RuleBase:RU004429};
KW Transmembrane helix {ECO:0000256|RuleBase:RU004429}.
FT TRANSMEM 27..46
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 134..157
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
SQ SEQUENCE 163 AA; 16626 MW; A92DBEE6922B5351 CRC64;
MTLWAVALAG AVAVVFAGVM LFHRSLYVSA VCLLVVLLQT GVIFLLRGAP LLGLIQVMVY
AGAVMVLVVV TIMASGGGAG DAPRFADFSF PRWLAFLGLA AALLEGALTL RGLGSAPVMV
AAAPGLSAAF GQALFTSYAL ATEAVTLLMF LASLAIAPDR EAV
//
