ID A0A1I1GW97_9BURK Unreviewed; 222 AA.
AC A0A1I1GW97;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=NADH-quinone oxidoreductase subunit J {ECO:0000256|RuleBase:RU004429};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN ORFNames=SAMN05216204_10486 {ECO:0000313|EMBL:SFC15831.1};
OS Massilia yuzhufengensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1164594 {ECO:0000313|EMBL:SFC15831.1, ECO:0000313|Proteomes:UP000198639};
RN [1] {ECO:0000313|EMBL:SFC15831.1, ECO:0000313|Proteomes:UP000198639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12041 {ECO:0000313|EMBL:SFC15831.1,
RC ECO:0000313|Proteomes:UP000198639};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FOLD01000004; SFC15831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1GW97; -.
DR STRING; 1164594.SAMN05216204_10486; -.
DR OrthoDB; 5295927at2; -.
DR Proteomes; UP000198639; 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 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..49
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 55..77
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 89..111
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 142..165
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
SQ SEQUENCE 222 AA; 24017 MW; C9B95D4B36998988 CRC64;
MEFTTGLFYV FATVMVVASL FVITTKNSVH AALFLVLAFF NAAGIWLLLK AEFLAIVLVL
VYVGAVMVLF LFVVMMLDIN IDRMREGFWG YLPLASAIGA LIVLEMSAVL YRAYNLTDLS
AEAAALNIGG TKELGLLIYT KYIYGFEIAA VILLVAIVAA VALTLRKRKD TKAIDPGLAV
RVQRNDRLRI VKMDAVNQRA IDAANVEAAA QAAAAAAPKE AP
//
