ID A0A255ZAE6_9FLAO Unreviewed; 168 AA.
AC A0A255ZAE6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=NADH-quinone oxidoreductase subunit J {ECO:0000256|RuleBase:RU004429};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN ORFNames=CHU92_05060 {ECO:0000313|EMBL:OYQ38429.1};
OS Flavobacterium cyanobacteriorum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2022802 {ECO:0000313|EMBL:OYQ38429.1, ECO:0000313|Proteomes:UP000216605};
RN [1] {ECO:0000313|EMBL:OYQ38429.1, ECO:0000313|Proteomes:UP000216605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH021 {ECO:0000313|EMBL:OYQ38429.1,
RC ECO:0000313|Proteomes:UP000216605};
RA Cai H.;
RT "Flavobacterium cyanobacteriorum sp. nov., isolated from cyanobacterial
RT aggregates in a eutrophic lake.";
RL Submitted (JUL-2017) 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}.
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:OYQ38429.1}.
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DR EMBL; NOXV01000216; OYQ38429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255ZAE6; -.
DR OrthoDB; 9790848at2; -.
DR Proteomes; UP000216605; 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:SF5; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 6, CHLOROPLASTIC; 1.
DR PANTHER; PTHR33269; 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:UP000216605};
KW Transmembrane {ECO:0000256|RuleBase:RU004429};
KW Transmembrane helix {ECO:0000256|RuleBase:RU004429}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 30..47
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 53..75
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 87..109
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 139..160
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
SQ SEQUENCE 168 AA; 18738 MW; 9D1B74A41DBAB515 CRC64;
MITTLFYILS AITLATAFLT ILSKNPIHSA IYLVLCFFSI AGHYLMFNAQ FLAIVHIIVY
SGAIMILMLF TIMLMNLNKE DEKNKSVLSR IAAVVSFCLV ALVLLATFIK AEPQMSRYYA
SGEDYQSIKV LGQVLLNDYM VPFEFASVLL LVSMIGAVLL SKKEYING
//
