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Database: UniProt
Entry: A0A238UPH6_9FLAO
LinkDB: A0A238UPH6_9FLAO
Original site: A0A238UPH6_9FLAO 
ID   A0A238UPH6_9FLAO        Unreviewed;       179 AA.
AC   A0A238UPH6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-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=SAMN04487979_101272 {ECO:0000313|EMBL:SNR24025.1};
OS   Flavobacterium sp. ov086.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1761785 {ECO:0000313|EMBL:SNR24025.1, ECO:0000313|Proteomes:UP000198291};
RN   [1] {ECO:0000313|EMBL:SNR24025.1, ECO:0000313|Proteomes:UP000198291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV086 {ECO:0000313|EMBL:SNR24025.1,
RC   ECO:0000313|Proteomes:UP000198291};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-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}.
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DR   EMBL; FZNL01000001; SNR24025.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238UPH6; -.
DR   OrthoDB; 9790848at2; -.
DR   Proteomes; UP000198291; 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   Transmembrane {ECO:0000256|RuleBase:RU004429};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU004429}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        40..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        64..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        99..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        150..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
SQ   SEQUENCE   179 AA;  20214 MW;  E428A43B94014996 CRC64;
     MIHIPDFAHA TTVQIIFCFL AFITVITAFL TIYSRNPIHS AIYLVICFFS IAGHYLLLNA
     QFLAVVHIIV YSGAIMILFL FTIMLMNLNE QREVHRPRIT RLGAIVSFCL ICIVLIAIFI
     NSKPIVGEYD STGEDFQSIQ VLGKILLNEY MVPFEFASIL LLVAMIGTVL LSKKEKLNK
//
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