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Database: UniProt
Entry: A0A1G5PJ30_9GAMM
LinkDB: A0A1G5PJ30_9GAMM
Original site: A0A1G5PJ30_9GAMM 
ID   A0A1G5PJ30_9GAMM        Unreviewed;       200 AA.
AC   A0A1G5PJ30;
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|ARBA:ARBA00019907, ECO:0000256|RuleBase:RU004429};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN   ORFNames=SAMN03097708_00159 {ECO:0000313|EMBL:SCZ49438.1};
OS   Thiohalomonas denitrificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalomonadales;
OC   Thiohalomonadaceae; Thiohalomonas.
OX   NCBI_TaxID=415747 {ECO:0000313|EMBL:SCZ49438.1, ECO:0000313|Proteomes:UP000199648};
RN   [1] {ECO:0000313|EMBL:SCZ49438.1, ECO:0000313|Proteomes:UP000199648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLD2 {ECO:0000313|EMBL:SCZ49438.1,
RC   ECO:0000313|Proteomes:UP000199648};
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   -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoA, H, J, K, L,
CC       M, N constitute the membrane sector of the complex.
CC       {ECO:0000256|ARBA:ARBA00025811}.
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; FMWD01000001; SCZ49438.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5PJ30; -.
DR   STRING; 415747.SAMN03097708_00159; -.
DR   OrthoDB; 9795409at2; -.
DR   Proteomes; UP000199648; 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:UP000199648};
KW   Transmembrane {ECO:0000256|RuleBase:RU004429};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU004429}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        32..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..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        143..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
SQ   SEQUENCE   200 AA;  22177 MW;  9DEDDA3C2C14175E CRC64;
     MAFEQIVFYA FSAILVFSAG MVITVRNPVH AALFLVLCFF STAGLWLLLR AEFLAIALVL
     VYVGAVMVLF LFVVMMLDIN IAVVREGFAR YLAVGGLVAI VLIAVMAMVV GGDYFGLERT
     PVPEQIGEVG NTRVLGLQLY TNYVYPFEIA SVILLVAIIA AIALTLRRRP DSRYQEPGRQ
     VVARRGDRVR LVSMKSEERR
//
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