ID A0A0M3QDG6_SPHS1 Unreviewed; 203 AA.
AC A0A0M3QDG6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=NADH-quinone oxidoreductase subunit J {ECO:0000256|RuleBase:RU004429};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN ORFNames=LH20_11435 {ECO:0000313|EMBL:ALC12563.1};
OS Sphingopyxis sp. (strain 113P3).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=292913 {ECO:0000313|EMBL:ALC12563.1, ECO:0000313|Proteomes:UP000061305};
RN [1] {ECO:0000313|EMBL:ALC12563.1, ECO:0000313|Proteomes:UP000061305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=113P3 {ECO:0000313|EMBL:ALC12563.1,
RC ECO:0000313|Proteomes:UP000061305};
RX PubMed=26472829;
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete Genome Sequence of Polyvinyl Alcohol-Degrading Strain
RT Sphingopyxis sp. 113P3 (NBRC 111507).";
RL Genome Announc. 3:e01169-15(2015).
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; CP009452; ALC12563.1; -; Genomic_DNA.
DR RefSeq; WP_053554266.1; NZ_CP009452.1.
DR AlphaFoldDB; A0A0M3QDG6; -.
DR STRING; 292913.LH20_11435; -.
DR KEGG; sphp:LH20_11435; -.
DR PATRIC; fig|292913.6.peg.2313; -.
DR OrthoDB; 9795409at2; -.
DR Proteomes; UP000061305; Chromosome.
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:UP000061305};
KW Transmembrane {ECO:0000256|RuleBase:RU004429};
KW Transmembrane helix {ECO:0000256|RuleBase:RU004429};
KW Ubiquinone {ECO:0000313|EMBL:ALC12563.1}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 31..50
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 56..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 90..112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 144..165
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT REGION 174..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 203 AA; 21870 MW; 53D449E6B01F141B CRC64;
MIQLIAFYLF AFLVIASAAM VIFARNPVHS VMWLILAFFN AAGLMLLAGA EFIAMLLVIV
YVGAVAVLFL FVVMMLDIDF AELRAGFVRY LPLGALVAII LAAELVFALG AWSAGGIDLA
ARAAPAVADK SNIQQIGELL YTRYIFLFEA AGIVLLVAMI GAIALTHRQR GGTRSQKIAA
QNRRRPDEAT RLVDPGVGQG MEL
//
