ID A0A1I0YWY7_9ACTN Unreviewed; 277 AA.
AC A0A1I0YWY7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=NADH-quinone oxidoreductase subunit J {ECO:0000256|RuleBase:RU004429};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN ORFNames=SAMN05192575_104312 {ECO:0000313|EMBL:SFB17854.1};
OS Nocardioides alpinus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=748909 {ECO:0000313|EMBL:SFB17854.1, ECO:0000313|Proteomes:UP000199113};
RN [1] {ECO:0000313|EMBL:SFB17854.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10697 {ECO:0000313|EMBL:SFB17854.1};
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|RuleBase:RU004429}.
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DR EMBL; FOKC01000004; SFB17854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0YWY7; -.
DR STRING; 748909.SAMN05192575_104312; -.
DR OrthoDB; 13239at2; -.
DR Proteomes; UP000199113; 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:SF19; NADH-QUINONE OXIDOREDUCTASE SUBUNIT J; 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 6..21
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 26..44
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 50..72
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 92..117
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 137..159
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT REGION 245..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 277 AA; 28998 MW; 19B6DAF56D59FF70 CRC64;
MTFWILAPLM VLSALGILFV RKAVHAALLL AVVMISLAFL YAVMDAPFLF AVQIIVYTGA
ILMLFLFVMM LIGVDASDSV VETIRGQRVM AIVVGLAFGT VLVVGISQVA FGTVVGLDEA
NAGGNVPAIA NILFSKYVFA FEATSALLIT AAVGAMVLAH RERLTPKPTQ ASMAAQRMRD
YADHGKHLGP LPSPGVYARH NAVDTPALLP DGTAAESSVS RVLAARGTVR SAPALADDID
DVRRQLGGLD GHSDPTTMPG ASGRSGAPAN TEEDVDK
//