ID A0A0D7CBQ5_9ACTN Unreviewed; 287 AA.
AC A0A0D7CBQ5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=NADH-quinone oxidoreductase subunit J {ECO:0000256|RuleBase:RU004429};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN ORFNames=SNA_38475 {ECO:0000313|EMBL:KIZ13345.1};
OS Streptomyces natalensis ATCC 27448.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1240678 {ECO:0000313|EMBL:KIZ13345.1, ECO:0000313|Proteomes:UP000032458};
RN [1] {ECO:0000313|EMBL:KIZ13345.1, ECO:0000313|Proteomes:UP000032458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27448 {ECO:0000313|EMBL:KIZ13345.1,
RC ECO:0000313|Proteomes:UP000032458};
RA Mendes M.V., Beites T., Pires S., Santos C.L., Moradas-Ferreira P.;
RT "Draft genome sequence of Streptomyces natalensis ATCC 27448, producer of
RT the antifungal pimaricin.";
RL Submitted (SEP-2014) 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:KIZ13345.1}.
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DR EMBL; JRKI01000063; KIZ13345.1; -; Genomic_DNA.
DR RefSeq; WP_030067014.1; NZ_JRKI01000063.1.
DR AlphaFoldDB; A0A0D7CBQ5; -.
DR PATRIC; fig|1240678.4.peg.8196; -.
DR Proteomes; UP000032458; 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};
KW Ubiquinone {ECO:0000313|EMBL:KIZ13345.1}.
FT TRANSMEM 14..33
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 40..61
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 67..90
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 142..171
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT REGION 177..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 287 AA; 30274 MW; 984D9C009A06C4FC CRC64;
MTVLAAAAST GEAVQFWLLG IVAVAGALCT IMLRRAVHSA LSLAGTMIVL AIFYLANGAY
FLGIVQIVVY TGAIMMLFLF VVMLVGVTAA DSLKETLKGQ RWLAAGLGIG FGVLLIAGIG
NASLKQFNGL GDANAGGNVQ GLAALIFTKY VFAFEITGAL LITAAVGAMV LTHRERTERA
KSQREQSIAR IKEGKHIPPL PAPGVYARHN AVDIPGLLPD GTPSELTVNP TLRGRGQIRD
VSRESLAELK ALERRSEKWL GRESADEPEP PPSGGPAPKE HTEGAKK
//
