ID A0A0C5FT89_9ACTN Unreviewed; 280 AA.
AC A0A0C5FT89;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-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=TU94_19100 {ECO:0000313|EMBL:AJP03267.1};
OS Streptomyces cyaneogriseus subsp. noncyanogenus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=477245 {ECO:0000313|EMBL:AJP03267.1, ECO:0000313|Proteomes:UP000032234};
RN [1] {ECO:0000313|EMBL:AJP03267.1, ECO:0000313|Proteomes:UP000032234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NMWT 1 {ECO:0000313|EMBL:AJP03267.1,
RC ECO:0000313|Proteomes:UP000032234};
RA Wang H., Li C., Xiang W., Wang X.;
RT "Genome sequence of thermotolerant Streptomyces cyaneogriseus subsp.
RT Noncyanogenus NMWT1, the producer of nematocidal antibiotics nemadectin.";
RL Submitted (FEB-2015) 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; CP010849; AJP03267.1; -; Genomic_DNA.
DR RefSeq; WP_044383174.1; NZ_CP010849.1.
DR AlphaFoldDB; A0A0C5FT89; -.
DR STRING; 477245.TU94_19100; -.
DR KEGG; scw:TU94_19100; -.
DR PATRIC; fig|477245.3.peg.4032; -.
DR HOGENOM; CLU_067307_1_0_11; -.
DR OrthoDB; 13239at2; -.
DR Proteomes; UP000032234; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000032234};
KW Transmembrane {ECO:0000256|RuleBase:RU004429};
KW Transmembrane helix {ECO:0000256|RuleBase:RU004429};
KW Ubiquinone {ECO:0000313|EMBL:AJP03267.1}.
FT TRANSMEM 16..35
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 42..63
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 69..92
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 104..122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 152..173
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT REGION 260..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 280 AA; 30058 MW; 464C5A86FC97B70A CRC64;
MTAQLAAYST STGEAVQFWV LGTVAVIGAL CTVFMKRAVH SALCLAGTMI VLAVFYLANG
AYFLGVVQIV VYTGAIMMLF LFVVMLVGVT AADSLKETIR GQRWLALVCG LGFGILLIAG
IGNASLKEFN GIGQANAGGN VEGIASLLFT KYVFAFEITG ALLITAAIGA MVLTHRERTE
RAKTQRELAE QRVREGTYLP PLPAPGVYAR HNAVDIAGLL PDGTPSELTV SRTLRERGQI
RDVSQEALGD LRALEQRAEE RLERKGTVPP PFKRSEEASK
//
