ID A0A1Q5JPR4_9ACTN Unreviewed; 281 AA.
AC A0A1Q5JPR4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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=AMK32_39355 {ECO:0000313|EMBL:OKJ71316.1};
OS Streptomyces sp. CB01883.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703943 {ECO:0000313|EMBL:OKJ71316.1, ECO:0000313|Proteomes:UP000186398};
RN [1] {ECO:0000313|EMBL:OKJ71316.1, ECO:0000313|Proteomes:UP000186398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01883 {ECO:0000313|EMBL:OKJ71316.1,
RC ECO:0000313|Proteomes:UP000186398};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKJ71316.1}.
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DR EMBL; LIWA01000014; OKJ71316.1; -; Genomic_DNA.
DR RefSeq; WP_073901862.1; NZ_LIWA01000014.1.
DR AlphaFoldDB; A0A1Q5JPR4; -.
DR OrthoDB; 13239at2; -.
DR Proteomes; UP000186398; 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 Reference proteome {ECO:0000313|Proteomes:UP000186398};
KW Transmembrane {ECO:0000256|RuleBase:RU004429};
KW Transmembrane helix {ECO:0000256|RuleBase:RU004429};
KW Ubiquinone {ECO:0000313|EMBL:OKJ71316.1}.
FT TRANSMEM 17..36
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 43..64
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 70..93
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 145..174
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
SQ SEQUENCE 281 AA; 30267 MW; 5DF8B4A678E1E7B4 CRC64;
MNETQLAAYT TSTGEAFQFW VLGTVAVIGA LCTVFMKKAV HSALCLAGTM IVLAVFYLAN
GAYFLGIVQI VVYTGAIMML FLFVVMLVGV TAADSLKETI KGQRWLALLC GVGFGVLLFA
GIANASLKDF DGIGGANANG NVEGLAALIF TKYVFAFEIT GALLITAAVG AMVLTHRERT
ERAKTQRELA EQRIREGVHI PPLPAPGVYA RHNAVDIAGL LPDGTTSELT VSKTLRERGQ
IRDVSTEALN DLKALEQRAE ERLERRVVEP ATFKRSEEAS K
//
