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Database: UniProt
Entry: A0A1M6TNY3_9ACTN
LinkDB: A0A1M6TNY3_9ACTN
Original site: A0A1M6TNY3_9ACTN 
ID   A0A1M6TNY3_9ACTN        Unreviewed;       313 AA.
AC   A0A1M6TNY3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=NADH-quinone oxidoreductase subunit J {ECO:0000256|RuleBase:RU004429};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN   ORFNames=SAMN05421803_12438 {ECO:0000313|EMBL:SHK58626.1};
OS   Nocardiopsis flavescens.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=758803 {ECO:0000313|EMBL:SHK58626.1, ECO:0000313|Proteomes:UP000184452};
RN   [1] {ECO:0000313|EMBL:SHK58626.1, ECO:0000313|Proteomes:UP000184452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5723 {ECO:0000313|EMBL:SHK58626.1,
RC   ECO:0000313|Proteomes:UP000184452};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQZK01000024; SHK58626.1; -; Genomic_DNA.
DR   RefSeq; WP_073383134.1; NZ_FQZK01000024.1.
DR   AlphaFoldDB; A0A1M6TNY3; -.
DR   STRING; 758803.SAMN05421803_12438; -.
DR   OrthoDB; 13239at2; -.
DR   Proteomes; UP000184452; 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   Reference proteome {ECO:0000313|Proteomes:UP000184452};
KW   Transmembrane {ECO:0000256|RuleBase:RU004429};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU004429}.
FT   TRANSMEM        25..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        55..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        80..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        113..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        163..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   REGION          190..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..208
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..303
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   313 AA;  32399 MW;  0067E6D56DD32124 CRC64;
     MTSAVPLAAP HEVHLAAPIG GGEAAAFWIL GAVVLLGALG VVFSRKAVHS AMSMALTMVG
     LAIFYGINAA PFLMVVQIVV YTGAVLMLFL FVLMLVGVSS ADSLKETLGG QRLLTAVVAL
     GFIGALATGI TRISVGDPVG LAAGTAAAGG SIPWIAGELL LRYVVAFEAT AALLVTAVLG
     ALVLAHTTRT KKRRTQREIS EDRIRGDHPT PLPGPGTYAR HNAIDMPALL PDGQVARLSL
     NPVLTARDPE YQSRVPEDVR AGRPPLPGGG SDPARSEEGG PTAGDHPREA DADTADGVRE
     NGDGQEVEST WTR
//
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