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Database: UniProt
Entry: A0A1G6ZCR5_9ACTN
LinkDB: A0A1G6ZCR5_9ACTN
Original site: A0A1G6ZCR5_9ACTN 
ID   A0A1G6ZCR5_9ACTN        Unreviewed;       164 AA.
AC   A0A1G6ZCR5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=NADH-quinone oxidoreductase subunit J {ECO:0000256|RuleBase:RU004429};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN   ORFNames=SAMN05216270_110182 {ECO:0000313|EMBL:SDE00428.1};
OS   Glycomyces harbinensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC   Glycomyces.
OX   NCBI_TaxID=58114 {ECO:0000313|EMBL:SDE00428.1, ECO:0000313|Proteomes:UP000198949};
RN   [1] {ECO:0000313|EMBL:SDE00428.1, ECO:0000313|Proteomes:UP000198949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3516 {ECO:0000313|EMBL:SDE00428.1,
RC   ECO:0000313|Proteomes:UP000198949};
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|ARBA:ARBA00005698, ECO:0000256|RuleBase:RU004429}.
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DR   EMBL; FNAD01000010; SDE00428.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6ZCR5; -.
DR   STRING; 58114.SAMN05216270_110182; -.
DR   Proteomes; UP000198949; 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:SF20; 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..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        31..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        55..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        96..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        138..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
SQ   SEQUENCE   164 AA;  16711 MW;  AE17CB4A42745F0E CRC64;
     MTLADVLLLA FGLLALGAAL AVVTTRRIVR AGLWLAVAFA GIAGAALVLT AEFLAWVLVL
     VYVGAIVVLL LFATMLTKAP TDASDDLDRA RWPGMVAAGG IGLGLGVVVT AAFGWIRVDP
     AGRDGGAAAM GEAVFADWVL PFEVLSLLLL AALVGAVVVS TRAK
//
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