ID A0A1T3NXM3_9ACTN Unreviewed; 330 AA.
AC A0A1T3NXM3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=NADH-quinone oxidoreductase subunit J {ECO:0000256|RuleBase:RU004429};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN ORFNames=B4N89_11730 {ECO:0000313|EMBL:OPC81524.1};
OS Embleya scabrispora.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Embleya.
OX NCBI_TaxID=159449 {ECO:0000313|EMBL:OPC81524.1, ECO:0000313|Proteomes:UP000190037};
RN [1] {ECO:0000313|EMBL:OPC81524.1, ECO:0000313|Proteomes:UP000190037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF3 {ECO:0000313|EMBL:OPC81524.1,
RC ECO:0000313|Proteomes:UP000190037};
RA Vazquez M., Ceapa C.D., Rodriguez Luna D., Sanchez Esquivel S.;
RT "Draft genome sequence of Streptomyces scabrisporus NF3, endophyte isolated
RT from Amphipterygium adstringens.";
RL Submitted (MAR-2017) 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:OPC81524.1}.
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DR EMBL; MWQN01000001; OPC81524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T3NXM3; -.
DR STRING; 159449.B4N89_11730; -.
DR eggNOG; COG0839; Bacteria.
DR OrthoDB; 13239at2; -.
DR Proteomes; UP000190037; 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:UP000190037};
KW Transmembrane {ECO:0000256|RuleBase:RU004429};
KW Transmembrane helix {ECO:0000256|RuleBase:RU004429};
KW Ubiquinone {ECO:0000313|EMBL:OPC81524.1}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 46..67
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 73..96
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 108..130
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 175..197
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT REGION 279..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 330 AA; 34621 MW; 4AD4E6CC94D7D957 CRC64;
MSPGMDFAAE VTKTSTGEAL QFWVLAAVAL IGALATVFMK KAVHSALALV TTMMCLAIFY
LAQGAVFLGI VQIVVYTGAI MMLFLFVLML VGVSSVDSLK ETLKGQRIAA AGLGLGFGIL
LTSAIANASI THFTALATKS AGSRPVYPAE TDEEALRAVS QGNVQGLAHQ IFTKYIWAFE
MTSALLITAA VGAMVLAHRE RLVPRKTQRE LSEERVRDNK QVAPLPTPGV YARHNAVDVP
ALLPDGSISE LSVNGTLRAR GQIRDVSAEA VHSVAALESA GADDDDEAWP DESDAPASAP
VPTARHEHED PDPGSGDEVG AGAGSKEGRS
//
