ID I7A314_MELRP Unreviewed; 169 AA.
AC I7A314;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=NADH-quinone oxidoreductase subunit J {ECO:0000256|RuleBase:RU004429};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN OrderedLocusNames=MROS_2373 {ECO:0000313|EMBL:AFN75603.1};
OS Melioribacter roseus (strain JCM 17771 / P3M-2).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Melioribacteraceae; Melioribacter.
OX NCBI_TaxID=1191523 {ECO:0000313|EMBL:AFN75603.1, ECO:0000313|Proteomes:UP000009011};
RN [1] {ECO:0000313|EMBL:AFN75603.1, ECO:0000313|Proteomes:UP000009011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17771 / P3M-2 {ECO:0000313|Proteomes:UP000009011};
RX PubMed=23301019; DOI=10.1371/journal.pone.0053047;
RA Kadnikov V.V., Mardanov A.V., Podosokorskaya O.A., Gavrilov S.N.,
RA Kublanov I.V., Beletsky A.V., Bonch-Osmolovskaya E.A., Ravin N.V.;
RT "Genomic analysis of Melioribacter roseus, facultatively anaerobic
RT organotrophic bacterium representing a novel deep lineage within
RT Bacteriodetes/Chlorobi group.";
RL PLoS ONE 8:E53047-E53047(2013).
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; CP003557; AFN75603.1; -; Genomic_DNA.
DR RefSeq; WP_014857033.1; NC_018178.1.
DR AlphaFoldDB; I7A314; -.
DR STRING; 1191523.MROS_2373; -.
DR GeneID; 78567286; -.
DR KEGG; mro:MROS_2373; -.
DR eggNOG; COG0839; Bacteria.
DR HOGENOM; CLU_085957_2_2_10; -.
DR OrthoDB; 981464at2; -.
DR Proteomes; UP000009011; 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:UP000009011};
KW Transmembrane {ECO:0000256|RuleBase:RU004429};
KW Transmembrane helix {ECO:0000256|RuleBase:RU004429}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 30..49
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 55..77
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 89..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 138..160
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
SQ SEQUENCE 169 AA; 18458 MW; 429538644E65B726 CRC64;
MSYFDIIFYL FAIITVASAF IVVTTRNIVY SAYSLLLTLF GISGIYVLLG ADFLAVVQIM
VYVGGILILL LFGVMLTNKI TSVDIRTGAV HLLPAAISSG VLLGILWAVM TWTDWKTYDA
QIPSTTIFGL GKILITNYVL IFELLAILLL VALIGAASIA RREESEENN
//
