ID A0A0J5FY20_9GAMM Unreviewed; 176 AA.
AC A0A0J5FY20;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=NADH-quinone oxidoreductase subunit J {ECO:0000256|ARBA:ARBA00019907, ECO:0000256|RuleBase:RU004429};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN ORFNames=AB204_00180 {ECO:0000313|EMBL:KMJ47098.1};
OS Xenorhabdus khoisanae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=880157 {ECO:0000313|EMBL:KMJ47098.1, ECO:0000313|Proteomes:UP000036277};
RN [1] {ECO:0000313|EMBL:KMJ47098.1, ECO:0000313|Proteomes:UP000036277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCB {ECO:0000313|EMBL:KMJ47098.1,
RC ECO:0000313|Proteomes:UP000036277};
RA Naidoo S., Featherston J., Gray V.M.;
RT "Draft Whole-Genome Sequence of the Entomopathogenic Bacterium Xenorhabdus
RT khoisanae.";
RL Submitted (JUN-2015) 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 -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoA, H, J, K, L,
CC M, N constitute the membrane sector of the complex.
CC {ECO:0000256|ARBA:ARBA00025811}.
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:KMJ47098.1}.
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DR EMBL; LFCV01000001; KMJ47098.1; -; Genomic_DNA.
DR RefSeq; WP_047961373.1; NZ_LFCV01000001.1.
DR AlphaFoldDB; A0A0J5FY20; -.
DR STRING; 880157.AB204_00180; -.
DR PATRIC; fig|880157.4.peg.38; -.
DR Proteomes; UP000036277; 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 Oxidoreductase {ECO:0000313|EMBL:KMJ47098.1};
KW Quinone {ECO:0000256|RuleBase:RU004429};
KW Transmembrane {ECO:0000256|RuleBase:RU004429};
KW Transmembrane helix {ECO:0000256|RuleBase:RU004429};
KW Ubiquinone {ECO:0000313|EMBL:KMJ47098.1}.
FT TRANSMEM 6..21
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 28..50
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 56..81
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 93..111
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 131..156
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
SQ SEQUENCE 176 AA; 19127 MW; 42B0F9A1B54058A0 CRC64;
MEFTFYVAGL VAILATLRVV THTNPVHALL YLIISLLALS VVFFSLGAYF AGALEIIVYA
GAIMVLFVFV VMMLNLGKSV VEQERAWLQP RAWIGPSILS IVLLIVLSYA ISRLPPAEIS
GEVVSAKEVG ISLFGPYVLA VELASLLLLA GIVVAYHIGR ENRQGEVISN RVEDQQ
//
