ID E3FQE0_STIAD Unreviewed; 519 AA.
AC E3FQE0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=NADH-quinone oxidoreductase subunit N {ECO:0000256|HAMAP-Rule:MF_00445};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_00445};
DE AltName: Full=NADH dehydrogenase I subunit N {ECO:0000256|HAMAP-Rule:MF_00445};
DE AltName: Full=NDH-1 subunit N {ECO:0000256|HAMAP-Rule:MF_00445};
GN Name=nuoN {ECO:0000256|HAMAP-Rule:MF_00445};
GN OrderedLocusNames=STAUR_1641 {ECO:0000313|EMBL:ADO69445.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:ADO69445.1, ECO:0000313|Proteomes:UP000001351};
RN [1] {ECO:0000313|EMBL:ADO69445.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO69445.1,
RC ECO:0000313|Proteomes:UP000001351};
RX PubMed=21037205; DOI=10.1093/molbev/msq292;
RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA Sogaard-Andersen L.;
RT "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL Mol. Biol. Evol. 28:1083-1097(2011).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient. {ECO:0000256|HAMAP-Rule:MF_00445}.
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|HAMAP-Rule:MF_00445};
CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoA, H,
CC J, K, L, M, N constitute the membrane sector of the complex.
CC {ECO:0000256|HAMAP-Rule:MF_00445}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00445}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00445}. Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC {ECO:0000256|ARBA:ARBA00007012, ECO:0000256|HAMAP-Rule:MF_00445}.
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DR EMBL; CP002271; ADO69445.1; -; Genomic_DNA.
DR RefSeq; WP_013374800.1; NZ_AAMD01000048.1.
DR AlphaFoldDB; E3FQE0; -.
DR STRING; 378806.STAUR_1641; -.
DR KEGG; sur:STAUR_1641; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_1_7; -.
DR OrthoDB; 9805769at2; -.
DR Proteomes; UP000001351; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR HAMAP; MF_00445; NDH1_NuoN_1; 1.
DR InterPro; IPR010096; NADH-Q_OxRdtase_suN/2.
DR InterPro; IPR001750; ND/Mrp_mem.
DR PANTHER; PTHR22773; NADH DEHYDROGENASE; 1.
DR PANTHER; PTHR22773:SF41; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 2; 1.
DR Pfam; PF00361; Proton_antipo_M; 2.
DR PRINTS; PR01434; NADHDHGNASE5.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00445};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00445};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00445};
KW NAD {ECO:0000256|HAMAP-Rule:MF_00445};
KW Oxidoreductase {ECO:0000313|EMBL:ADO69445.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_00445};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_00445};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00445};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00445}; Transport {ECO:0000256|HAMAP-Rule:MF_00445};
KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_00445}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 40..61
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 81..99
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 111..128
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 165..188
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 208..233
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 305..326
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 358..379
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 405..428
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT DOMAIN 128..323
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 353..453
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 519 AA; 55142 MW; BF546A8D63F381F8 CRC64;
MTPNLTSADF LPMLPALILV VGACVLLLSE VFLATTSSRG YQTVLATATA VVAATVSVAL
MFQPPQQVFL GYAVLDPFSS FLSFVVCVAL ALAALSSAGF LRRRGAERGE FYALMLFASA
GMTLLAVSAE LITLFVNIEV LSIGTYALTS YLRRGTRPSE AGFKYFILGA FSSAVLLYGA
ALLYGATGHT RLADLSAALP GALVENRALV YSGVMLVAAG FAFKVAAVPF HMWTPDVYEG
APTPVTALMS AGVKAAAFAA MVRVFLSVSQ GMDPQIPFVI FSVLAFLTMI VGNLLALPQR
NVKRMLAYSS IAHAGYLLVG VASLFVNRPG EQFRLLSPTM LGSGSPLELA RADALRGILF
YLLAYTVTAV GAFALISSLE RREDEEKGTA WDLDRFSGLA QRRPGWAVAM AVFMLSLSGI
PPTIGFMSKL LIFRSAVDTG LIGLAIVGML SSAVGVYYYL RVIVYMFMRP VPEGAHTLER
TWTTELTLVL STAAVVLLGI VPGPLKGWLA QAGSLFIGP
//
