ID A0A378I4D7_9GAMM Unreviewed; 480 AA.
AC A0A378I4D7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
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 ECO:0000313|EMBL:STX30077.1};
GN ORFNames=NCTC13315_02640 {ECO:0000313|EMBL:STX30077.1};
OS Legionella beliardensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=91822 {ECO:0000313|EMBL:STX30077.1, ECO:0000313|Proteomes:UP000254968};
RN [1] {ECO:0000313|EMBL:STX30077.1, ECO:0000313|Proteomes:UP000254968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13315 {ECO:0000313|EMBL:STX30077.1,
RC ECO:0000313|Proteomes:UP000254968};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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. 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 membrane {ECO:0000256|HAMAP-Rule:MF_00445};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00445}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC 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; UGNV01000001; STX30077.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A378I4D7; -.
DR OrthoDB; 9768329at2; -.
DR Proteomes; UP000254968; Unassembled WGS sequence.
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 NCBIfam; TIGR01770; NDH_I_N; 1.
DR PANTHER; PTHR22773; NADH DEHYDROGENASE; 1.
DR PANTHER; PTHR22773:SF41; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 2; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01434; NADHDHGNASE5.
PE 3: Inferred from homology;
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:STX30077.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_00445};
KW Reference proteome {ECO:0000313|Proteomes:UP000254968};
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|ARBA:ARBA00023075, ECO:0000256|HAMAP-
KW Rule:MF_00445}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 78..94
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 106..123
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 160..184
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 204..231
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 276..294
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 301..322
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 328..350
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 371..394
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 457..478
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT DOMAIN 125..419
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 480 AA; 52245 MW; 8E2ACDDA3964A1C4 CRC64;
MIPLLDNLSF ALPEIILLVT LTIALLADLF FRHHYKNITL SISLIGLALA GLTSFMLLGN
FKVLILNGLF ISDDIAQLMK IFITLSAFIC FAYSSEYIDE RQMPSGDYYI LGLSSTLGMM
ILVSAHSLLT IYLGLELLSL PLYAMTAIRR TNSDAAEAAL KYFIMGAIAS GMLLYGFSLL
YGATGKLDLT DMANAIAVNW DKQNMLISFA LVFVLVGVGF KLAAVPFHMW APDVYQGAPS
SVTLFISSAP KIAALGMALR LLTIGLIKFA PQWQQLLLAM TLLSTAIGNF VAVNQTNIKR
LLAYSAVAHV GYALFGILAG SAAGYAAATY YILVYSLMTV AAFGFIVLLS RNGYEIEEVN
DLRGLNKRNP WLAFMMLIVM FSMAGVPPTV GFFTKLLVLK ALIDVGMTWV AVLGLIFAVV
GAYYYIRIVK IMYFDDAAEF SEVTLPMSST LLYSANCLSL LFLGIFPSGL INACVNAFTS
//
