ID A0A1R4J1B3_9SPHI Unreviewed; 487 AA.
AC A0A1R4J1B3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ORFNames=FM107_04560 {ECO:0000313|EMBL:SJN25433.1};
OS Sphingobacterium sp. JB170.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1434842 {ECO:0000313|EMBL:SJN25433.1, ECO:0000313|Proteomes:UP000195951};
RN [1] {ECO:0000313|EMBL:SJN25433.1, ECO:0000313|Proteomes:UP000195951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB170 {ECO:0000313|EMBL:SJN25433.1,
RC ECO:0000313|Proteomes:UP000195951};
RA Peterson S.W.;
RL Submitted (FEB-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. The immediate
CC electron acceptor for the enzyme in this species is believed to be a
CC menaquinone. 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; FUKU01000014; SJN25433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4J1B3; -.
DR OrthoDB; 9811718at2; -.
DR Proteomes; UP000195951; 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; IPR003918; NADH_UbQ_OxRdtase.
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; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
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:SJN25433.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_00445};
KW Reference proteome {ECO:0000313|Proteomes:UP000195951};
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:0000313|EMBL:SJN25433.1}.
FT TRANSMEM 23..40
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 47..63
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 83..101
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 110..126
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 132..154
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 166..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 245..266
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 278..297
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 309..327
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 333..354
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 375..397
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 417..439
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 460..483
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT DOMAIN 130..410
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 487 AA; 53767 MW; 36D3D5BF34C13D54 CRC64;
MNTALTNILD QIINSVPLFK PELALITGFV ISIFSSLFLT KIYKHSTYIT TLLSLIAVGY
LLFDQIGQTA TGFSESWIVD PLSSYARIII VLSAFVITIF IKHRHSCNNG DVYSVLLAAV
LGTHVLSSTS NWLLAFIGIE MVSIASYILV GYFSKNKIQA EAAMKYALFG SVCAAVMLYG
LSLVYGLTGD LNFEATAHLQ GLMDAPELIV SLALLFVFVG IGFKLGFVPF HVWTPDVYQG
APTSITAFLS TIPKVGALIL FARLYRSWSS TDFYFSELLE WYMVVVAIAT MLIGNLAALR
QQDAKRMMAY SSIGHTGFLL MAIYAYQDSA AFLFFYISAY VLMNLAAFLF IDQLEQRTGS
TAINSYAGLG KKMPILFTAF SLVCISLVGL PPTIGFMGKL MVFSALFDFT GAYDNTAVIL
LLAVGALTSV ISLFFYFRIP LYAFLRKSED HAKQRIAPNT LLYVSYAFTI LLIFFGLFPS
FLIDLFN
//
