ID A0A0U4WIE5_9PSED Unreviewed; 483 AA.
AC A0A0U4WIE5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=APT59_13560 {ECO:0000313|EMBL:ALZ85170.1};
OS Pseudomonas oryzihabitans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=47885 {ECO:0000313|EMBL:ALZ85170.1, ECO:0000313|Proteomes:UP000064137};
RN [1] {ECO:0000313|EMBL:ALZ85170.1, ECO:0000313|Proteomes:UP000064137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA-ARS-USMARC-56511 {ECO:0000313|EMBL:ALZ85170.1,
RC ECO:0000313|Proteomes:UP000064137};
RA Harhay G.P., Harhay D.M., Smith T.P.L., Bono J.L., Heaton M.P.,
RA Clawson M.L., Chitko-Mckown C.G., Capik S.F., DeDonder K.D., Apley M.D.,
RA Lubbers B.V., White B.J., Larson R.L.;
RT "Annotation of Pseudomonas oryzihabitans USDA-ARS-USMARC-56511.";
RL Submitted (JAN-2016) 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 13 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013987; ALZ85170.1; -; Genomic_DNA.
DR RefSeq; WP_059315336.1; NZ_CP013987.1.
DR AlphaFoldDB; A0A0U4WIE5; -.
DR KEGG; por:APT59_13560; -.
DR OrthoDB; 9768329at2; -.
DR Proteomes; UP000064137; 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 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 Quinone {ECO:0000256|HAMAP-Rule:MF_00445};
KW Reference proteome {ECO:0000313|Proteomes:UP000064137};
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..30
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 42..63
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 75..93
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 105..122
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 160..181
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 201..226
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 270..291
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 298..315
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 327..346
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..427
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 448..470
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT DOMAIN 122..420
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 483 AA; 51787 MW; 99FCFD436211CD76 CRC64;
MTFTYEHFTA LLPIIITGLT AVVVMLGIAW RRDHTIIPTL GVIGLNLALL SCIPALGVGA
IDVTPLLRID GFSCFYMALI LIATLACMTL SHAYMEGYPG NREELYLLLL ISATGGLVLV
AAQNVAGLFI GLELLSVPVY GLVAYSYFNR RSLEAGMKYL VLSAAGSAIL LFGMALLYAQ
SGSLNFADIG MQMDAPASTG LLMEIGLGML IVGLGFKLSL VPFHLWTPDV YEGSPAPVGA
FLATASKVAV FAVLVRVFQT MPMASDDGWL HDAIAFIAIA SMLVGNLLAL MQSNLKRLLG
YSSISHFGYL LVAVASGEGL SMEAVAVYLV TYVFTSLGAF GVITLMSSPS NGQRDADALF
EYRGLFWRRP YLTAALTVMM LSLAGIPLTA GFIGKFYVIT VGVEAGMWWQ TAAIVLGSAI
GLFYYLRVMV TLYLTEQGLQ RHDAPMNWGQ RAGGVMLIAI SIATFVLGVY PQPLLQLAQL
TVF
//
