NUON_POLNA
ID NUON_POLNA Reviewed; 500 AA.
AC A1VM73;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=NADH-quinone oxidoreductase subunit N {ECO:0000255|HAMAP-Rule:MF_00445};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NADH dehydrogenase I subunit N {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NDH-1 subunit N {ECO:0000255|HAMAP-Rule:MF_00445};
GN Name=nuoN {ECO:0000255|HAMAP-Rule:MF_00445}; OrderedLocusNames=Pnap_1437;
OS Polaromonas naphthalenivorans (strain CJ2).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=365044;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ2;
RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT tar-contaminated sediment, reveals physiological and metabolic versatility
RT and evolution through extensive horizontal gene transfer.";
RL Environ. Microbiol. 11:2253-2270(2009).
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00445}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00445}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00445}.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00445}.
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DR EMBL; CP000529; ABM36751.1; -; Genomic_DNA.
DR RefSeq; WP_011800838.1; NC_008781.1.
DR AlphaFoldDB; A1VM73; -.
DR SMR; A1VM73; -.
DR STRING; 365044.Pnap_1437; -.
DR EnsemblBacteria; ABM36751; ABM36751; Pnap_1437.
DR KEGG; pna:Pnap_1437; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_3_4; -.
DR OMA; FYIRVIV; -.
DR OrthoDB; 1664448at2; -.
DR Proteomes; UP000000644; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Pfam; PF00361; Proton_antipo_M; 1.
DR TIGRFAMs; TIGR01770; NDH_I_N; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..500
FT /note="NADH-quinone oxidoreductase subunit N"
FT /id="PRO_0000391203"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 106..125
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 129..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 500 AA; 53393 MW; 700471E2104F9E3D CRC64;
MIDKLSWIAV YPELVLLVMA CLIALVDLGV KSPRRTLTYA LTLLTLGAVA VMEASYALGG
QTFYGFGNMV VVDPMGSWLK CFSSIALMIT VVYGRPYAAD RDMLRGGEFF TLSLFALLGM
FVMISGHNFL VLYMGLELMT LCSYALVALR RDDAQATEAA MKYFVLGALA SGFLLYGLSM
LYGATGSLNI NEVFNAIASR QVKHQVLVFG LVFIVAGLAF KLGAVPFHMW LPDVYQGAPT
AVTLIIGGAP QLAAFAMTIR LLVEGLLPLA IDWQQMLALM AIGSLVIGNL AAVAQTNLKR
MLAFSTISQM GFLLLGLLAG VVNGNQLHTE SAYGAAMFYA LTYVLTTLAA FGIILLLARA
GHESEEITDL SGLNQRSPLY AGVMAMSMFS LAGLPPLVGF YAKLGVLQAL ISSGQTSYLV
LAVFAVFMSL IGAFYYLRVI KVMYFDAPHS HNAQPISAPA DAQIVLAING ALLLVLGIAP
SSLMTLCAQS INSIVNSLGV
