NUON_NOCSJ
ID NUON_NOCSJ Reviewed; 533 AA.
AC A1SE40;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=Noca_0533;
OS Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC Nocardioides.
OX NCBI_TaxID=196162;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-499 / JS614;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL Submitted (DEC-2006) 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: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 membrane {ECO:0000255|HAMAP-Rule:MF_00445};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-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; CP000509; ABL80075.1; -; Genomic_DNA.
DR RefSeq; WP_011754025.1; NC_008699.1.
DR AlphaFoldDB; A1SE40; -.
DR SMR; A1SE40; -.
DR STRING; 196162.Noca_0533; -.
DR EnsemblBacteria; ABL80075; ABL80075; Noca_0533.
DR KEGG; nca:Noca_0533; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_1_11; -.
DR OMA; FYIRVIV; -.
DR OrthoDB; 1664448at2; -.
DR Proteomes; UP000000640; 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 membrane; Membrane; NAD; Quinone; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..533
FT /note="NADH-quinone oxidoreductase subunit N"
FT /id="PRO_0000391191"
FT TRANSMEM 13..33
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 87..107
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 141..161
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 200..220
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 310..330
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 373..393
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 451..471
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 533 AA; 56131 MW; 68DF5F7C1A0048E7 CRC64;
MDFIKPTIEY GDVWPLLVVF GVAAVGVLVE GFVPRAQRYL VQAALAIAGV VVALVGTILV
ARDLDVLGDG AARGAIDVEG TIAVDGPALF IWGMLLVFAL GGALLFAERR LEGGVSAFAG
QAAALPGTEA ERQASTRGLE HTEVYPLMMF ALGGMMLFAA ANDLLTLFVA LEVLSLPLYL
LSGLARRRRL LSQEAALKYF MLGAFSSGFF LYGAALVYGF SGSMGFAEIN EAVRDDVGNQ
TLLLIGIGML SVGLLFKVGA VPFHSWTPDV YQGAPTAVTA FMAAGTKIAA FGAMLRLFYV
AFGSDRWSWQ PMLWIIAILT MLVGALIAIV QTDMKRMLAY SSVAHTGFLL TGVLGVQQAS
ELADGEVTSL QAVLFYLVTY GFAVVGAFAV VTLVRDAGGE AGQFVRWRGI GRRSPLVAGV
FAFFLLSMAG IPLTAGFVGK WAVFTVALAA GAWPVVIAAV LCSIIAVFFY VRVILLMFFE
DDDVSAQGEV ASVTKPSVLT SATIFVGVAA TLVLGVVPGP VLDLAANAGQ FVR
