NUON_PARUW
ID NUON_PARUW Reviewed; 480 AA.
AC Q6MDQ3;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=pc0572;
OS Protochlamydia amoebophila (strain UWE25).
OC Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC Candidatus Protochlamydia.
OX NCBI_TaxID=264201;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWE25;
RX PubMed=15073324; DOI=10.1126/science.1096330;
RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA Mewes H.-W., Wagner M.;
RT "Illuminating the evolutionary history of chlamydiae.";
RL Science 304:728-730(2004).
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; BX908798; CAF23296.1; -; Genomic_DNA.
DR RefSeq; WP_011175122.1; NC_005861.1.
DR AlphaFoldDB; Q6MDQ3; -.
DR SMR; Q6MDQ3; -.
DR STRING; 264201.pc0572; -.
DR EnsemblBacteria; CAF23296; CAF23296; PC_RS02735.
DR KEGG; pcu:PC_RS02735; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_5_0; -.
DR OMA; YYLQWTA; -.
DR OrthoDB; 1664448at2; -.
DR Proteomes; UP000000529; 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..480
FT /note="NADH-quinone oxidoreductase subunit N"
FT /id="PRO_0000391207"
FT TRANSMEM 10..30
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 80..100
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 246..266
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 304..324
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 409..431
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 480 AA; 52626 MW; B21ACD1FE167A360 CRC64;
MNPTLTLTDF ISIGPLLIVL MTALIIILIE SFSENCSKKW SSLISIGGLT LSIFAVWGGI
SSNHSSLLNP WIHFDTLARF FTVFFLVIGI GASLLATAFF QRFKASHGEY FFLLQSAVFG
LILIGAAADL LTLFLGIETL SISLYVLCGY MKKWEISHES SFKYFLMGSI VAGFLLYGIA
LVYGAIGTTR LDVLLSSYQT ISLTTEKVLF FSGIAMITLG LAFKAALVPF HTWSPDVYAG
ASNPVTAFMA VGTKVGVFAA FVRLFFEALP QFDAAWNQVI DTLVYATLIY ANFVALKQIQ
LRRFFAYSSI SHAGFLMIPV VIGNQEALSA LTFYLVIYAI ATFGCFAVLA YLDQNQEGVH
FSDLHGLFSR SPWLASLLSI CLLTLAGIPP TAGFLAKFYV FKVAFQAGYY GLVIVGLLTT
ILSSYYYLRI IGILFSESKN DEKLPYSMPA AIVGTTSFIA IIILSFYPAP FLKVLSHLSN
