NUON_WOLTR
ID NUON_WOLTR Reviewed; 465 AA.
AC Q5GS15;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
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=Wbm0621;
OS Wolbachia sp. subsp. Brugia malayi (strain TRS).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=292805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRS;
RX PubMed=15780005; DOI=10.1371/journal.pbio.0030121;
RA Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N.,
RA Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J.,
RA Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S.,
RA Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D.,
RA Koonin E., Slatko B.;
RT "The Wolbachia genome of Brugia malayi: endosymbiont evolution within a
RT human pathogenic nematode.";
RL PLoS Biol. 3:599-614(2005).
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 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; AE017321; AAW71209.1; -; Genomic_DNA.
DR RefSeq; WP_011256819.1; NC_006833.1.
DR AlphaFoldDB; Q5GS15; -.
DR SMR; Q5GS15; -.
DR STRING; 292805.Wbm0621; -.
DR EnsemblBacteria; AAW71209; AAW71209; Wbm0621.
DR KEGG; wbm:Wbm0621; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_3_5; -.
DR OMA; FYIRVIV; -.
DR OrthoDB; 1664448at2; -.
DR Proteomes; UP000000534; 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; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..465
FT /note="NADH-quinone oxidoreductase subunit N"
FT /id="PRO_0000391245"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 465 AA; 51678 MW; F7C0304AE993AEFB CRC64;
MSYIQILPET FSIISSLVLL LLGIVFNRRT INLLALGCTV ITLIILILSA KDSGFFPFNS
LLKLDLYIRS AQGLILIAGI LVLLLLNLSK YDYEYEFSIL ILFTLFGMIT LVSANNLISF
YLSFELMSIP LYVLASFNKD SVYSCEAGVK YFTLSALSSC IMLYGMSLLY GYTGLVNFSE
LSSFLENHQM TYGIVFGLVL ILIGLCFKLA IAPFHMWAPD VYQGAPTIVT AFFSTVPKAA
LVTFLIRFFM GEELVGVEKY FQPVLLYISA LSVLISAFGA LRQRNLKRLL AYSSIGHIGF
ILASLSIFTR MGTDSSLIYL VIYIITNIGL FSYFIQIDDD DCSVANLSGI GKKRPVLAFH
LSILLFSMAG IPPLAGFFAK LFIFKSLVNS GFIGMSLIFI VASVISCYYY LSIIKAMYFD
KPSDSKVIYS KSLFIVTSVA SLINIVLFMC VEDLYSLIHL VTKSL
