NUON3_STRGG
ID NUON3_STRGG Reviewed; 554 AA.
AC B1W506;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=NADH-quinone oxidoreductase subunit N 3 {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 3 {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NDH-1 subunit N 3 {ECO:0000255|HAMAP-Rule:MF_00445};
GN Name=nuoN3 {ECO:0000255|HAMAP-Rule:MF_00445}; OrderedLocusNames=SGR_2971;
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=455632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350;
RX PubMed=18375553; DOI=10.1128/jb.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(2008).
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}.
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; AP009493; BAG19800.1; -; Genomic_DNA.
DR RefSeq; WP_003967071.1; NC_010572.1.
DR AlphaFoldDB; B1W506; -.
DR SMR; B1W506; -.
DR STRING; 455632.SGR_2971; -.
DR EnsemblBacteria; BAG19800; BAG19800; SGR_2971.
DR GeneID; 6214835; -.
DR KEGG; sgr:SGR_2971; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_1_11; -.
DR OMA; FYIRVIV; -.
DR Proteomes; UP000001685; 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.
FT CHAIN 1..554
FT /note="NADH-quinone oxidoreductase subunit N 3"
FT /id="PRO_0000391231"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 222..242
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 322..342
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 554 AA; 57196 MW; 765A3FD0D456AC26 CRC64;
MSATAVHSLW TTASGVTSAA PGNSFTAPKI EYTQLMPVLI IVVAAVLGIL VEAFVPRRAR
YHTQLFLTVV AVAGSFAAIV GLAAGGYGTT DAGIVAMGAI AIDGPTLFLQ GTILLVAMVA
LFTFAERRLD PGSNGNRVDS FAAQAGSVPG GEGEKAAVRA GFTTTEVFPL LLFSVAGLLV
FPAANDLLTL FIALEVFSLP LYLLCAVARR KRLMSQEAAV KYFLLGAFSS AFLLFGIALL
YGYAGSLSYA DIANVVDGSV LEIDPALADT MGNDALLLIG GAMILTGLLF KVGAVPFHMW
TPDVYQGAPT PVTGFMAAAT KVAAFGALLR LLYVALPGLA WDLRPVMWAV AIVTMLGGAI
VAITQTDIKR LLAYSSIAHA GFILAGVIAA SPEGISSVLF YLLAYSFVTV GAFAVVTLVR
DAGGEATHLS KWAGLGRRSP LVAAVFAVFL LAFAGIPLTS GFSGKFAVFK AAAEGGAGAL
VVVGVLSSAV AAFFYIRVIV LMFFSEPKAD GPTVAVPSPL TMTTIAVGVA VTLVLGLAPQ
YFLDLASQAG VFVR
