NUON2_SYMTH
ID NUON2_SYMTH Reviewed; 508 AA.
AC Q67KP6;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=NADH-quinone oxidoreductase subunit N 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NDH-1 subunit N 2 {ECO:0000255|HAMAP-Rule:MF_00445};
GN Name=nuoN2 {ECO:0000255|HAMAP-Rule:MF_00445}; OrderedLocusNames=STH2767;
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863;
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(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 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; AP006840; BAD41752.1; -; Genomic_DNA.
DR AlphaFoldDB; Q67KP6; -.
DR SMR; Q67KP6; -.
DR STRING; 292459.STH2767; -.
DR EnsemblBacteria; BAD41752; BAD41752; STH2767.
DR KEGG; sth:STH2767; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_5_9; -.
DR OMA; FYIRVIV; -.
DR Proteomes; UP000000417; 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..508
FT /note="NADH-quinone oxidoreductase subunit N 2"
FT /id="PRO_0000391234"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 223..243
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 298..318
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 433..455
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 508 AA; 53747 MW; 3526A2DB4CCD79A4 CRC64;
MPGVVSWSQL VNPSYVAILP HLIVTATLLV VIVLDAYFKE KRSLVWVTLG GVVLAMLSIW
YTASDPQIQA GIAAGRPPEF WGGMIIADGF TFFMNGVLLG IAALVILLSA DYVGKFLRGA
HMEFYEIILA VTLGMMFMVS SRDLLTIYIG LELTSISSYV LAGILRKDAK SNEAALKYFL
TGATASAVLL FGLSLIYGVT GSTRLPEVAA ALAGGSHVVA AAGPALTPLL VAGMAFLMVG
FGFKVAAVPV HQWAPDVYEG APTPVTAFFS AGPKGAAMAA ILRVFVGGLG VAPFTDKWAL
IWALAAAASM TVGNLVALQQ TNIKRMMAYS SIAQAGYILV GVAASGLQSV EGISSVLFYV
MAYAVTNLGI FAVLTHMDQE GGWVEVDNYA GLAKRNPLYA WALLLFFVSL IGIPPTVGFL
GKFFLFRAAA ASGYLWLAVL MAVNSVISVG YYYRVVKVMF LDQSDYPALT PSTGISATVL
LSLLGVVALT IFANPFVQWT AQSAALLH
