NUON_ALIB4
ID NUON_ALIB4 Reviewed; 506 AA.
AC A8ERK3;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=Abu_0302;
OS Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Arcobacteraceae; Aliarcobacter.
OX NCBI_TaxID=367737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM4018;
RX PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A.,
RA Rogosin A., Stanker L.H., Mandrell R.E.;
RT "The complete genome sequence and analysis of the Epsilonproteobacterium
RT Arcobacter butzleri.";
RL PLoS ONE 2:E1358-E1358(2007).
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; CP000361; ABV66577.1; -; Genomic_DNA.
DR RefSeq; WP_012012146.1; NC_009850.1.
DR AlphaFoldDB; A8ERK3; -.
DR SMR; A8ERK3; -.
DR STRING; 367737.Abu_0302; -.
DR EnsemblBacteria; ABV66577; ABV66577; Abu_0302.
DR KEGG; abu:Abu_0302; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_1_7; -.
DR OMA; NAWAPDA; -.
DR OrthoDB; 1664448at2; -.
DR Proteomes; UP000001136; 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..506
FT /note="NADH-quinone oxidoreductase subunit N"
FT /id="PRO_0000391100"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 506 AA; 56474 MW; DAB4CD7FBD2F2F4B CRC64;
MSQFLYLVPT LTILVGALVL MFMSMYDKFN IKNHIFASSV FLIIALLFAL SNVSNSFSVQ
PYESFLNNVL TFDSFSNFFN ILLIAGTLLT LLIGEHYFQH RSYFKGEFFS ILLFALFGMM
VLAQANELIT AFIALEIASF SIYIMVGYNS DDSKRVEAIF KYLVLGSFIG AFYLLGMVLV
YGATTSTNLA DVSTFIATAN QQDMILVYIG LTLILFTFLF KIAAFPFQSW LLDVYRGAPM
IITAYMASTF KIAIFSFFLR VILDYISPII DFWDTILSVV IILTLVFGTW LAVTQQIVKR
MLAASSIVHT GYLLLAFIAL GYKDGHLINI DSAYAVMFYL IAYLLSALGA FGLASHIISE
TNVKVTFDDF KGLAKQRPFL AAMMTIFLLS LAGIPSTIGF IGKIYVFTEA IASGYTLLTV
IAILATIVSV YYYFRLIAVM YFYPAPDNCE TEEFDDKRVS TYAIMFVAIL TVLGGIGSAI
VFFIPAMNID TLINFSQVAV QSLFIR
