NUON_CLOB8
ID NUON_CLOB8 Reviewed; 472 AA.
AC A6LXP5;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Cbei_2986;
OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS acetobutylicum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=290402;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51743 / NCIMB 8052;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA Blaschek H., Richardson P.;
RT "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000721; ABR35125.1; -; Genomic_DNA.
DR AlphaFoldDB; A6LXP5; -.
DR SMR; A6LXP5; -.
DR STRING; 290402.Cbei_2986; -.
DR EnsemblBacteria; ABR35125; ABR35125; Cbei_2986.
DR KEGG; cbe:Cbei_2986; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_5_9; -.
DR OMA; FYIRVIV; -.
DR Proteomes; UP000000565; 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; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
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..472
FT /note="NADH-quinone oxidoreductase subunit N"
FT /id="PRO_5000253552"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 69..89
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 120..140
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 295..315
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 361..381
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 472 AA; 51019 MW; 375ABF3CAE436462 CRC64;
MSYIVELLTA ALCLVLLIAS LSLQRYKEKL SLFTGICLFI ILIVSLFSEA LLNGSQSQSL
FGGAYINDSF STFFKQLFLI AAVLTVLISR DHLVSKQGEF YALIVSALLG MMIMVSSGEL
IAIYIGLELM TISFCVLIAY KGDDKSKEAS LKYLILSAMS SAIFLYGLSL IYGITQTTAI
KEIAEALVTG QIAPLEILGM IFLIAGFAFK IAIVPFHMWA PDIYEGAPTS ITVFLAVASK
TAGLAVLLRL FMTGMSSASS YWIDLIIVLS VITLVLGNLV AIPQTNIKRL LAYSSISQAG
YFLLGIIANS SLGIASILLY SLFYLFANMG AFGVVIAVSK ATGNDQIKDY AYLAKRSPFL
AAVMLISLLS LAGIPPLAGF IGKFYLFLSI IEKGQIWLAF LSIGMSVISV YYYLKVVKVM
YFGESPTKLE SIPVSISTKL ALTISMTVLV ILGIYPSQVV NVVLSVSKAF LS
