ID J7L5A8_NOCAA Unreviewed; 554 AA.
AC J7L5A8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=NADH-quinone oxidoreductase subunit N {ECO:0000256|HAMAP-Rule:MF_00445};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_00445};
DE AltName: Full=NADH dehydrogenase I subunit N {ECO:0000256|HAMAP-Rule:MF_00445};
DE AltName: Full=NDH-1 subunit N {ECO:0000256|HAMAP-Rule:MF_00445};
GN Name=nuoN {ECO:0000256|HAMAP-Rule:MF_00445};
GN OrderedLocusNames=B005_2624 {ECO:0000313|EMBL:AFR05964.1};
OS Nocardiopsis alba (strain ATCC BAA-2165 / BE74).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1205910 {ECO:0000313|EMBL:AFR05964.1, ECO:0000313|Proteomes:UP000003779};
RN [1] {ECO:0000313|EMBL:AFR05964.1, ECO:0000313|Proteomes:UP000003779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2165 / BE74 {ECO:0000313|Proteomes:UP000003779};
RX PubMed=23105086; DOI=10.1128/JB.01522-12;
RA Qiao J., Chen L., Li Y., Wang J., Zhang W., Chen S.;
RT "Whole-Genome Sequence of Nocardiopsis alba Strain ATCC BAA-2165,
RT Associated with Honeybees.";
RL J. Bacteriol. 194:6358-6359(2012).
RN [2] {ECO:0000313|Proteomes:UP000003779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2165 / BE74 {ECO:0000313|Proteomes:UP000003779};
RA Qiao J., Chen L., Li Y., Wang J., Zhang W., Chen S.;
RT "Whole-genome sequence of Nocardiopsis alba strain ATCC BAA-2165 associated
RT with honeybees.";
RL Submitted (AUG-2012) 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00445}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00445};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00445}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU000320}.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC {ECO:0000256|ARBA:ARBA00007012, ECO:0000256|HAMAP-Rule:MF_00445}.
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DR EMBL; CP003788; AFR05964.1; -; Genomic_DNA.
DR RefSeq; WP_014908432.1; NC_018524.1.
DR AlphaFoldDB; J7L5A8; -.
DR STRING; 1205910.B005_2624; -.
DR KEGG; nal:B005_2624; -.
DR PATRIC; fig|1205910.3.peg.2479; -.
DR eggNOG; COG1007; Bacteria.
DR HOGENOM; CLU_007100_1_1_11; -.
DR OrthoDB; 9811718at2; -.
DR Proteomes; UP000003779; Chromosome.
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 NCBIfam; TIGR01770; NDH_I_N; 1.
DR PANTHER; PTHR22773; NADH DEHYDROGENASE; 1.
DR PANTHER; PTHR22773:SF41; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 2; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00445};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00445};
KW NAD {ECO:0000256|HAMAP-Rule:MF_00445};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_00445};
KW Reference proteome {ECO:0000313|Proteomes:UP000003779};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_00445};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00445};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00445}; Transport {ECO:0000256|HAMAP-Rule:MF_00445}.
FT TRANSMEM 26..45
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 150..169
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 175..193
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 205..229
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 257..281
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 293..314
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 326..345
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 352..373
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 379..400
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 425..451
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 463..488
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 500..521
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT DOMAIN 169..474
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 554 AA; 57652 MW; CDECEEC7A1D050E3 CRC64;
MNALYVADGA PPSLPGITEA APTLDWWLLA PYLVVFGAGV LAVLFEAFVP KRSLRPVQIT
VAAAALIAAF ALIVLQVETV GAGGAMIAGG VLAVDGTVLF LQGTIAVLAL VSLMLIAERR
DGRDAFSAQA ATVPGSEEER RHILAGSQHT EVYPLVLFAV LGMLMFPAAN DFLTMFIALE
VMSLPLYLLC ALARRRRLFS QEAAVKYFLL GAFSSAFFLF GIAMVYGYAG SVNFAAIRAA
VESGGAEIFA QGDGEPLLIM GIGLVAIGLL FKVGAVPFHN WKPDVYQGAP TPITALMASC
TLVAAFGALL RVFFVPFGGS VEIWEPMLWT VAILTMVVAA FIAVTQRDVK RLLAYSSVVH
AGFILTAVIA SSTEGLAGAM FYLAAYGFTT LGAFAIVTLV RTRDGGQELG DLDGWAGLGR
RSPGLALALS LFLLAFAGIP LTSGFIGKFA VFEAAVAAGA TPLVVVGVLS SAVTAFFYVR
IIVVMFFRDS EGEGPTVARA GVLTGGVITV GVAATLALGI FPGPVLDNLL PSSETGGEPA
AVMIYQVTDG GTTD
//
