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Database: UniProt
Entry: A0A081XWU5_STRTO
LinkDB: A0A081XWU5_STRTO
Original site: A0A081XWU5_STRTO 
ID   A0A081XWU5_STRTO        Unreviewed;       551 AA.
AC   A0A081XWU5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
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   ORFNames=BU52_06195 {ECO:0000313|EMBL:KES08018.1};
OS   Streptomyces toyocaensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=55952 {ECO:0000313|EMBL:KES08018.1, ECO:0000313|Proteomes:UP000028341};
RN   [1] {ECO:0000313|EMBL:KES08018.1, ECO:0000313|Proteomes:UP000028341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 15009 {ECO:0000313|EMBL:KES08018.1,
RC   ECO:0000313|Proteomes:UP000028341};
RA   Hong H.-J., Kwun M.J.;
RT   "The genome announcement of Streptomyces toyocaensis NRRL15009.";
RL   Submitted (FEB-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KES08018.1}.
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DR   EMBL; JFCB01000003; KES08018.1; -; Genomic_DNA.
DR   RefSeq; WP_037929359.1; NZ_JFCB01000003.1.
DR   AlphaFoldDB; A0A081XWU5; -.
DR   STRING; 55952.BU52_06195; -.
DR   eggNOG; COG1007; Bacteria.
DR   OMA; FYIRVIV; -.
DR   OrthoDB; 9811718at2; -.
DR   Proteomes; UP000028341; Unassembled WGS sequence.
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:UP000028341};
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};
KW   Ubiquinone {ECO:0000313|EMBL:KES08018.1}.
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        59..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        101..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        157..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        184..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        217..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        272..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        309..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        342..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        368..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        395..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        437..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        477..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        513..535
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   DOMAIN          181..487
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
SQ   SEQUENCE   551 AA;  57063 MW;  2832A5DB14BB2AD2 CRC64;
     MSATAAVHSL WTTAAADPIS KIDAPKIEYG QLAPILIVVG AAVVGILVEA FVPRRTRYYA
     QLFVAVVALA AAFASVVALA ADGYATTKAG IAAMGAVAVD GPALFLQGTI LLTALVGLFT
     FAERRLDPEA HGNRVDSFAA QAASVPGSDS EKKAVKAGFT TTEVFPLLLF AVAGMLVFPA
     ANDLLTLFVA LEVLSLPLYL LCALARRKRL MSQEAAVKYF LLGAFASAFT LFGIALLYGY
     SGSMSYATIA QVVDGTVPEV TPALADTMGN DVLLLVGAAL LVMGLLFKVG AVPFHMWTPD
     VYQGAPTPVT GFMAAATKVA AFGALLRILY VVLPGLRWDW RPVMWGVAIV TMVVGAVVAI
     TQTDIKRLLA YSAISHAGFI LAGVIAATPS GVSSVLFYLA AYSFVTIGAF AVVTLVRDAG
     GEATHLSKWA GLGRRSPLVA AVFAVFLLAF AGIPLTSGFA GKFAVFKAAA EGGAAPLVVV
     GVIASAIAAF FYIRVIVLMF FSEPRPEGPT VAVPSPLTMT AIGVGVAVTV VLGVAPQYFL
     ELAGDAGVFV R
//
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