ID G4E694_9GAMM Unreviewed; 465 AA.
AC G4E694;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=ThisiDRAFT_1823 {ECO:0000313|EMBL:EGZ45086.1};
OS Thiorhodospira sibirica ATCC 700588.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thiorhodospira.
OX NCBI_TaxID=765914 {ECO:0000313|EMBL:EGZ45086.1};
RN [1] {ECO:0000313|EMBL:EGZ45086.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700588 {ECO:0000313|EMBL:EGZ45086.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J.,
RA Frigaard N.-U., Bryant D., Woyke T.;
RT "The draft genome of Thiorhodospira sibirica ATCC 700588.";
RL Submitted (SEP-2011) 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
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: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:EGZ45086.1}.
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DR EMBL; AGFD01000035; EGZ45086.1; -; Genomic_DNA.
DR RefSeq; WP_006787839.1; NZ_MU255056.1.
DR AlphaFoldDB; G4E694; -.
DR STRING; 765914.ThisiDRAFT_1823; -.
DR PATRIC; fig|765914.3.peg.1807; -.
DR eggNOG; COG1007; Bacteria.
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 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 Oxidoreductase {ECO:0000313|EMBL:EGZ45086.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_00445};
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:0000256|ARBA:ARBA00023075, ECO:0000256|HAMAP-
KW Rule:MF_00445}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 38..56
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 76..93
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 100..117
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 123..144
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 156..175
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 195..220
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 290..309
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 356..374
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 394..413
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 440..463
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT DOMAIN 119..407
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 465 AA; 50445 MW; D7BB61D195C86272 CRC64;
MTQLHPMLTG MLVEHILLAG LLLLLILEML TRQRREPLLL TLGTVGLALG VSLWLALQGY
SATPFAGEFS VDPAALIAKA ILLGLSLPVI LSLRGQGLDY RLAALLLSSL YGASLLLSAD
SLIMLFISLE LMSLPLYALI VYGSTHVHRA QAALKYLILG SVGTASLLLG IAWLLGTTGS
LSLSAFTQAL NMDSLPAQTA ALLVLLGLLL KAALVPFHTW APDAYEAASA PLTAYMATVI
KAALFFFIVR LFDQYALPGQ WVSLIVLLAL LSMAWGNLTA MRQTSFKRII AYSSIAHAGY
LLLVLLAVGE QWYGVIAFYL LVYGIATVLA FACLPQRKDG PLLDRLDALQ GLFYQRPWAA
VLIGVAMLSL AGLPPLPGFV AKFYIFQQLI AQGWVLYAVL GLGLSYLGLY FYLRVIQYLF
MHPHDPQAPP LRRAYPTQQL AAALSLTALI CVMLLPGFVM SWLNI
//
