NUON_RHOCA
ID NUON_RHOCA Reviewed; 478 AA.
AC P50973;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 85.
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};
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33303 / B10;
RX PubMed=8566820; DOI=10.1016/0378-1119(95)00693-1;
RA Dupuis A., Peinnequin A., Chevallet M., Lunardi J., Darrouzet E.,
RA Pierrard B., Procaccio V., Issartel J.P.;
RT "Identification of five Rhodobacter capsulatus genes encoding the
RT equivalent of ND subunits of the mitochondrial NADH-ubiquinone
RT oxidoreductase.";
RL Gene 167:99-104(1995).
RN [2]
RP SUBCELLULAR LOCATION IN CHROMATOPHORE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33303 / B10;
RX PubMed=9632256; DOI=10.1046/j.1365-2958.1998.00814.x;
RA Dupuis A., Darrouzet E., Duborjal H., Pierrard B., Chevallet M.,
RA van Belzen R., Albracht S.P.J., Lunardi J.;
RT "Distal genes of the nuo operon of Rhodobacter capsulatus equivalent to the
RT mitochondrial ND subunits are all essential for the biogenesis of the
RT respiratory NADH-ubiquinone oxidoreductase.";
RL Mol. Microbiol. 28:531-541(1998).
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.
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 (Probable).
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC {ECO:0000269|PubMed:9632256}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00445, ECO:0000269|PubMed:9632256}.
CC -!- DISRUPTION PHENOTYPE: No functional NADH-quinone oxidoreductase
CC complex. Cells lacking this gene have a nearly normal respiratory
CC growth phenotype on lactate, however they are unable to perform
CC anaerobic photosynthesis. It is suggested that in R.capsulatus this
CC complex may function in reverse flow under physiological conditions.
CC {ECO:0000269|PubMed:9632256}.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00445}.
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DR EMBL; AF029365; AAC25005.1; -; Genomic_DNA.
DR RefSeq; WP_013067261.1; NZ_VIBE01000008.1.
DR AlphaFoldDB; P50973; -.
DR SMR; P50973; -.
DR GeneID; 31490417; -.
DR OMA; FYIRVIV; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0042717; C:plasma membrane-derived chromatophore 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 Membrane; NAD; Quinone; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..478
FT /note="NADH-quinone oxidoreductase subunit N"
FT /id="PRO_0000117696"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 478 AA; 50128 MW; F95DF45E5DEAC94D CRC64;
MTKAEFSLVL PEVLLAIYAM GVLLFGVWTG KDRVAKPILW ASAVTMLALA LIIGLGTGND
TAFGGLFIAD GFARFSKVVI LVSAAAVLAM SSDYMGRRGL LRFEYPILIV LAVVGMMMMV
SAGDLMSLYI GLELQSLALY VVAALRRDSA VSSEAGLKYF VLGSLSSGLL LYGASLVYGF
AGTTTFSGII TVVEQGHLPI GLLFGLVFLL AGLAFKVSAV PFHMWTPDVY EGSPTPVTAF
FATAPKLAAM ALIARVVHDA FGQVPGEWGQ ILAALALASM YLGAIAGIGQ RDIKRLMAYS
SISHMGFGLL GLAAGTAAGV ESMLLYMTIY IVMNVGTFAF ILSMERDGKP VTEIAALNML
SKTDPVKAFA LLVLLFSLAG VPPMLGFFAK FAVIKAAIGA GFVWVPVAAV VASVIGAFYY
LRIVYFMYFG EKSAPLDGRM PALQFAFLVL AAVAMLGGAI NMAGVEGAAQ AAAASLVN
