ID   NU6C_LEPBY              Reviewed;         199 AA.
AC   Q00243;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase chain 6;
DE            EC=7.1.1.-;
DE   AltName: Full=NAD(P)H dehydrogenase I, chain 6;
DE   AltName: Full=NDH-1, chain 6;
GN   Name=ndhG; Synonyms=ndh6;
OS   Leptolyngbya boryana (Plectonema boryanum).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Leptolyngbyaceae; Leptolyngbya.
OX   NCBI_TaxID=1184;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27894 / CCAP 1463/1 / IAM M-101 / PCC 6306 / UTEX 581;
RA   Takahashi Y., Shonai F., Fujita Y., Kohchi T., Ohyama K., Matsubara H.;
RT   "Structure of a co-transcribed gene cluster, ndh1-frxB-ndh6-ndh4L, cloned
RT   from the filamentous cyanobacterium Plectonema boryanum.";
RL   Plant Cell Physiol. 32:969-981(1991).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NAD(P)H, via FMN and iron-
CC       sulfur (Fe-S) centers, to quinones in the respiratory chain. The
CC       immediate electron acceptor for the enzyme in this species is believed
CC       to be plastoquinone. Couples the redox reaction to proton translocation
CC       (for every two electrons transferred, four hydrogen ions are
CC       translocated across the cytoplasmic membrane), and thus conserves the
CC       redox energy in a proton gradient (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC         H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC         Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC         H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC         Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 6 family. {ECO:0000305}.
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DR   EMBL; D01014; BAA00816.1; -; Genomic_DNA.
DR   PIR; JQ2137; JQ2137.
DR   AlphaFoldDB; Q00243; -.
DR   SMR; Q00243; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.1200; -; 1.
DR   InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6.
DR   InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ.
DR   Pfam; PF00499; Oxidored_q3; 1.
PE   3: Inferred from homology;
KW   Membrane; NAD; NADP; Plastoquinone; Quinone; Translocase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..199
FT                   /note="NAD(P)H-quinone oxidoreductase chain 6"
FT                   /id="PRO_0000118366"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   199 AA;  21299 MW;  E4FD4FC68D442FB9 CRC64;
     MNLAEGVQIV SFAILAAMMI GSAIGVVLLE NVVYSAFLLG GVFISIAGLY LLLNADFVAA
     AQVLIYVGAV NVLILFAIML VNKREAFQPI AKSWIRRAAT ALVCAGIFAL LSAMVLTTPW
     AISTAVPIES SIITIGLHFF TDFLLPFELA SILLLMALVG AIVLARREFL PDEDEADTAL
     TLPERPRELV PAGQNNPEN