NU6C_PAUCH
ID NU6C_PAUCH Reviewed; 205 AA.
AC B1X496;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 6, organellar chromatophore;
DE EC=7.1.1.-;
DE AltName: Full=NAD(P)H dehydrogenase subunit 6;
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 6;
GN Name=ndhG; OrderedLocusNames=PCC_0324;
OS Paulinella chromatophora.
OG Plastid; Organellar chromatophore.
OC Eukaryota; Sar; Rhizaria; Imbricatea; Silicofilosea; Euglyphida;
OC Paulinellidae; Paulinella.
OX NCBI_TaxID=39717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18356055; DOI=10.1016/j.cub.2008.02.051;
RA Nowack E.C.M., Melkonian M., Gloeckner G.;
RT "Chromatophore genome sequence of Paulinella sheds light on acquisition of
RT photosynthesis by eukaryotes.";
RL Curr. Biol. 18:410-418(2008).
CC -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN
CC and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain
CC and possibly in a chloroplast respiratory chain. The immediate electron
CC acceptor for the enzyme in this species is believed to be
CC plastoquinone. Couples the redox reaction to proton translocation, and
CC thus conserves the redox energy in a proton gradient (By similarity).
CC {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 -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC are encoded in the nucleus. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, organellar chromatophore thylakoid
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I subunit 6 family. {ECO:0000305}.
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DR EMBL; CP000815; ACB42765.1; -; Genomic_DNA.
DR RefSeq; YP_002048975.1; NC_011087.1.
DR AlphaFoldDB; B1X496; -.
DR SMR; B1X496; -.
DR GeneID; 6481774; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070118; C:organellar chromatophore thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; 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; Organellar chromatophore; Plastid; Plastoquinone;
KW Quinone; Thylakoid; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..205
FT /note="NAD(P)H-quinone oxidoreductase subunit 6, organellar
FT chromatophore"
FT /id="PRO_0000360297"
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 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 205 AA; 22325 MW; 7E44ABCCF690DE75 CRC64;
MTISNATQLI CFFALSATLI LGALGVVLLP NIVYSAFLLG SVFLSVAGLY LLLNASFVAA
AQVLIYVGAV NVLILFAIML VNREEELKVI PGLAIRRFFS GVVCMGLLVI LERIATTTHW
AQVGPIPLGE EATIRIGEHL FSDYLLPFEL ASILLLIAMI GAIVLARKDL VDLKPIIEQR
IDPKEIKLPS SSMFRKKSKK LTDMG