NU6C_SYNY3
ID NU6C_SYNY3 Reviewed; 198 AA.
AC P26523; Q55523;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 120.
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; OrderedLocusNames=sll0521;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1463844; DOI=10.1007/bf00028896;
RA Ellersiek U., Steinmueller K.;
RT "Cloning and transcription analysis of the ndh(A-I-G-E) gene cluster and
RT the ndhD gene of the cyanobacterium Synechocystis sp. PCC6803.";
RL Plant Mol. Biol. 20:1097-1110(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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.
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; X62517; CAA44376.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA10883.1; -; Genomic_DNA.
DR PIR; S76036; QXYB6.
DR AlphaFoldDB; P26523; -.
DR SMR; P26523; -.
DR IntAct; P26523; 7.
DR STRING; 1148.1001393; -.
DR PaxDb; P26523; -.
DR EnsemblBacteria; BAA10883; BAA10883; BAA10883.
DR KEGG; syn:sll0521; -.
DR eggNOG; COG0839; Bacteria.
DR InParanoid; P26523; -.
DR OMA; MLVNKRE; -.
DR PhylomeDB; P26523; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
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; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..198
FT /note="NAD(P)H-quinone oxidoreductase chain 6"
FT /id="PRO_0000118367"
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 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 168..198
FT /note="RDLIPELSEENKTATALTLPERPRELTSASK -> PGLNSRIVRGKQNRHGP
FT DFARASPGVNLRFQIDAA (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 21523 MW; A92685FB148C5FEE CRC64;
MNLAEGVQYI SFLILAFLVI GAALGVVLLS NIVYSAFLLG GVFLSISGIY ILLNADFVAA
AQVLVYVGAV SVLILFAIML VNKREDFSKI PGRWLRNVST ALVCTGIFAL LSTMVLITPW
QINETGPFVE NTLVTIGKHF FSDYLLPFEL ASVLLLMAMV GAIILARRDL IPELSEENKT
ATALTLPERP RELTSASK
