位置:首页 > 蛋白库 > NU6C_NOSS1
NU6C_NOSS1
ID   NU6C_NOSS1              Reviewed;         202 AA.
AC   Q8Z075; Q9WWM5;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 85.
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;
DE   AltName: Full=NDH-G;
GN   Name=ndhG; OrderedLocusNames=alr0225;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Schiefer W., Happe T.;
RT   "Isolation of the ndhAIGE gene cluster of Anabaena sp. PCC 7120.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ242867; CAB44670.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB77749.1; -; Genomic_DNA.
DR   PIR; AI1834; AI1834.
DR   RefSeq; WP_010994402.1; NZ_RSCN01000026.1.
DR   AlphaFoldDB; Q8Z075; -.
DR   SMR; Q8Z075; -.
DR   STRING; 103690.17135203; -.
DR   EnsemblBacteria; BAB77749; BAB77749; BAB77749.
DR   KEGG; ana:alr0225; -.
DR   eggNOG; COG0839; Bacteria.
DR   OMA; MLVNKRE; -.
DR   OrthoDB; 1683794at2; -.
DR   Proteomes; UP000002483; Chromosome.
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; Reference proteome;
KW   Translocase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..202
FT                   /note="NAD(P)H-quinone oxidoreductase chain 6"
FT                   /id="PRO_0000118365"
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        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        11
FT                   /note="S -> P (in Ref. 1; CAB44670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        22
FT                   /note="T -> P (in Ref. 1; CAB44670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177..181
FT                   /note="SGLPQ -> IWLTS (in Ref. 1; CAB44670)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   202 AA;  21406 MW;  A677898543F0F7CC CRC64;
     MNLAEGVQVV SFGILATMLI GTALGVVLAT SIVYSAFLLG GVFISIAGMY LLLNGDFVAA
     AQVLVYVGAV NVLILFAIML VNKRQDFTPY PSAGIRKVLT AIVSVGLFAL LSTMVLATPW
     AYSTTPKVGD GSIIVIGEHF FSDFLLPFEL ASVLLLMAMV GAIILARREY LPEVTPSGLP
     QTVLTLPERP RELVGAGSET QE
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024