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NU5C_ATRBE
ID   NU5C_ATRBE              Reviewed;         740 AA.
AC   Q8S8V0; Q31773;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic;
DE            EC=7.1.1.-;
DE   AltName: Full=NAD(P)H dehydrogenase subunit 5;
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit 5;
GN   Name=ndhF;
OS   Atropa belladonna (Belladonna) (Deadly nightshade).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Hyoscyameae; Atropa.
OX   NCBI_TaxID=33113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Ab5p(kan);
RX   PubMed=12200487; DOI=10.1093/oxfordjournals.molbev.a004222;
RA   Schmitz-Linneweber C., Regel R., Du T.G., Hupfer H., Herrmann R.G.,
RA   Maier R.M.;
RT   "The plastid chromosome of Atropa belladonna and its comparison with that
RT   of Nicotiana tabacum: the role of RNA editing in generating divergence in
RT   the process of plant speciation.";
RL   Mol. Biol. Evol. 19:1602-1612(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-703.
RA   Olmstead R.G., Sweere J.A.;
RT   "Combining data in phylogenetic systematics: an empirical approach using
RT   three molecular data sets in the Solanaceae.";
RL   Syst. Biol. 43:467-481(1994).
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, chloroplast thylakoid membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR   EMBL; AJ316582; CAC88093.1; -; Genomic_DNA.
DR   EMBL; U08915; AAA18597.2; -; Genomic_DNA.
DR   RefSeq; NP_783279.1; NC_004561.1.
DR   AlphaFoldDB; Q8S8V0; -.
DR   SMR; Q8S8V0; -.
DR   GeneID; 806500; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   InterPro; IPR002128; NADH_UbQ_OxRdtase_chlpt_su5_C.
DR   InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   InterPro; IPR003945; NU5C-like.
DR   InterPro; IPR001516; Proton_antipo_N.
DR   PANTHER; PTHR42829; PTHR42829; 1.
DR   Pfam; PF01010; Proton_antipo_C; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   Pfam; PF00662; Proton_antipo_N; 1.
DR   TIGRFAMs; TIGR01974; NDH_I_L; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   Thylakoid; Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..740
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT                   chloroplastic"
FT                   /id="PRO_0000118172"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        543..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        602..622
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        718..738
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        62
FT                   /note="Q -> Z (in Ref. 2; AAA18597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        568
FT                   /note="V -> W (in Ref. 2; AAA18597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        670
FT                   /note="F -> L (in Ref. 2; AAA18597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        674
FT                   /note="I -> L (in Ref. 2; AAA18597)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   740 AA;  83956 MW;  A72CAE65EA7B70C2 CRC64;
     MEQTYEYAWI IPFIPLPVPM LIGAGLILFP TATKSFRRMW AFQSVLLLSI VMIFSIYLSI
     QQINSSSFYQ YVWSWIINND FSLDFGYLID PLTSIMSILI TTVGIMVLIY SDNYMAHDQG
     YLRFFAYMSF FSTSMLGLVT SSNLIQIYIF WELVGLCSYL LIGFWFTRPV AANACQKAFV
     TNRVGDFGLL LGILGFYWIT GSFEFRDLFE IFNNLSSNNE VNFLFVTLCA VLLFAGAVAK
     SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLVARL LPLFRVIPYI MYLISVIGII
     TVLLGATLAL AQKDIKRGLA YSTMSQLGYM MLALGMGSYR SALFHLITHA YSKALLFLGS
     GSIIHSMETI VGYSPAKSQN MGLMGGLRKH VPITQITFLL GTLSLCGIPP LACFWSKDEI
     LNDSWLYSPI FAIIAWATAG LTAFYMFRIY LLTFEGHLNV HFQNYGGKQK TPFYSISLWG
     KKGVKKNSYL LTMNNNESTY FFSKTKYPID KNGRKMTRPF MTIAHFEHKT VYSYPYESDN
     TMLFPIFVLG LFTLFVGSIG IPFNQEGVNL DILSKWLAPS INLLHQKSNN SMDWNEFLKD
     AVLSVSIAYF GIFLASFLYK PIYSSLKNFE LINSFVKKGP KRILWDKIIN GIYDWSYNRA
     YIDAFYTRFF VGGIRGLAEF IHFFDRRVID GMTNGVGVIS FIVGEGIKYI GGGRISSYLF
     LYLAYVSVFL LVYYLFFLTF
 
 
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