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NDHJ_PAUCH
ID   NDHJ_PAUCH              Reviewed;         192 AA.
AC   B1X4R3;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit J, organellar chromatophore {ECO:0000255|HAMAP-Rule:MF_01357};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01357};
DE   AltName: Full=NAD(P)H dehydrogenase subunit J;
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit J {ECO:0000255|HAMAP-Rule:MF_01357};
GN   Name=ndhJ {ECO:0000255|HAMAP-Rule:MF_01357}; OrderedLocusNames=PCC_0496;
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-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC       reaction to proton translocation (for every two electrons transferred,
CC       four hydrogen ions are translocated across the cytoplasmic membrane),
CC       and thus conserves the redox energy in a proton gradient (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC         Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01357};
CC   -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC       are encoded in the nucleus. {ECO:0000255|HAMAP-Rule:MF_01357}.
CC   -!- SUBCELLULAR LOCATION: Plastid, organellar chromatophore thylakoid
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01357}; Stromal side {ECO:0000255|HAMAP-Rule:MF_01357}.
CC   -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01357}.
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DR   EMBL; CP000815; ACB42932.1; -; Genomic_DNA.
DR   RefSeq; YP_002049142.1; NC_011087.1.
DR   AlphaFoldDB; B1X4R3; -.
DR   SMR; B1X4R3; -.
DR   PRIDE; B1X4R3; -.
DR   GeneID; 6481480; -.
DR   GO; GO:0070118; C:organellar chromatophore thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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; 3.30.460.80; -; 1.
DR   HAMAP; MF_01357; NDH1_NuoC; 1.
DR   InterPro; IPR010218; NADH_DH_suC.
DR   InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR   InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR   InterPro; IPR020396; NADH_UbQ_OxRdtase_CS.
DR   Pfam; PF00329; Complex1_30kDa; 1.
DR   SUPFAM; SSF143243; SSF143243; 1.
DR   PROSITE; PS00542; COMPLEX1_30K; 1.
PE   3: Inferred from homology;
KW   Membrane; NAD; NADP; Organellar chromatophore; Plastid; Plastoquinone;
KW   Quinone; Thylakoid; Translocase; Transport.
FT   CHAIN           1..192
FT                   /note="NAD(P)H-quinone oxidoreductase subunit J, organellar
FT                   chromatophore"
FT                   /id="PRO_0000358310"
SQ   SEQUENCE   192 AA;  21988 MW;  59F452A0E59F1631 CRC64;
     MIEPSIIPVL VENTEEKTFK FQPGQVSQWL TGQGLQHQIL EPDLLGVELI GVEPSELQKI
     AEALKSNGFD YLQCQGGYDE GPGGRLVSFY HLIKLGTIAD HYLTPNTLPP NSILKEVRLK
     VFLLRDGNLS VPSLYSIFRG SDWQERETFD MFGISYEGHP HPKRLLMPED WKGYPLRKDY
     IQPDFYEMQV AY
 
 
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