位置:首页 > 蛋白库 > NDHK_ANTAG
NDHK_ANTAG
ID   NDHK_ANTAG              Reviewed;         247 AA.
AC   Q31791; Q85UU2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   25-MAR-2003, sequence version 3.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit K, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01356};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01356};
DE   AltName: Full=NAD(P)H dehydrogenase subunit K {ECO:0000255|HAMAP-Rule:MF_01356};
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit K {ECO:0000255|HAMAP-Rule:MF_01356};
GN   Name=ndhK {ECO:0000255|HAMAP-Rule:MF_01356};
OS   Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC   Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC   Anthoceros.
OX   NCBI_TaxID=48387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX   PubMed=12527781; DOI=10.1093/nar/gkg155;
RA   Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT   "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT   chloroplast genome: insight into the earliest land plants.";
RL   Nucleic Acids Res. 31:716-721(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC   TISSUE=Thallus;
RX   PubMed=12711687; DOI=10.1093/nar/gkg327;
RA   Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT   "RNA editing in hornwort chloroplasts makes more than half the genes
RT   functional.";
RL   Nucleic Acids Res. 31:2417-2423(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
RC   TISSUE=Thallus;
RX   PubMed=8604330; DOI=10.1093/nar/24.6.1008;
RA   Yoshinaga K., Iinuma H., Masuzawa T., Ueda K.;
RT   "Extensive RNA editing of U to C in addition to C to U substitution in the
RT   rbcL transcripts of hornwort chloroplasts and the origin of RNA editing in
RT   green plants.";
RL   Nucleic Acids Res. 24:1008-1014(1996).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_01356}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01356};
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01356};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01356};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01356};
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_01356}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01356}; Peripheral membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01356}; Stromal side {ECO:0000255|HAMAP-
CC       Rule:MF_01356}.
CC   -!- RNA EDITING: Modified_positions=3 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 35 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 117 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 128 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 133 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687};
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01356}.
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; AB086179; BAC55353.2; -; Genomic_DNA.
DR   EMBL; AB087445; BAC55447.1; ALT_SEQ; mRNA.
DR   EMBL; D43695; BAA07792.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AB087446; BAC55448.1; -; mRNA.
DR   PIR; S71143; S71143.
DR   RefSeq; NP_777417.3; NC_004543.1.
DR   AlphaFoldDB; Q31791; -.
DR   SMR; Q31791; -.
DR   GeneID; 2553504; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01356; NDH1_NuoB; 1.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   TIGRFAMs; TIGR01957; nuoB_fam; 1.
DR   PROSITE; PS01150; COMPLEX1_20K; 1.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Chloroplast; Iron; Iron-sulfur; Membrane; Metal-binding; NAD; NADP;
KW   Plastid; Plastoquinone; Quinone; RNA editing; Thylakoid; Translocase;
KW   Transport.
FT   CHAIN           1..247
FT                   /note="NAD(P)H-quinone oxidoreductase subunit K,
FT                   chloroplastic"
FT                   /id="PRO_0000118742"
FT   BINDING         61
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT   BINDING         62
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT   BINDING         126
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT   BINDING         157
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
SQ   SEQUENCE   247 AA;  27831 MW;  4406DB94B0B26D73 CRC64;
     MVLVPKYLNF ESDLAESVTN SMDSSLPDET TSDSIILTTF NDFSNWARLS SLWPLLYGTS
     CCFIEFASLI GSRFDFDRYG LVPRSSPRQA DLIITAGTVT MKMAPSLVRL YEQMPEPKYV
     IAMGACTITG GMFSTDSYST VRGVDKLIPV DIYLPGCPPK PEAIIDAIIK LRKGVAREVH
     ERKDKLRQTR RYFTLNHQLE IVPIIHTGKY DEHLFSKFSE ISIEPKLNVS PQRIEKSKSS
     ISSQISF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024