ID   NDHK_CERDE              Reviewed;         228 AA.
AC   A8SEA7;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 48.
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   Ceratophyllum demersum (Rigid hornwort) (Coontail).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ceratophyllales; Ceratophyllaceae;
OC   Ceratophyllum.
OX   NCBI_TaxID=4428;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18048334; DOI=10.1073/pnas.0708072104;
RA   Moore M.J., Bell C.D., Soltis P.S., Soltis D.E.;
RT   "Using plastid genome-scale data to resolve enigmatic relationships among
RT   basal angiosperms.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:19363-19368(2007).
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   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01356}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABQ81454.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; EF614270; ABQ81454.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_001542451.1; NC_009962.1.
DR   AlphaFoldDB; A8SEA7; -.
DR   SMR; A8SEA7; -.
DR   GeneID; 5729382; -.
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   3: Inferred from homology;
KW   4Fe-4S; Chloroplast; Iron; Iron-sulfur; Membrane; Metal-binding; NAD; NADP;
KW   Plastid; Plastoquinone; Quinone; Thylakoid; Translocase; Transport.
FT   CHAIN           1..228
FT                   /note="NAD(P)H-quinone oxidoreductase subunit K,
FT                   chloroplastic"
FT                   /id="PRO_0000358528"
FT   BINDING         43
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT   BINDING         44
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT   BINDING         108
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT   BINDING         139
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
SQ   SEQUENCE   228 AA;  25824 MW;  8D61FFF01C08D4BA CRC64;
     MNSIEFPLFD RTTKNSVIST TSNDLSNWSR LSSLWPLLYG TSCCFIEFAS LIGSRFDFDR
     YGLVPRSSPR QADLILTAGT ITMKMAPSLV RLYEQMPKPK YVIAMGACTI TGGMFSTDSY
     STVRGVDKLI PVDVYLPGCP PKPEAVIDAI TKLRKKVSRE IYEDRISSQQ ENRCFTINHK
     FRIRRSTHTG NYDQGLLDQS PSTSTSRIRP SENFFKYKST VFSHELVN