NDHK_PSINU
ID NDHK_PSINU Reviewed; 207 AA.
AC Q8WI14;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 74.
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 Psilotum nudum (Whisk fern) (Lycopodium nudum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Ophioglossidae; Psilotales; Psilotaceae; Psilotum.
OX NCBI_TaxID=3240;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kingyoku;
RX PubMed=15240838; DOI=10.1093/molbev/msh203;
RA Nishiyama T., Wolf P.G., Kugita M., Sinclair R.B., Sugita M., Sugiura C.,
RA Wakasugi T., Yamada K., Yoshinaga K., Yamaguchi K., Ueda K., Hasebe M.;
RT "Chloroplast phylogeny indicates that bryophytes are monophyletic.";
RL Mol. Biol. Evol. 21:1813-1819(2004).
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}.
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DR EMBL; AP004638; BAB84220.1; -; Genomic_DNA.
DR RefSeq; NP_569633.2; NC_003386.1.
DR AlphaFoldDB; Q8WI14; -.
DR SMR; Q8WI14; -.
DR GeneID; 2545126; -.
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..207
FT /note="NAD(P)H-quinone oxidoreductase subunit K,
FT chloroplastic"
FT /id="PRO_0000358580"
FT BINDING 47
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 143
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
SQ SEQUENCE 207 AA; 23294 MW; 9F74CB203A82844E CRC64;
MNITINPMES LVSKPNTSNS IILTNLNDFS NWARLSSLWP LLYGTSCCFI EFASLIGSRF
DFDRYGLVPR SSPRQADLII TAGTVTMKMA PSLIRLYEQM PEPKYVIAMG ACTITGGMFS
TDSYSTVRGV DKLIPVDIYL PGCPPKPEAI IDAVIKLRKK VAQETYKDQK RSIRGNRFFT
LKHQFDFVPS IHTGQYTQQL HDKSLSK
