NDHK_ARATH
ID NDHK_ARATH Reviewed; 225 AA.
AC P56756;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
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}; Synonyms=psbG;
GN OrderedLocusNames=AtCg00430;
OS Arabidopsis thaliana (Mouse-ear cress).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10574454; DOI=10.1093/dnares/6.5.283;
RA Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.;
RT "Complete structure of the chloroplast genome of Arabidopsis thaliana.";
RL DNA Res. 6:283-290(1999).
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; AP000423; BAA84389.1; -; Genomic_DNA.
DR RefSeq; NP_051063.1; NC_000932.1.
DR PDB; 7WFG; EM; 4.33 A; K=1-225.
DR PDB; 7WG5; EM; 3.89 A; K=1-225.
DR PDBsum; 7WFG; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; P56756; -.
DR SMR; P56756; -.
DR BioGRID; 29963; 3.
DR STRING; 3702.ATCG00430.1; -.
DR TCDB; 3.D.1.8.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR iPTMnet; P56756; -.
DR PaxDb; P56756; -.
DR PRIDE; P56756; -.
DR ProteomicsDB; 251320; -.
DR EnsemblPlants; ATCG00430.1; ATCG00430.1; ATCG00430.
DR GeneID; 844761; -.
DR Gramene; ATCG00430.1; ATCG00430.1; ATCG00430.
DR KEGG; ath:ArthCp026; -.
DR Araport; ATCG00430; -.
DR TAIR; locus:504954666; ATCG00430.
DR eggNOG; KOG1687; Eukaryota.
DR HOGENOM; CLU_055737_2_1_1; -.
DR InParanoid; P56756; -.
DR OMA; TMKMAPQ; -.
DR OrthoDB; 1278656at2759; -.
DR BioCyc; ARA:ATCG00430-MON; -.
DR PRO; PR:P56756; -.
DR Proteomes; UP000006548; Chloroplast.
DR ExpressionAtlas; P56756; baseline and differential.
DR Genevisible; P56756; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Chloroplast; Iron; Iron-sulfur; Membrane;
KW Metal-binding; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW Reference proteome; Thylakoid; Translocase; Transport.
FT CHAIN 1..225
FT /note="NAD(P)H-quinone oxidoreductase subunit K,
FT chloroplastic"
FT /id="PRO_0000118743"
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 225 AA; 25366 MW; 1210C11820FD533D CRC64;
MNSIKFPILD RTTKNSVIST TLNDLSNWSR LSSLWPLLYG TSCCFIEFAS LIGSRFDFDR
YGLVPRSSPR QADLILTAGT VTMKMAPSLV RLYEQMPEPK YVIAMGACTI TGGMFSTDSY
STVRGVDKLI PVDVYLPGCP PKPEAVIDAI TKLRKKIARE IYKDRIRPQQ GNRCFTTNHK
FFVVRSPHIG NYDQELLYPP SSTSEISTET FFKYKSPVSS HELVN
