NDHK_MAIZE
ID NDHK_MAIZE Reviewed; 227 AA.
AC P06670;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 3.
DT 03-AUG-2022, entry version 126.
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;
OS Zea mays (Maize).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3512536; DOI=10.1016/s0021-9258(17)35808-8;
RA Steinmetz A.A., Castroviejo M., Sayre R.T., Bogorad L.;
RT "Protein PSII-G. An additional component of photosystem II identified
RT through its plastid gene in maize.";
RL J. Biol. Chem. 261:2485-2488(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2499764; DOI=10.1007/bf00332231;
RA Steinmueller K., Ley A.C., Steinmetz A.A., Sayre R.T., Bogorad L.;
RT "Characterization of the ndhC-psbG-ORF157/159 operon of maize plastid DNA
RT and of the cyanobacterium Synechocystis sp. PCC6803.";
RL Mol. Gen. Genet. 216:60-69(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=7666415; DOI=10.1006/jmbi.1995.0460;
RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.;
RT "Complete sequence of the maize chloroplast genome: gene content, hotspots
RT of divergence and fine tuning of genetic information by transcript
RT editing.";
RL J. Mol. Biol. 251:614-628(1995).
RN [4]
RP RNA EDITING, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Perceval; TISSUE=Bundle sheath cell, and Mesophyll cell;
RX PubMed=16436305; DOI=10.1016/j.jplph.2005.11.014;
RA Darie C.C., De Pascalis L., Mutschler B., Haehnel W.;
RT "Studies of the Ndh complex and photosystem II from mesophyll and bundle
RT sheath chloroplasts of the C(4)-type plant Zea mays.";
RL J. Plant Physiol. 163:800-808(2006).
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 -!- DEVELOPMENTAL STAGE: The NDH complex is 2.5-3 times more abundant in
CC bundle sheath than mesophyll cells. {ECO:0000269|PubMed:16436305}.
CC -!- RNA EDITING: Modified_positions=22 {ECO:0000269|PubMed:16436305};
CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01356}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA84484.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA35482.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA60290.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M12704; AAA84484.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X17438; CAA35482.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X86563; CAA60290.1; ALT_SEQ; Genomic_DNA.
DR PIR; A25710; F2ZMG.
DR RefSeq; NP_043029.2; NC_001666.2.
DR AlphaFoldDB; P06670; -.
DR SMR; P06670; -.
DR STRING; 4577.GRMZM5G800980_P01; -.
DR PaxDb; P06670; -.
DR PRIDE; P06670; -.
DR GeneID; 845190; -.
DR KEGG; zma:845190; -.
DR MaizeGDB; 69598; -.
DR eggNOG; KOG1687; Eukaryota.
DR OrthoDB; 1278656at2759; -.
DR Proteomes; UP000007305; Chloroplast.
DR ExpressionAtlas; P06670; baseline.
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; 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 2: Evidence at transcript level;
KW 4Fe-4S; Chloroplast; Iron; Iron-sulfur; Membrane; Metal-binding; NAD; NADP;
KW Plastid; Plastoquinone; Quinone; Reference proteome; RNA editing;
KW Thylakoid; Translocase; Transport.
FT CHAIN 1..227
FT /note="NAD(P)H-quinone oxidoreductase subunit K,
FT chloroplastic"
FT /id="PRO_0000118746"
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 227 AA; 25497 MW; 523BDF64FB42B52F CRC64;
MSLIEFPLLD QTSSNSVIST TLNDLSNWSR LSSLWPLLYG TSCCFIEFAS LIGSRFDFDR
YGLVPRSSPR QADLILTAGT VTMKMAPSLV RLYEQMPEPK YVIAMGACTI TGGMFSTDSY
STVRGVDKLI PVDVYLPGCP PKPEAVIDAL TKLRKKIARE IIEDRTLCQS QKKNRSFTTR
HKLYVRRSTH TGTYEQELLY QSPSTLDISS ETFFKSKSSV SSYKLVN
