NDHJ_CHLAT
ID NDHJ_CHLAT Reviewed; 195 AA.
AC Q19V88;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit J, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01357};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01357};
DE AltName: Full=NAD(P)H dehydrogenase subunit J;
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit J {ECO:0000255|HAMAP-Rule:MF_01357};
GN Name=ndhJ {ECO:0000255|HAMAP-Rule:MF_01357};
OS Chlorokybus atmophyticus (Soil alga).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Chlorokybophyceae; Chlorokybales;
OC Chlorokybaceae; Chlorokybus.
OX NCBI_TaxID=3144;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 48.80;
RX PubMed=17222354; DOI=10.1186/1741-7007-5-2;
RA Lemieux C., Otis C., Turmel M.;
RT "A clade uniting the green algae Mesostigma viride and Chlorokybus
RT atmophyticus represents the deepest branch of the Streptophyta in
RT chloroplast genome-based phylogenies.";
RL BMC Biol. 5:2-2(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_01357}.
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_01357};
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_01357};
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_01357}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01357}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01357}; Stromal side {ECO:0000255|HAMAP-
CC Rule:MF_01357}.
CC -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01357}.
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DR EMBL; DQ422812; ABD62198.2; -; Genomic_DNA.
DR RefSeq; YP_001019117.2; NC_008822.1.
DR AlphaFoldDB; Q19V88; -.
DR SMR; Q19V88; -.
DR GeneID; 4783262; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 3.30.460.80; -; 1.
DR HAMAP; MF_01357; NDH1_NuoC; 1.
DR InterPro; IPR010218; NADH_DH_suC.
DR InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR InterPro; IPR020396; NADH_UbQ_OxRdtase_CS.
DR Pfam; PF00329; Complex1_30kDa; 1.
DR SUPFAM; SSF143243; SSF143243; 1.
DR PROSITE; PS00542; COMPLEX1_30K; 1.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW Thylakoid; Translocase; Transport.
FT CHAIN 1..195
FT /note="NAD(P)H-quinone oxidoreductase subunit J,
FT chloroplastic"
FT /id="PRO_0000358253"
SQ SEQUENCE 195 AA; 22487 MW; AE35C3EC84F936B5 CRC64;
MKNNEKVSDS FLTSSGKELS EATPSASSYT TVVRDKNIKG VVSNWLAEMK LRHKPLGFDY
QGVEILEVKP EDLTSVAIAL YAYGFNYLRN QCAYDVSPGG NLASVYHLTK LDADVDQPQE
VCLKVFLPRE NPRVPSVFWI WKTADFQERE SYDMFGIYYE GHPHLKRILM PENWVGWPLR
KDYITPDFFE LQDAY