NDHJ_CRYJA
ID NDHJ_CRYJA Reviewed; 158 AA.
AC B1VKF6;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 46.
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 Cryptomeria japonica (Japanese cedar) (Cupressus japonica).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC Cryptomeria.
OX NCBI_TaxID=3369;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18570682; DOI=10.1186/1471-2229-8-70;
RA Hirao T., Watanabe A., Kurita M., Kondo T., Takata K.;
RT "Complete nucleotide sequence of the Cryptomeria japonica D. Don.
RT chloroplast genome and comparative chloroplast genomics: diversified
RT genomic structure of coniferous species.";
RL BMC Plant Biol. 8:70-70(2008).
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; AP009377; BAG16667.1; -; Genomic_DNA.
DR RefSeq; YP_001806669.1; NC_010548.1.
DR AlphaFoldDB; B1VKF6; -.
DR SMR; B1VKF6; -.
DR GeneID; 6166569; -.
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..158
FT /note="NAD(P)H-quinone oxidoreductase subunit J,
FT chloroplastic"
FT /id="PRO_0000358258"
SQ SEQUENCE 158 AA; 18312 MW; CAF6F0B0690DCFB4 CRC64;
MQGRLSAWLA KHKLAHRPLG FDYQGTETLQ IKAEDWVSIA VALYVYGFNY LRSQCAYDVA
PGGSLASVYH LTKINDNADQ PEEVCIKVFV PREDPRIPSV LRIWKGANFQ ERESYDMLGI
FYESHPCLKR ILMPESWIGW PLRKDYIAPD FYEIQDSH