NDHJ_SOYBN
ID NDHJ_SOYBN Reviewed; 158 AA.
AC P31174; Q2PMU6;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 111.
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 Glycine max (Soybean) (Glycine hispida).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PI 437654;
RX PubMed=16247559; DOI=10.1007/s11103-005-8882-0;
RA Saski C., Lee S.-B., Daniell H., Wood T.C., Tomkins J., Kim H.-G.,
RA Jansen R.K.;
RT "Complete chloroplast genome sequence of Glycine max and comparative
RT analyses with other legume genomes.";
RL Plant Mol. Biol. 59:309-322(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-97.
RC STRAIN=cv. Saxa;
RX PubMed=1463827; DOI=10.1007/bf00027160;
RA Whelan J., Young S., Day D.A.;
RT "Cloning of ndhK from soybean chloroplasts using antibodies raised to
RT mitochondrial complex I.";
RL Plant Mol. Biol. 20:887-895(1992).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ317523; ABC25112.1; -; Genomic_DNA.
DR EMBL; X64329; CAA45613.1; -; mRNA.
DR PIR; S28884; S28884.
DR RefSeq; YP_538752.1; NC_007942.1.
DR AlphaFoldDB; P31174; -.
DR SMR; P31174; -.
DR STRING; 3847.GLYMA16G11475.1; -.
DR PRIDE; P31174; -.
DR GeneID; 3989278; -.
DR KEGG; gmx:3989278; -.
DR eggNOG; KOG1713; Eukaryota.
DR InParanoid; P31174; -.
DR OrthoDB; 1276923at2759; -.
DR Proteomes; UP000008827; Chloroplast.
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 Pfam; PF00329; Complex1_30kDa; 1.
DR SUPFAM; SSF143243; SSF143243; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW Reference proteome; Thylakoid; Translocase; Transport.
FT CHAIN 1..158
FT /note="NAD(P)H-quinone oxidoreductase subunit J,
FT chloroplastic"
FT /id="PRO_0000118661"
FT CONFLICT 15
FT /note="I -> S (in Ref. 2; CAA45613)"
FT /evidence="ECO:0000305"
FT CONFLICT 77..79
FT /note="GID -> DIG (in Ref. 2; CAA45613)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="I -> M (in Ref. 2; CAA45613)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="K -> G (in Ref. 2; CAA45613)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="I -> S (in Ref. 2; CAA45613)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 18623 MW; CA3724711105177C CRC64;
MQGRLSSWLV KHGLIHRSLG FDYQGIETLQ IKPEDWHSIA VILYVYGYNY LRSQCAYDVA
PGGLLASVYH LTRLEYGIDQ PEEVCIKIFV ARKNPRIPSI FWVWKSADFQ EKESYDMLGI
SYDNHPRLRR ILMPESWIGW PLRKDYIAPN FYEIQDAH
