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NDHK_SOYBN
ID   NDHK_SOYBN              Reviewed;         212 AA.
AC   P31175; Q2PMU7;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 2.
DT   03-AUG-2022, entry version 118.
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   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 4-212.
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_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; DQ317523; ABC25111.1; -; Genomic_DNA.
DR   EMBL; X64329; CAA45612.1; -; mRNA.
DR   PIR; S27978; S27978.
DR   RefSeq; YP_538751.1; NC_007942.1.
DR   AlphaFoldDB; P31175; -.
DR   SMR; P31175; -.
DR   STRING; 3847.GLYMA08G05521.1; -.
DR   PRIDE; P31175; -.
DR   GeneID; 3989277; -.
DR   KEGG; gmx:3989277; -.
DR   eggNOG; KOG1687; Eukaryota.
DR   InParanoid; P31175; -.
DR   OrthoDB; 1278656at2759; -.
DR   Proteomes; UP000008827; Chloroplast.
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; Thylakoid;
KW   Translocase; Transport.
FT   CHAIN           1..212
FT                   /note="NAD(P)H-quinone oxidoreductase subunit K,
FT                   chloroplastic"
FT                   /id="PRO_0000118754"
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"
FT   CONFLICT        23
FT                   /note="N -> I (in Ref. 2; CAA45612)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        32
FT                   /note="S -> P (in Ref. 2; CAA45612)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        78
FT                   /note="A -> V (in Ref. 2; CAA45612)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="P -> T (in Ref. 2; CAA45612)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        156
FT                   /note="K -> E (in Ref. 2; CAA45612)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="F -> FKVQLEIAIPFFLITS (in Ref. 2; CAA45612)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   212 AA;  23886 MW;  36B9B84BE8483C05 CRC64;
     MNSIEFPLLD QTTKNSVIST TLNDLSNWSR LSSLWPLLYG TSCCFIEFAS LIGSRFDFDR
     YGLVPRSSPR QADLILTAGT VTMKMAPSLV RLYEQMPEPK YVIAMGACTI TGGMFSTDSY
     STVRGVDKLI PVDVYLPGCP PKPEAIIDAI TKLRKKISRE IYENQMSSQR ENRCFTTNHK
     FHIGYSTHTG NYGQELFYQL PSTSEIPSDT FF
 
 
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