NDHK_PEA
ID NDHK_PEA Reviewed; 227 AA.
AC O98679;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 90.
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, ECO:0000312|EMBL:CAA06191.1};
OS Pisum sativum (Garden pea).
OG Plastid; Chloroplast {ECO:0000312|EMBL:CAA06191.1}.
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; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA06191.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION IN THE NDH COMPLEX,
RP CATALYTIC ACTIVITY OF THE NDH COMPLEX, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Lincoln {ECO:0000269|PubMed:10202810};
RC TISSUE=Leaf {ECO:0000312|EMBL:CAA06191.1};
RX PubMed=10202810; DOI=10.1093/oxfordjournals.pcp.a029522;
RA Elortza F., Asturias J.A., Arizmendi J.M.;
RT "Chloroplast NADH dehydrogenase from Pisum sativum: characterization of its
RT activity and cloning of ndhK gene.";
RL Plant Cell Physiol. 40:149-154(1999).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-11, IDENTIFICATION IN THE NDH COMPLEX, FUNCTION,
RP CATALYTIC ACTIVITY OF THE NDH COMPLEX, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Little Marvel {ECO:0000269|PubMed:9448329};
RC TISSUE=Leaf {ECO:0000269|PubMed:9448329};
RX PubMed=9448329; DOI=10.1073/pnas.95.3.1319;
RA Sazanov L.A., Burrows P.A., Nixon P.J.;
RT "The plastid ndh genes code for an NADH-specific dehydrogenase: isolation
RT of a complex I analogue from pea thylakoid membranes.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:1319-1324(1998).
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. It has NADH- and
CC deamino-NADH-specific dehydrogenase activity, using ferricyanide or
CC quinones as acceptors. The immediate electron acceptor for the enzyme
CC in this species is believed to be plastoquinone. Couples the redox
CC reaction to proton translocation, and thus conserves the redox energy
CC in a proton gradient. {ECO:0000269|PubMed:9448329}.
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 ECO:0000269|PubMed:10202810, ECO:0000269|PubMed:9448329};
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 ECO:0000269|PubMed:10202810, ECO:0000269|PubMed:9448329};
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 ECO:0000269|PubMed:10202810, ECO:0000269|PubMed:9448329}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000305|PubMed:10202810, ECO:0000305|PubMed:9448329}; Peripheral
CC membrane protein {ECO:0000305|PubMed:10202810,
CC ECO:0000305|PubMed:9448329}; Stromal side {ECO:0000305|PubMed:10202810,
CC ECO:0000305|PubMed:9448329}.
CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01356}.
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DR EMBL; AJ004882; CAA06191.1; -; Genomic_DNA.
DR AlphaFoldDB; O98679; -.
DR SMR; O98679; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
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; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 4Fe-4S; Chloroplast; Direct protein sequencing; Iron; Iron-sulfur;
KW Membrane; Metal-binding; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW Thylakoid; Translocase; Transport.
FT CHAIN 1..227
FT /note="NAD(P)H-quinone oxidoreductase subunit K,
FT chloroplastic"
FT /id="PRO_0000118753"
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; 25495 MW; D5CDEB2BF3032FE0 CRC64;
MNSIEFPLLD QKTKNSVIST TLNDLSNWSR LSSLWPLLYG TSCCFIEFAS LIGSRFDFDR
YGLVPRSSPR QADLILTAGT VTMKMAPSLV RLYEQMPEPK YVIAMGACTI TGGMFSTDSY
STVRGVDKLI PVDVYLPGCP PKPEAVIDAI TKLRKKISRE IDEDPISYQR ENRSFTTNHK
FDVGRSTHTG NSNQGLFYQP SSISEMTSDT FLKYKKVQYP ATNEKVN
