ID A0A7T0M4A8_9ERIC Unreviewed; 282 AA. AC A0A7T0M4A8; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 25-MAY-2022, entry version 4. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit K, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01356}; DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01356}; DE AltName: Full=NAD(P)H dehydrogenase subunit K {ECO:0000256|HAMAP-Rule:MF_01356}; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit K {ECO:0000256|HAMAP-Rule:MF_01356}; GN Name=ndhK {ECO:0000256|HAMAP-Rule:MF_01356, GN ECO:0000313|EMBL:QPL15758.1}; OS Camellia pubipetala. OG Plastid; Chloroplast {ECO:0000313|EMBL:QPL15758.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; Ericales; Theaceae; Camellia. OX NCBI_TaxID=147930 {ECO:0000313|EMBL:QPL15758.1}; RN [1] {ECO:0000313|EMBL:QPL15758.1} RP NUCLEOTIDE SEQUENCE. RA Fan Y., Zhao B.; RL Submitted (OCT-2020) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01356}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01356}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01356}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_01356}; Peripheral membrane protein CC {ECO:0000256|HAMAP-Rule:MF_01356}; Stromal side {ECO:0000256|HAMAP- CC Rule:MF_01356}. CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family. CC {ECO:0000256|ARBA:ARBA00009173, ECO:0000256|HAMAP-Rule:MF_01356, CC ECO:0000256|RuleBase:RU004464}. 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; MW186719; QPL15758.1; -; Genomic_DNA. 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; 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 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464}; KW Chloroplast {ECO:0000313|EMBL:QPL15758.1}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01356, KW ECO:0000256|RuleBase:RU004464}; Membrane {ECO:0000256|HAMAP-Rule:MF_01356}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01356, KW ECO:0000256|RuleBase:RU004464}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01356}; KW Plastid {ECO:0000313|EMBL:QPL15758.1}; KW Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01356}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01356}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01356}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01356}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01356}. FT DOMAIN 103..210 FT /note="Oxidored_q6" FT /evidence="ECO:0000259|Pfam:PF01058" FT METAL 100 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" FT METAL 101 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" FT METAL 165 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" FT METAL 196 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" SQ SEQUENCE 282 AA; 32265 MW; FF163D24A70CDC41 CRC64; MGNEFRCIGC ICIYRSFNFR AYLNCWFSLC MAKRGIGMVL APEYSDNKKK KKKIETVMNS IEFTLLDRTT QNSVISTTFN DLSNWSRLSS LWPLLYGTSC CFIEFASLIG SRFDFDRYGL VPRSSPRQAD LILTAGTVTM KMAPSLVRLY EQMPEPKYVI AMGACTITGG MFSTDSYSTV RGVDKLIPVD VYLPGCPPKP EAVIDAITKL RKKISREIYE DRIRSQQENR YFTTNHKFHV GRSIHTGNYE QGLLYQPPST SEIPREIFFK YKSSVFSHEL VN //