ID NDHH_LEPVR Reviewed; 393 AA. AC A4QLG5; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 1. DT 02-SEP-2026, entry version 63. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit H, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01358}; DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01358}; DE AltName: Full=NAD(P)H dehydrogenase subunit H; DE AltName: Full=NADH-plastoquinone oxidoreductase 49 kDa subunit {ECO:0000255|HAMAP-Rule:MF_01358}; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit H {ECO:0000255|HAMAP-Rule:MF_01358}; GN Name=ndhH {ECO:0000255|HAMAP-Rule:MF_01358}; OS Lepidium virginicum (Virginia pepperweed). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Lepidieae; Lepidium. OX NCBI_TaxID=59292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Hosouchi T., Tsuruoka H., Kotani H.; RT "Sequencing analysis of Lepidium virginicum JO26 chloroplast DNA."; RL Submitted (MAR-2007) 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:0000255|HAMAP-Rule:MF_01358}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a plastoquinone + NADH + (n+1) H(+)(in) = a plastoquinol + CC NAD(+) + n H(+)(out); 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_01358}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a plastoquinone + NADPH + (n+1) H(+)(in) = a plastoquinol + CC NADP(+) + n H(+)(out); 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_01358}; 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_01358}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000255|HAMAP-Rule:MF_01358}; Peripheral membrane protein CC {ECO:0000255|HAMAP-Rule:MF_01358}; Stromal side {ECO:0000255|HAMAP- CC Rule:MF_01358}. CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family. CC {ECO:0000255|HAMAP-Rule:MF_01358}. 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; AP009374; BAF50520.1; -; Genomic_DNA. DR RefSeq; YP_001123695.1; NC_009273.1. DR AlphaFoldDB; A4QLG5; -. DR SMR; A4QLG5; -. DR GeneID; 4962058; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule. DR GO; GO:0048038; F:quinone binding; IEA:InterPro. DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule. DR FunFam; 1.10.645.10:FF:000003; NAD(P)H-quinone oxidoreductase subunit H, chloroplastic; 1. DR Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1. DR HAMAP; MF_01358; NDH1_NuoD; 1. DR InterPro; IPR001135; NADH_Q_OxRdtase_suD. DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS. DR InterPro; IPR022885; NDH1_su_D/H. DR InterPro; IPR029014; NiFe-Hase_large. DR NCBIfam; NF004739; PRK06075.1; 1. DR NCBIfam; NF005649; PRK07415.1; 1. DR PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1. DR PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1. DR Pfam; PF00346; Complex1_49kDa; 1. DR SUPFAM; SSF56762; HydB/Nqo4-like; 1. DR PROSITE; PS00535; COMPLEX1_49K; 1. PE 3: Inferred from homology; KW Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone; KW Thylakoid; Translocase; Transport. FT CHAIN 1..393 FT /note="NAD(P)H-quinone oxidoreductase subunit H, FT chloroplastic" FT /id="PRO_0000358000" SQ SEQUENCE 393 AA; 45505 MW; 89E8287261A853BA CRC64; MKRPVTGKDL MIVNMGPHHP SMHGVLRLIV TLDGEDVVDC EPILGYLHRG MEKIAENRAI IQYLPYVTRW DYLATMFTEA ITVNGPEQLG NIQVPKRASY IRVIMLELSR IASHLLWLGP FMADIGAQTP FFYIFREREF VYDLFEAATG MRMMHNFFRI GGIAADLPYG WIDKCLDFCD YFLTEVVEYQ KLITRNPIFL ERVEGVGIIG GEEAINWGLS GPMLRASGIP WDLRKVDRYE SYDEFEWEIQ WQKQGDSLAR YLVRLSEMTE SIKIIQQALE GLPGGPYENL ESRSFDRKRN PEWNDFDYRF ISKKPSPTFE LSKQELYVRV EAPKGELGIF LIGDQSGFPW RWKIRPPGFI NLQILPELVK RMKLADIMTI LGSIDIIMGE VDR //