ID A0A5P8ZZ52_9FABA Unreviewed; 393 AA. AC A0A5P8ZZ52; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 10-FEB-2021, entry version 5. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit H, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01358}; DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01358}; DE AltName: Full=NAD(P)H dehydrogenase, subunit H {ECO:0000256|HAMAP-Rule:MF_01358}; DE AltName: Full=NADH-plastoquinone oxidoreductase 49 kDa subunit {ECO:0000256|HAMAP-Rule:MF_01358}; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit H {ECO:0000256|HAMAP-Rule:MF_01358}; GN Name=ndhH {ECO:0000256|HAMAP-Rule:MF_01358, GN ECO:0000313|EMBL:QFS94933.1}; OS Arachis stenosperma. OG Plastid; Chloroplast {ECO:0000313|EMBL:QFS94933.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis. OX NCBI_TaxID=217475 {ECO:0000313|EMBL:QFS94933.1}; RN [1] {ECO:0000313|EMBL:QFS94933.1} RP NUCLEOTIDE SEQUENCE. RA Wang J., Li Y., Li C., Yan C., Zhao X., Yuan C., Sun Q., Shi C., Shan S.; RT "Twelve complete chloroplast genomes of wild peanuts: great genetic RT resources and a better understanding of Arachis phylogeny."; RL Submitted (NOV-2018) 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_01358}. 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_01358}; 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_01358}; 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_01358}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_01358}; Peripheral membrane protein CC {ECO:0000256|HAMAP-Rule:MF_01358}; Stromal side {ECO:0000256|HAMAP- CC Rule:MF_01358}. CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family. CC {ECO:0000256|ARBA:ARBA00005769, ECO:0000256|HAMAP-Rule:MF_01358, CC ECO:0000256|RuleBase:RU003685}. 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; MK144819; QFS94933.1; -; Genomic_DNA. 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:UniProtKB-KW. DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.645.20; -; 1. DR HAMAP; MF_01358; NDH1_NuoD; 1. DR InterPro; IPR001135; NADH_Q_OxRdtase_suD. DR InterPro; IPR038290; NADH_Q_OxRdtase_suD_sf. DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS. DR InterPro; IPR022885; NDH1_su_D/H. DR InterPro; IPR029014; NiFe-Hase_large. DR Pfam; PF00346; Complex1_49kDa; 1. DR SUPFAM; SSF56762; SSF56762; 1. DR PROSITE; PS00535; COMPLEX1_49K; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:QFS94933.1}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01358}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01358, KW ECO:0000256|RuleBase:RU003685}; NADP {ECO:0000256|HAMAP-Rule:MF_01358}; KW Plastid {ECO:0000313|EMBL:QFS94933.1}; KW Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01358}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01358}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01358}; KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP- KW Rule:MF_01358, ECO:0000256|RuleBase:RU003685}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01358, KW ECO:0000256|RuleBase:RU003685}. FT DOMAIN 124..393 FT /note="Complex1_49kDa" FT /evidence="ECO:0000259|Pfam:PF00346" SQ SEQUENCE 393 AA; 45505 MW; 5CB02F3A51826035 CRC64; MNGTAKRKDL MVVNMGPHHP SMHGVLRLIV TLDGEDVIDC EPLLGYLHRG MEKIAENRTI IQYLPYVTRW DYLATMFTEA ITVNGPEQLG NIQVPQRASY IRVIMLELSR IASHLLWLGP FMADIGAQTP FFYIFREREL IYDLFEAATG MRMMHNFFRI GGVAADLPHG WIDKCLDFCD YFLTGVVEYQ KLITRNPIFL ERVEGIGIVS GKEVINWGLS GPMLRASGIQ WDLRKVENYE CYGEFDWDVQ WQKEGDSLAR YLVRIGEMVE SIKIIQQALE GIPGGPYENL EIRYFDRERE PEWNDFEYRF ISKKPSPTFE LPKQELYVRV EAPKGELGIF LIGDQNGFPW RWKIRPPGFI NLQILPQLVK RMKLADIMTI LGSIDIIMGE VDR //