ID A0A2D3C2A0_9MAGN Unreviewed; 510 AA. AC A0A2D3C2A0; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 22-FEB-2023, entry version 16. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic {ECO:0000256|HAMAP-Rule:MF_00445}; DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_00445}; DE AltName: Full=NAD(P)H dehydrogenase, subunit 2 {ECO:0000256|HAMAP-Rule:MF_00445}; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 2 {ECO:0000256|HAMAP-Rule:MF_00445}; GN Name=ndhB {ECO:0000256|HAMAP-Rule:MF_00445, GN ECO:0000313|EMBL:ATU06867.1}; OS Aconitum angustius. OG Plastid; Chloroplast {ECO:0000313|EMBL:ATU06867.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Ranunculoideae; OC Delphinieae; Aconitum. OX NCBI_TaxID=1045221 {ECO:0000313|EMBL:ATU06867.1}; RN [1] {ECO:0000313|EMBL:ATU06867.1} RP NUCLEOTIDE SEQUENCE. RA Kong H., Gong W.; RT "A comparison of chloroplast genome sequences in Aconitum (Ranunculaceae): RT a traditional herbal medicinal genus."; RL J. Anim. Genet. 5:e4018-0(2017). 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_00445}. 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_00445}; 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_00445}; 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_00445}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid, CC chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_00445}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00445}. CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. CC {ECO:0000256|HAMAP-Rule:MF_00445}. 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; MF155664; ATU06853.1; -; Genomic_DNA. DR EMBL; MF155664; ATU06867.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2D3C2A0; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule. DR HAMAP; MF_00445; NDH1_NuoN_1; 1. DR InterPro; IPR010096; NADH-Q_OxRdtase_suN/2. DR InterPro; IPR001750; ND/Mrp_mem. DR InterPro; IPR045693; Ndh2_N. DR PANTHER; PTHR22773:SF116; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 2 A, CHLOROPLASTIC-RELATED; 1. DR PANTHER; PTHR22773; NADH DEHYDROGENASE; 1. DR Pfam; PF19530; Ndh2_N; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR PRINTS; PR01434; NADHDHGNASE5. DR TIGRFAMs; TIGR01770; NDH_I_N; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:ATU06867.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00445}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00445}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00445}; KW Plastid {ECO:0000313|EMBL:ATU06867.1}; KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957, ECO:0000256|HAMAP- KW Rule:MF_00445}; KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_00445}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00445}; KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP- KW Rule:MF_00445}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_00445}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_00445}; Transport {ECO:0000256|HAMAP-Rule:MF_00445}. FT TRANSMEM 25..47 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 59..79 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 99..119 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 126..143 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 223..244 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 296..316 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 323..342 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 348..372 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 393..415 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 427..448 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 480..505 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT DOMAIN 18..117 FT /note="NAD(P)H-quinone oxidoreductase subunit 2 N-terminal" FT /evidence="ECO:0000259|Pfam:PF19530" FT DOMAIN 146..442 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" SQ SEQUENCE 510 AA; 56679 MW; 262A91273B3C1FC1 CRC64; MIWHVQNENF ILDSTRIFMK AFHLLLFHGS FIFPECILIF GLILLLMIDS TSDQKDIPWL YFISSTSLVM SIAALLFRWR EEPMISFSGN FQTNNFNEIF QFLILLCSTL CIPLSVEYIE CTEMAITEFL LFVLTATLGG MFLCGANDLI TIFVAPECFS LCSYLLSGYT KRDVRSNEAT TKYLLMGGAS SSILVHGFSW LYGSSGGEIE LQEIVNGLIN TQMYNSPGIS IALIFITVGI GFKLSPAPSH QWTPDVYEGS PTPVVAFLSV TSKVAASALA TRIFDIPFYF SSNEWHLLLE ILAILSMILG NLIAITQTSM KRMLAYSSIG QIGYVIIGII VGDSNDGYAS MITYMLFYIY MNLGTFACIV SFGLRTGTDN IRDYAGLYTK DPFLALSLAL CLLSLGGLPP LAGFFGKLHL FWCGWQAGLY FLVSIGLLTS VVSIYYYLKI IKLLMTGRNQ EITPHVRNYK RSPLRSNNSI ELSMIVCVIA STIPGISMNP IIAIAQDTLF //