ID A0A2D3C2A0_9MAGN Unreviewed; 510 AA. AC A0A2D3C2A0; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 05-DEC-2018, entry version 5. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic {ECO:0000256|HAMAP-Rule:MF_00445}; DE EC=1.6.5.- {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; Magnoliophyta; eudicotyledons; Ranunculales; OC Ranunculaceae; Ranunculoideae; 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 RT (Ranunculaceae): a traditional herbal medicinal genus."; RL J. Anim. Genet. PeerJ:e4018-e4018(2017). CC -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via CC FMN and iron-sulfur (Fe-S) centers, to quinones in the CC photosynthetic chain and possibly in a chloroplast respiratory CC chain. The immediate electron acceptor for the enzyme in this CC species is believed to be plastoquinone. Couples the redox CC reaction to proton translocation, and thus conserves the redox CC energy in a proton gradient. {ECO:0000256|HAMAP-Rule:MF_00445}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a plastoquinone + H(+) + NADPH = a plastoquinol + CC NADP(+); Xref=Rhea:RHEA:42612, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17757, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:62192, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00445}; CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of CC which are encoded in the nucleus. {ECO:0000256|HAMAP- CC Rule:MF_00445}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_00445}; Multi-pass membrane protein CC {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 GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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 Pfam; PF00361; Proton_antipo_M; 1. DR TIGRFAMs; TIGR01770; NDH_I_N; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:ATU06867.1}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00445}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00445}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00445}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00445}; KW Plastid {ECO:0000313|EMBL:ATU06867.1}; KW Plastoquinone {ECO:0000256|HAMAP-Rule:MF_00445}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_00445}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00445}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00445}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00445}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00445}. FT TRANSMEM 25 47 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 59 79 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 99 119 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 126 143 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 223 244 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 296 316 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 323 342 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 348 372 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 393 415 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 427 448 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 480 505 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT DOMAIN 146 442 Proton_antipo_M. {ECO:0000259|Pfam: FT 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 //