ID A0A290D499_9ASPA Unreviewed; 510 AA. AC A0A290D499; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 16-JAN-2019, entry version 5. 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:ATB18773.1}; OS Barnardia japonica. OG Plastid; Chloroplast {ECO:0000313|EMBL:ATB18773.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Asparagales; Hyacinthaceae; OC Hyacinthoideae; Hyacintheae; Barnardia. OX NCBI_TaxID=2033023 {ECO:0000313|EMBL:ATB18773.1}; RN [1] {ECO:0000313|EMBL:ATB18773.1} RP NUCLEOTIDE SEQUENCE. RA Park H., Kim C., Kim J.-H.; RT "The comparative plastid genome analysis and its phylogenetic RT implication on Asparagaceae s.l."; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. 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 quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:132124; Evidence={ECO:0000256|HAMAP-Rule:MF_00445}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + 5 H(+)(in) + NADPH = a quinol + 4 H(+)(out) + CC NADP(+); Xref=Rhea:RHEA:57892, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:24646, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:132124; 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; KX822775; ATB18773.1; -; Genomic_DNA. DR EMBL; KX822775; ATB18789.1; -; 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:ATB18773.1}; 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 Plastid {ECO:0000313|EMBL:ATB18773.1}; 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 Translocase {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 183 203 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 DOMAIN 146 442 Proton_antipo_M. {ECO:0000259|Pfam: FT PF00361}. SQ SEQUENCE 510 AA; 56753 MW; DEB143525A73F2D7 CRC64; MIWHVQNENF ILDSTRIFMK AFHLLLFHGS FIFPECILIF GLILLLMIDS TSDQKDRPWF YFISSTSLVM SITALLFRWK EEPIISFSGN FQTNNFNEIF QFLILLCSTL CIPLSVEYIE CTEMAITEFL LFVLTATLGG MFLCGANDLI TIFVAPECFS LCSYLLSGYT KRDVRSNEAT TKYLLMGGAS SSILVHGFSW LYGSSGGEIE LQEIVNGLIN TQMYNSPGIS IALISITVGI GFKLSPAPFH QWTPDVYEGS PTPVVAFLSV TSKVAASASA TRIFDIPFYF SSNEWHLLLE ILAILSMILG NLIAITQTSM KRMLAYSSIG QIGYVIIGII VGDSNDGYAS MITYMLFYIS MNLGTFARIV SFGLRTGTDN IRDYAGLYTK DPFLALSSAL CLLSLGGLPP LAGFFGKLHL FWCGWQAGLY FLVSIGLLTS VVSIYYYLKI IKLLMTGRNQ EITPHVRNYR RSPLRSNNSI EWSMTVCVIA STIPGISMNP ILAIAQDTLF //