ID A0A0K0LN23_9ORYZ Unreviewed; 510 AA. AC A0A0K0LN23; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 20-JAN-2016, entry version 3. 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:AJC09909.1}; OS Oryza glumipatula. OG Plastid; Chloroplast {ECO:0000313|EMBL:AJC09909.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza. OX NCBI_TaxID=40148 {ECO:0000313|EMBL:AJC09909.1}; RN [1] {ECO:0000313|EMBL:AJC09909.1} RP NUCLEOTIDE SEQUENCE. RA Chen X.-L., Norrbom A., Zhu C.-D.; RT "A systematic study of Ichneumonosoma Meijere, Pelmatops Enderlein, RT Pseudopelmatops Shiraki and Soita Walker (Diptera: Tephritidae)."; RL Submitted (JUL-2014) 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: NAD(P)H + plastoquinone = NAD(P)(+) + CC plastoquinol. {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; KM103374; AJC09887.1; -; Genomic_DNA. DR EMBL; KM103374; AJC09909.1; -; 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-HAMAP. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 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:AJC09909.1}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00445}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00445, ECO:0000256|RuleBase:RU000317}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00445, ECO:0000256|RuleBase:RU000319}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00445, KW ECO:0000256|RuleBase:RU000317}; KW Plastid {ECO:0000313|EMBL:AJC09909.1}; KW Plastoquinone {ECO:0000256|HAMAP-Rule:MF_00445, KW ECO:0000256|RuleBase:RU000319}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_00445, KW ECO:0000256|RuleBase:RU000319}; 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 31 51 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 124 144 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 149 169 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 183 203 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 229 249 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 295 315 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 323 343 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 354 374 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 395 415 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 418 438 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT DOMAIN 146 443 Proton_antipo_M. {ECO:0000259|Pfam: FT PF00361}. SQ SEQUENCE 510 AA; 56769 MW; 8BC27F90806815E6 CRC64; MIWHVQNENF ILDSTRIFMK AFHLLLFQGS FIFPECILIF GLILLLMIDL TSDQKDRPWF YFISSTSLVI SITALLFRWR EEPIISFSGN FQTNNFNEIF QFLILLCSTL CIPLSVEYIE CTEMAITEFL LFVLTATLGG MFLCGANDLI TIFVAPECFS LCSYLLSGYT KRDLRSNEAT MKYLLMGGAS SSILVHGFSW LYGSSGGEIE LQEIVNGLIN TQMYNSPGIS IALISITVGL GFKLSPAPFH QWTPDVYEGS PTPVVAFLSV TSKVAASASA TRILDIPFYF SSNEWHLLLE ILAILSMILG NLLAITQTSM KRMLAYSSIG QIGYVIIGII VGDSNDGYAS MITYMLFYIS MNLGTFACIV LFGLRTGTDN IRDYAGLYTK DPFLALSLAL CLLSLGGLPP LAGFFGKLYL FWCGWQAGLY FLVSIGLLTS VLSIYYYLKI VKLLMTGRNQ EITPYVRNYR RSPLRSNNSI ELSMTVCVIA STIPGISMNP ILAIAQDTLF //