ID A0A060CY16_9ASTR Unreviewed; 510 AA. AC A0A060CY16; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 16-SEP-2015, entry version 10. 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:AIB03821.1}; OS Centaurea diffusa. OG Plastid; Chloroplast {ECO:0000313|EMBL:AIB03821.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; campanulids; Asterales; Asteraceae; OC Carduoideae; Cardueae; Centaureinae; Centaurea. OX NCBI_TaxID=124929 {ECO:0000313|EMBL:AIB03821.1}; RN [1] {ECO:0000313|EMBL:AIB03821.1} RP NUCLEOTIDE SEQUENCE. RA Turner K.G., Grassa C.J.; RT "Centaurea diffusa plastid genome."; RL Submitted (APR-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; KJ690264; AIB03800.1; -; Genomic_DNA. DR EMBL; KJ690264; AIB03821.1; -; Genomic_DNA. DR RefSeq; YP_009040845.1; NC_024286.1. DR RefSeq; YP_009040866.1; NC_024286.1. DR GeneID; 19592143; -. DR GeneID; 19592176; -. 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:AIB03821.1}; 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:AIB03821.1}; 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 24 44 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. FT TRANSMEM 57 77 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 227 247 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 TRANSMEM 484 504 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00445}. SQ SEQUENCE 510 AA; 56706 MW; 7D2F395FCE93A3D9 CRC64; MIWHVQNENF ILDSTRIFMK AFRLLLFDGS LIFPECILIF GLILLLMIDS TSDQKDIPWL YFISSTSLVM SITALLFRWR EEPMISFSGN FQTNNFNEIF QFLILLCSTL CIPLSVEYIE CTEMAITEFL LFVLTATIGG MFLCGANDLI TIFVAPECFS LCSYLLSGYT KKDVRSNEAT MKYLLMGGAS SSILVHGFSW LYGSSGGEIE LQEIVNGLIN TQMYNSPGIS IALIFITVGI GFKLSPAPSH QWTPDVYEGS PTPVVAFLSV TSKVAASASA TRIFDIPFYF SSNEWHLLLE ILAILSMILG NLIAITQTSM KRMLAYSSIA QIGYVIIGII VGDSNDGYAS MITYMLFYIS MNLGTFACIV LFGLRTGTEN IRDYAGLYTK DPFLALSLAL CLLSLGGLPP LAGFFGKLYL FWCGWQAGLY FLVLIGLLTS VVSIYYYLKI IKLLMTGRNQ EITPHVRNYR RSPLRSNNSI ELSMIVCVIA STIPGISMNP IIAIAQDTLF //