ID A0A0K0LN23_9ORYZ Unreviewed; 510 AA. AC A0A0K0LN23; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 27-MAR-2024, entry version 23. 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:AJC09909.1}; OS Oryza glumipatula. OG Plastid; Chloroplast {ECO:0000313|EMBL:AJC09909.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza. OX NCBI_TaxID=40148 {ECO:0000313|EMBL:AJC09909.1}; RN [1] {ECO:0000313|EMBL:AGY93501.1} RP NUCLEOTIDE SEQUENCE. RA Pilkington S.; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {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. RN [3] {ECO:0000313|EMBL:ALK00732.1} RP NUCLEOTIDE SEQUENCE. RA Kim K.-H., Yu Y.-S., Wing R.-A., Yang T.-J.; RT "High throughput and simultaneous assembly of complete chloroplast and RT nuclear ribosomal DNA sequences from plant genomes."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain CC NADH dehydrogenase (Complex I) that is believed to belong to the CC minimal assembly required for catalysis. Complex I functions in the CC transfer of electrons from NADH to the respiratory chain. The immediate CC electron acceptor for the enzyme is believed to be ubiquinone. CC {ECO:0000256|ARBA:ARBA00003257}. 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; KF359905; AGY93501.1; -; Genomic_DNA. DR EMBL; KF359905; AGY93520.1; -; Genomic_DNA. DR EMBL; KM103374; AJC09887.1; -; Genomic_DNA. DR EMBL; KM103374; AJC09909.1; -; Genomic_DNA. DR EMBL; KR364802; ALK00732.1; -; Genomic_DNA. DR EMBL; KR364802; ALK00759.1; -; Genomic_DNA. DR EMBL; KR364803; ALK00837.1; -; Genomic_DNA. DR EMBL; KR364803; ALK00862.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0K0LN23; -. DR SMR; A0A0K0LN23; -. 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 NCBIfam; TIGR01770; NDH_I_N; 1. DR PANTHER; PTHR22773:SF112; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 2 B, CHLOROPLASTIC; 1. DR PANTHER; PTHR22773; NADH DEHYDROGENASE; 1. DR Pfam; PF19530; Ndh2_N; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR PRINTS; PR01434; NADHDHGNASE5. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:AJC09909.1}; 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:AJC09909.1}; 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|ARBA:ARBA00023078, 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}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00445}. FT TRANSMEM 22..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 181..203 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 223..242 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 295..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 DOMAIN 18..117 FT /note="NAD(P)H-quinone oxidoreductase subunit 2 N-terminal" FT /evidence="ECO:0000259|Pfam:PF19530" FT DOMAIN 146..443 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam: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 //