ID NU2C_PAUCH Reviewed; 512 AA. AC B1X5D6; DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 1. DT 13-SEP-2023, entry version 44. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 2, organellar chromatophore {ECO:0000255|HAMAP-Rule:MF_00445}; DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00445}; DE AltName: Full=NAD(P)H dehydrogenase, subunit 2 {ECO:0000255|HAMAP-Rule:MF_00445}; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00445}; GN Name=ndhB {ECO:0000255|HAMAP-Rule:MF_00445}; GN OrderedLocusNames=PCC_0740; OS Paulinella chromatophora. OG Plastid; Organellar chromatophore. OC Eukaryota; Sar; Rhizaria; Cercozoa; Imbricatea; Silicofilosea; Euglyphida; OC Paulinellidae; Paulinella. OX NCBI_TaxID=39717; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=18356055; DOI=10.1016/j.cub.2008.02.051; RA Nowack E.C.M., Melkonian M., Gloeckner G.; RT "Chromatophore genome sequence of Paulinella sheds light on acquisition of RT photosynthesis by eukaryotes."; RL Curr. Biol. 18:410-418(2008). CC -!- FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via CC FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory CC and/or the photosynthetic chain. The immediate electron acceptor for CC the enzyme in this species is believed to be plastoquinone. Couples the CC redox reaction to proton translocation, and thus conserves the redox CC energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in CC inorganic carbon-concentration. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00445}; CC -!- SUBUNIT: NDH-1 can be composed of about 15 different subunits; CC different subcomplexes with different compositions have been identified CC which probably have different functions. {ECO:0000255|HAMAP- CC Rule:MF_00445}. CC -!- SUBCELLULAR LOCATION: Plastid, organellar chromatophore thylakoid CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00445}. CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. CC {ECO:0000255|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; CP000815; ACB43155.1; -; Genomic_DNA. DR RefSeq; YP_002049365.1; NC_011087.1. DR AlphaFoldDB; B1X5D6; -. DR SMR; B1X5D6; -. DR GeneID; 6481593; -. DR GO; GO:0070118; C:organellar chromatophore thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule. DR GO; GO:0009536; C:plastid; 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 HAMAP; MF_00445; NDH1_NuoN_1; 1. DR InterPro; IPR010096; NADH-Q_OxRdtase_suN/2. DR InterPro; IPR001750; ND/Mrp_mem. DR NCBIfam; TIGR01770; NDH_I_N; 1. DR PANTHER; PTHR22773:SF116; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 2 A, CHLOROPLASTIC-RELATED; 1. DR PANTHER; PTHR22773; NADH DEHYDROGENASE; 1. DR Pfam; PF00361; Proton_antipo_M; 1. PE 3: Inferred from homology; KW Membrane; NAD; NADP; Organellar chromatophore; Plastid; Plastoquinone; KW Quinone; Thylakoid; Translocase; Transmembrane; Transmembrane helix. FT CHAIN 1..512 FT /note="NAD(P)H-quinone oxidoreductase subunit 2, organellar FT chromatophore" FT /id="PRO_0000344284" FT TRANSMEM 6..26 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 43..63 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 80..100 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 107..127 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 133..153 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 168..188 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 210..230 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 242..262 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 276..296 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 304..324 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 332..352 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 376..396 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 411..431 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" FT TRANSMEM 464..484 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445" SQ SEQUENCE 512 AA; 54053 MW; 8C927D63F7E8FFBD CRC64; MENSGLLALP LNAATIVPEG AILLALLSSL LVDLAGEKTA SRWVPPICYA GLGSALILLA SQWNSTLSPS FLGAFLADNL AIAFRAIIAT STLFSLMISW RYVERSGAPM GEYAAILLAA TLGAMFLCGS TDLVSIFVSL ETLSVSSYLL AGYMKQDARS SEAALKYLLV GSATAAVFLY GASLLYGLTG GSTNLDAVAL ALQSSDTPVA ALALVFVLAT VAFKIAAVPF HQWTPDVYEG APTPIVAFLS VGSKTAGFAL ALRLLVGCFE SFDIQWKFLF SLLAILSMVL GNIVALSQTS MKRMLAYSSI GQAGFVMIGL VCGTEDGFAA MILYLATYLF MNMGAFACVI LFSIRTGSDL IADYAGLYQK DPLVTIGLSL CLLSLGGIPP MLGFFGKIYL FFAGWADHQY LLVVTGLITS VVSIYYYISV IRMMVVIEPK EASDVVKSYA AVNWNIPGLN PLRVALLVCV IVTGIGGIFS NPLFQWANSA VAGTPILQKV IVTALGTTGT IS //