ID A0A8F8SNH4_CONCI Unreviewed; 501 AA. AC A0A8F8SNH4; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 02-OCT-2024, entry version 10. 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:QYB18653.1}; GN Synonyms=ndh2 {ECO:0000313|EMBL:QYB18653.1}; OS Conocephalum conicum (Snakeskin liverwort) (Marchantia conica). OG Plastid; Chloroplast {ECO:0000313|EMBL:QYB18653.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta; OC Marchantiopsida; Marchantiidae; Marchantiales; Conocephalaceae; OC Conocephalum. OX NCBI_TaxID=41839 {ECO:0000313|EMBL:QYB18653.1}; RN [1] {ECO:0000313|EMBL:QYB18653.1} RP NUCLEOTIDE SEQUENCE. RA Sawicki J., Baczkiewicz A., Buczkowska K., Gorski P., Krawczyk K., RA Mizia P., Myszczynski K., Slipiko M., Szczecinska M.; RT "Combined nanopore and short reads sequencing enabled assembling tandem RT repeats rich plastome of Concephalum species (Marchantiales, Bryophyta) RT revealing the first exception in the evolutionarily-stable structure of RT liverwort chloroplast genomes."; RL Submitted (FEB-2020) 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; MT023024; QYB18653.1; -; Genomic_DNA. DR EMBL; MT023025; QYB18740.1; -; Genomic_DNA. 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:SF116; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 2 A, CHLOROPLASTIC-RELATED; 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:QYB18653.1}; 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:QYB18653.1}; 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|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 15..35 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 42..62 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 82..102 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 109..126 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 132..152 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 164..185 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 211..235 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 247..274 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 280..299 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 306..324 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 330..354 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 375..398 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 410..430 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT TRANSMEM 466..489 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445" FT DOMAIN 1..100 FT /note="NAD(P)H-quinone oxidoreductase subunit 2 N-terminal" FT /evidence="ECO:0000259|Pfam:PF19530" FT DOMAIN 129..425 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" SQ SEQUENCE 501 AA; 56227 MW; FD1291DED869BEEE CRC64; MKLELNLFFL YENTILPECI LIFSLLTILI IDLTVSKKDT TWLYLISLTS LLISIIILLF QYKTEPILTF LGSFETNSFN RIFRSFIALC SILCIPLSIE YIKCTKMPIP EFIIFILTAT VGGMFLCGAN DLVTIFVSLE CLSLCSYLLC GYTKRDIRSN EAAMKYLLIG GTSSSILAYG FSWLYGLSGG ETNIEKIVNG LLNTQMSNSS VTYIAFICIL VGLGFKLSIV PFHQWTPDIY EGSPTPVVAF LSVTSKIAGL ALAAKIFNIL FGFSPNEWKV FLEILAILSM ILGNLVAITQ TSMKRMLAYS SISQIGYILI GLILNDLKGY TSMTIYVFFY IFMNLGTFAS IILFSLRTGT DNIRDYAGLY IKDPLLSVSL TLCLLSLGGL PPLTGFFGKL YLFWCGWQSG FYLLVFVGLI TSVISLYYYL KIIKLILNKK NNEINPYIQA YIITSPTFFS KNPVEFVIIF CTLGSTFLGI IINPIFYFFQ DNLSLSIFFI N //