ID A0A249JMU4_9ROSI Unreviewed; 744 AA. AC A0A249JMU4; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 12-AUG-2020, entry version 11. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic {ECO:0000256|RuleBase:RU364062}; DE EC=7.1.1.- {ECO:0000256|RuleBase:RU364062}; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 5 {ECO:0000256|RuleBase:RU364062}; DE Flags: Fragment; GN Name=ndhF {ECO:0000256|RuleBase:RU364062, GN ECO:0000313|EMBL:ASY02466.1}; OS Geranium reflexum. OG Plastid; Chloroplast {ECO:0000313|EMBL:ASY02466.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Geraniales; Geraniaceae; Geranium. OX NCBI_TaxID=379954 {ECO:0000313|EMBL:ASY02466.1}; RN [1] {ECO:0000313|EMBL:ASY02466.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28854633; DOI=10.1093/gbe/evx124; RA Park S., Ruhlman T.A., Weng M.L., Hajrah N.H., Sabir J.S.M., Jansen R.K.; RT "Contrasting Patterns of Nucleotide Substitution Rates Provide Insight into RT Dynamic Evolution of Plastid and Mitochondrial Genomes of Geranium."; RL Genome Biol. Evol. 9:1766-1780(2017). 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|ARBA:ARBA00003229, ECO:0000256|RuleBase:RU364062}. 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|ARBA:ARBA00001230, CC ECO:0000256|RuleBase:RU364062}; 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|ARBA:ARBA00001558, CC ECO:0000256|RuleBase:RU364062}; CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which CC are encoded in the nucleus. {ECO:0000256|ARBA:ARBA00011199, CC ECO:0000256|RuleBase:RU364062}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid, CC chloroplast thylakoid membrane {ECO:0000256|ARBA:ARBA00004454, CC ECO:0000256|RuleBase:RU364062}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004454, ECO:0000256|RuleBase:RU364062}. CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. CC {ECO:0000256|ARBA:ARBA00008200, ECO:0000256|RuleBase:RU364062}. 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; KY687055; ASY02466.1; -; 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 InterPro; IPR002128; NADH_UbQ_OxRdtase_chlpt_su5_C. DR InterPro; IPR003945; NADHpl_OxRdtase_5. DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr. DR InterPro; IPR001750; ND/Mrp_mem. DR InterPro; IPR001516; Proton_antipo_N. DR Pfam; PF01010; Proton_antipo_C; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR Pfam; PF00662; Proton_antipo_N; 1. DR PRINTS; PR01435; NPOXDRDTASE5. DR TIGRFAMs; TIGR01974; NDH_I_L; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000256|ARBA:ARBA00022528, ECO:0000256|RuleBase:RU364062, KW ECO:0000313|EMBL:ASY02466.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364062}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU364062}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU364062}; KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000256|RuleBase:RU364062, KW ECO:0000313|EMBL:ASY02466.1}; KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957, KW ECO:0000256|RuleBase:RU364062}; KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|RuleBase:RU364062}; KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|RuleBase:RU364062}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU364062}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU364062}; Transport {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 6..28 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 40..60 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 92..110 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 122..139 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 145..167 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 179..201 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 221..239 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 260..278 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 284..306 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 327..348 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 354..373 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 393..412 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 424..447 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 545..566 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 600..622 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 721..742 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT DOMAIN 72..128 FT /note="Proton_antipo_N" FT /evidence="ECO:0000259|Pfam:PF00662" FT DOMAIN 141..442 FT /note="Proton_antipo_M" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 448..688 FT /note="Proton_antipo_C" FT /evidence="ECO:0000259|Pfam:PF01010" FT NON_TER 744 FT /evidence="ECO:0000313|EMBL:ASY02466.1" SQ SEQUENCE 744 AA; 84613 MW; 1F6DAA8E2F8B92B9 CRC64; MEYTNKYSWI MPLIPLPVPM LIGVGLLLFP TTTKHLRRIW AFPTVFLLGI VMLLSAYLSI QQLNRSYIYQ YVWSWTINND FSLEFGHLID PLTSTMSILI TTVGLTVLIY SENYMFHDQG YLRFFYYMAF FNASMLGLVT SSNLIQIYIF WEFVGMCSYL LIGFWFTRPV AAKACQKAFV TNRVGDFSLL LGILGLYWIT GSFEFRDLFQ IFNNLVHNNE IPFLFFTLCA FLLFGGALAK SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLVARL LPLFIAIPSI LNLISLIAII TVFLGATLAL AQKDIKRVLA YSTMSQLGYM MLALGVGSYR AALFHLITHA YSKALLFLGS GSIIHSMEAL VGYSPEKSQN MVLMGGLTKH MPITKTAFLL GTLSLCGIPP LACFWSKDEI LNESWLYSPI FAIIAFSTAG FTAFYMFRIY LLTFEGHLNV YFLNYSGKRS SSLYSISLWG NEGLKTIQNP FFFKTSLTMN NKQRVPFFCK KTYRLDSSVR SMIRLFTHFG TKNTLPYPHE SENTMLFPIV VLFLFTFFVG AIGIPFNQEG GGLDILSKFL TPYRNLLHQK SNNSVGWHEF ITNGTLSVTI SYLGIVIASF LYKPFYLSLT KLNFINLFVK GGPKKIWRDK IINRIYDWSY NRGYIDAFYT ISLIKGIREL VEFTHFFDAR VIDGITNGLG ILSFFVGEGI KYVGGGRVSS YLLFYLSCVL ICLLIYYFLY FFNF //