ID A0A0S2IGG9_CUCPE Unreviewed; 748 AA. AC A0A0S2IGG9; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 29-MAY-2024, entry version 26. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic {ECO:0000256|ARBA:ARBA00018648}; DE AltName: Full=NAD(P)H dehydrogenase subunit 5 {ECO:0000256|ARBA:ARBA00031649}; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 5 {ECO:0000256|ARBA:ARBA00029876}; GN Name=ndhF {ECO:0000313|EMBL:ALO22672.1}; OS Cucurbita pepo var. ozarkana. OG Plastid {ECO:0000313|EMBL:ALO22672.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita. OX NCBI_TaxID=184142 {ECO:0000313|EMBL:ALO22672.1}; RN [1] {ECO:0000313|EMBL:ALO22672.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=013 {ECO:0000313|EMBL:ALO22672.1}; RX PubMed=26630007; DOI=10.1073/pnas.1516109112; RA Kistler L., Newsom L.A., Ryan T.M., Clarke A.C., Smith B.D., Perry G.H.; RT "Gourds and squashes (Cucurbita spp.) adapted to megafaunal extinction and RT ecological anachronism through domestication."; RL Proc. Natl. Acad. Sci. U.S.A. 112:15107-15112(2015). 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:ARBA00004059}. 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 -!- 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 -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which CC are encoded in the nucleus. {ECO:0000256|ARBA:ARBA00011199}. 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}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004454}. CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. CC {ECO:0000256|ARBA:ARBA00008200}. 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; KT898818; ALO22672.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0S2IGG9; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IEA:TreeGrafter. 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:0015990; P:electron transport coupled proton transport; IEA:TreeGrafter. DR Gene3D; 1.20.5.2700; -; 1. DR InterPro; IPR002128; NADH_UbQ_OxRdtase_chlpt_su5_C. DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr. DR InterPro; IPR001750; ND/Mrp_mem. DR InterPro; IPR003945; NU5C-like. DR InterPro; IPR001516; Proton_antipo_N. DR NCBIfam; TIGR01974; NDH_I_L; 1. DR PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1. DR PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1. DR Pfam; PF01010; Proton_antipo_C; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR Pfam; PF00662; Proton_antipo_N; 1. DR PRINTS; PR01434; NADHDHGNASE5. DR PRINTS; PR01435; NPOXDRDTASE5. PE 3: Inferred from homology; KW Chloroplast {ECO:0000256|ARBA:ARBA00022528}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857}; KW Plastid {ECO:0000313|EMBL:ALO22672.1}; KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957}; KW Quinone {ECO:0000256|ARBA:ARBA00022719}; KW Thylakoid {ECO:0000256|ARBA:ARBA00023078}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 6..28 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 40..60 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 85..109 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 121..139 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 145..167 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 179..201 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 221..239 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 260..281 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 287..311 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 327..348 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 354..373 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 393..412 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 424..447 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 549..570 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 611..629 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 728..747 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 75..125 FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5 FT N-terminal" FT /evidence="ECO:0000259|Pfam:PF00662" FT DOMAIN 141..440 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 448..695 FT /note="NADH:ubiquinone/plastoquinone oxidoreductase FT chloroplast chain 5 C-terminal" FT /evidence="ECO:0000259|Pfam:PF01010" SQ SEQUENCE 748 AA; 85002 MW; F5EE2BC5D6131EB1 CRC64; MEYTYQYSWI IPFISLPIPI LIGVGLLLFP TATKNLRRMW SFPSILLLSI VMIFSVYLSI DQINSSYIYQ YVWSWTINNA FSLELGYLID PLTCIMSILI TTVGIMVLIY SDNYMSHDQG YLRFFAYMSL FNTSMLGLVT SSNLIQIYIF WELVGMCSYL LIGFWFTRPT AANACQKAFV TNRVGDFGLL LGILGLYWTT GSFEFRDLFK IFNNLIYNNE VNLLFVTLCA VLLFAGAVAK SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLVARL LPLFIVIPYI MNLIAFIGII TVLFGATLAL AQKDIKRSLA YSTMSQLGYM MLALGIGSYR AALFHLITHA YSKALLFLGS GSIIHSMESV VGYSPDKSQN MVLMGGLTKH VPITKNAFLL GTLSLCGIPP LACFWSKDEI LNDSWLYSPI FAIIACSTAG LTAFYMFRIY LLTFEGHLNL YFKKYSGKTN NSLYSISLWG KEGSKIIKKN FPFLSLLTMN NNQRSSFLGK KTAYQMDSNV TKMMRPFVSI PHFCTKTTFS YPYESDNTML FPMFVLSLFT LFVGVIGIPF TQFNQEAIEL NILDKWLTPS INLLHESSTD SENWYEFVKN ATFSVSIAYF GIFIASFFYK PAYSSLQNLN FRNSFVKSFT KNFFFEKLIN IIYNWSYNRG YIDAFYRISL IGGIRVLAEL TYFFDRRVID GITNAVGILN FFVAESIKYV GGGRISSYIF LYLAYVFIFI LLIYFVLF //