ID Q32862_9ASTR Unreviewed; 744 AA. AC Q32862; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 106. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic {ECO:0000256|ARBA:ARBA00018648, 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}; GN Name=ndhF {ECO:0000256|RuleBase:RU364062, GN ECO:0000313|EMBL:AAA81357.1}; OS Perezia microcephala. OG Plastid; Chloroplast {ECO:0000313|EMBL:AAA81357.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; campanulids; Asterales; Asteraceae; Mutisioideae; Nassauvieae; OC Perezia. OX NCBI_TaxID=40565 {ECO:0000313|EMBL:AAA81357.1}; RN [1] {ECO:0000313|EMBL:AAA81357.1} RP NUCLEOTIDE SEQUENCE. RA Kim K.-J., Jansen R.K.; RT "ndhF sequence evolution and phylogenetic relationships in the sunflower RT family."; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. 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, 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; L39407; AAA81357.1; -; Genomic_DNA. DR PIR; T13585; T13585. DR AlphaFoldDB; Q32862; -. 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 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, ECO:0000256|RuleBase:RU364062}; 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|RuleBase:RU364062, ECO:0000313|EMBL:AAA81357.1}; 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 85..109 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 121..139 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 145..166 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 187..209 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..287 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 293..311 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 327..348 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 396..417 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 429..451 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 548..569 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 607..625 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 694..713 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 725..742 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" 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..441 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 448..691 FT /note="NADH:ubiquinone/plastoquinone oxidoreductase FT chloroplast chain 5 C-terminal" FT /evidence="ECO:0000259|Pfam:PF01010" SQ SEQUENCE 744 AA; 84227 MW; EC6542FEA7DCC051 CRC64; MEQTYQYAWI IPFLPLPVPM LIGLGLLLFP TATKSLRRMW AFQSVLLLSI VMIFSMNLSI QQINSSSVYQ YVWSWIINND FSLEFGYLID PLTSIMSILI TTVGILVLIY SDNYMSYDHG YLRFFAYMSF FSTSMLGLVT SSNLIQIYIF WELVGICSYL LIGFWFTRPV AAKACQKAFV TNRVGDFGLL LGILGFYWVT GSFEFRNLFQ IFNNLISNNE VNFVFVTLCA ILLFAGAIAK SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLVARL LPLFIVIPHI MNLISLIGII TVFLGATLAL AQKDIKRGLA YSTMSQLGYM MLALGMGSYR SALFHLITHA YSKALLFLGS GSVIHSMETL VGYCPKKSQN MVLMGGLTKH VPITKTSFLL GTLSLCGIPP LACFWSKDEI LNDSWLYSPI FAIIAWSTAG LTAFYMCRIY LLTFEGHLNV HFQNYSGKKN TPFYSISLWG KEGSKISNKN FRLVTLLKMK NNGCASFFSN KVYKIDENLR NMIQPFLSIH HFGNTKTYSY PYESDNTMLF PILILVLFTL FVGFLGIPFN QDGGYLDILS KWLTPSINLL HKNSNNSIDW YEFCKDAVFS VSISSFGILI AFFLYKPVYS SFQNLDLINS FVKIGPKRIF SDKIKNGIYD WSYNRGYIDA FYGTFLTVGI RKLAKFAHFF DRRIIDGIPN GVGLMSFFVA EVIKSVGGGR ISSYLFFYFS YVSIFLLIYY CLNF //