ID A0A0R5WSX9_9MAGN Unreviewed; 564 AA. AC A0A0R5WSX9; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 31-JUL-2019, entry version 16. 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:AJF44262.1}; OS Goniothalamus wrayi. OG Plastid; Chloroplast {ECO:0000313|EMBL:AJF44262.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Magnoliidae; Magnoliales; Annonaceae; OC Annonoideae; Annoneae; Goniothalamus. OX NCBI_TaxID=261085 {ECO:0000313|EMBL:AJF44262.1}; RN [1] {ECO:0000313|EMBL:AJF44262.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26286044; DOI=10.1016/j.dib.2015.06.021; RA Tang C.C., Thomas D.C., Saunders R.M.K.; RT "Molecular and morphological data supporting phylogenetic RT reconstruction of the genus Goniothalamus (Annonaceae), including a RT reassessment of previous infrageneric classifications."; RL Data Brief 4:410-421(2015). RN [2] {ECO:0000313|EMBL:AJF44262.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26134978; DOI=10.1016/j.ympev.2015.06.016; RA Tang C.C., Thomas D.C., Saunders R.M.; RT "Molecular phylogenetics of the species-rich angiosperm genus RT Goniothalamus (Annonaceae) inferred from nine chloroplast DNA regions: RT Synapomorphies and putative correlated evolutionary changes in fruit RT and seed morphology."; RL Mol. Phylogenet. Evol. 92:124-139(2015). CC -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via CC FMN and iron-sulfur (Fe-S) centers, to quinones in the CC photosynthetic chain and possibly in a chloroplast respiratory CC chain. The immediate electron acceptor for the enzyme in this CC species is believed to be plastoquinone. Couples the redox CC reaction to proton translocation, and thus conserves the redox CC energy in a proton gradient. {ECO:0000256|RuleBase:RU364062}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol CC + n H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA- CC COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17757, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:62192; Evidence={ECO:0000256|RuleBase:RU364062, CC ECO:0000256|SAAS:SAAS01131453}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol CC + n H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA- CC COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17757, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:62192; Evidence={ECO:0000256|RuleBase:RU364062, CC ECO:0000256|SAAS:SAAS01131456}; CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of CC which are encoded in the nucleus. {ECO:0000256|RuleBase:RU364062}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|RuleBase:RU364062}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU364062}. CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. CC {ECO:0000256|RuleBase:RU364062, ECO:0000256|SAAS:SAAS00573047}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {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; KM818671; AJF44262.1; -; 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 Pfam; PF01010; Proton_antipo_C; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR PRINTS; PR01435; NPOXDRDTASE5. DR TIGRFAMs; TIGR01974; NDH_I_L; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000256|RuleBase:RU364062, KW ECO:0000313|EMBL:AJF44262.1}; KW Membrane {ECO:0000256|RuleBase:RU364062, KW ECO:0000256|SAAS:SAAS00106943}; KW NAD {ECO:0000256|RuleBase:RU364062, ECO:0000256|SAAS:SAAS00464237}; KW NADP {ECO:0000256|RuleBase:RU364062, ECO:0000256|SAAS:SAAS00093259}; KW Plastid {ECO:0000256|RuleBase:RU364062, ECO:0000313|EMBL:AJF44262.1}; KW Plastoquinone {ECO:0000256|RuleBase:RU364062, KW ECO:0000256|SAAS:SAAS00430364}; KW Quinone {ECO:0000256|RuleBase:RU364062}; KW Signal {ECO:0000256|SAM:SignalP}; KW Thylakoid {ECO:0000256|RuleBase:RU364062}; KW Translocase {ECO:0000256|SAAS:SAAS01133474}; KW Transmembrane {ECO:0000256|RuleBase:RU364062, KW ECO:0000256|SAAS:SAAS00470986}; KW Transmembrane helix {ECO:0000256|RuleBase:RU364062, KW ECO:0000256|SAAS:SAAS00470995}; KW Transport {ECO:0000256|RuleBase:RU364062}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 564 NAD(P)H-quinone oxidoreductase subunit 5, FT chloroplastic. {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006587608. FT TRANSMEM 34 53 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 65 89 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 109 128 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 140 158 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 178 197 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 275 297 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 445 471 Helical. {ECO:0000256|RuleBase:RU364062}. FT DOMAIN 1 292 Proton_antipo_M. {ECO:0000259|Pfam: FT PF00361}. FT DOMAIN 298 537 Proton_antipo_C. {ECO:0000259|Pfam: FT PF01010}. FT NON_TER 1 1 {ECO:0000313|EMBL:AJF44262.1}. FT NON_TER 564 564 {ECO:0000313|EMBL:AJF44262.1}. SQ SEQUENCE 564 AA; 62629 MW; B08D06EB7E28C266 CRC64; WELVGMCSYL LIGFWFTRPI AANACQKAFV TNRVGDFGLL LGILGFYWIT GSFEFRELFE MLNNLISNGG VNSFFVTLCA FLLFVGAVAK SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGVFLVARL FPLFRVIPHI MGLISFIGII TVLLGATLSL AQRDIKGSLA YSTTSQLGYI MLAPGIGSYR AALFHLITHA YSKALLFLGS GSVIHSMESI VGYSPDKSQN MVLMGGLTKY VPITKSTFYV GTLSLCGIPP LACFWSKDEX XNDSWLYSPV FAIIACSAAG LTAFYMFRIY LLTFEGHLRV QFQNYSGTKN GSLYSIPIWG KEGVGLGNKN LSFLVITNNE RLSFFSNKVY QMGGNVRNSM QVFSTHSDNK DNSTYPHESD XXXXXXXXXX XXFTLFVGSI GISFEQLGMS FDILSKLLTP PITFLQKKIK YSVDWYEFVT TNSIFSVSIA CFGIFVASLF YGSVYSSFQN LDLINSFVKK VSYRIFSDQI TSGIYSWSYN RGYIDVFYTT FVIRGIRELA QLTHFFDKRI IDGITNSVGI ATFFVGEGIK YVRG //