ID   A0A0R5WSX9_9MAGN        Unreviewed;       564 AA.
AC   A0A0R5WSX9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-NOV-2024, entry version 32.
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};
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 reconstruction of
RT   the genus Goniothalamus (Annonaceae), including a reassessment of previous
RT   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 Goniothalamus
RT   (Annonaceae) inferred from nine chloroplast DNA regions: Synapomorphies and
RT   putative correlated evolutionary changes in fruit and seed morphology.";
RL   Mol. Phylogenet. Evol. 92:124-139(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, ECO:0000256|RuleBase:RU364062}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + NADH + (n+1) H(+)(in) = a plastoquinol +
CC         NAD(+) + n H(+)(out); 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 + NADPH + (n+1) H(+)(in) = a plastoquinol +
CC         NADP(+) + n H(+)(out); 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: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000256|ARBA:ARBA00004454, ECO:0000256|RuleBase:RU364062}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004454,
CC       ECO:0000256|RuleBase:RU364062}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 5 family.
CC       {ECO:0000256|ARBA:ARBA00008200, ECO:0000256|RuleBase:RU364062}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU364062}.
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DR   EMBL; KM818671; AJF44262.1; -; 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:0003954; F:NADH dehydrogenase activity; IEA:TreeGrafter.
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   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   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:AJF44262.1};
KW   Plastoquinone {ECO:0000256|ARBA:ARBA00022957,
KW   ECO:0000256|RuleBase:RU364062};
KW   Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|RuleBase:RU364062};
KW   Signal {ECO:0000256|SAM:SignalP};
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};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364062}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..564
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT                   chloroplastic"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006587608"
FT   TRANSMEM        34..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   TRANSMEM        65..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   TRANSMEM        109..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   TRANSMEM        140..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   TRANSMEM        178..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   TRANSMEM        275..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   TRANSMEM        445..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   DOMAIN          1..290
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
FT   DOMAIN          298..537
FT                   /note="NADH:ubiquinone/plastoquinone oxidoreductase
FT                   chloroplast chain 5 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01010"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AJF44262.1"
FT   NON_TER         564
FT                   /evidence="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
//