ID   A0A6M8ZIZ6_TROMA        Unreviewed;       739 AA.
AC   A0A6M8ZIZ6;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   27-NOV-2024, entry version 17.
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:QKK51133.1};
OS   Tropaeolum majus (Common nasturtium) (Indian cress).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:QKK51133.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Tropaeolaceae; Tropaeolum.
OX   NCBI_TaxID=4020 {ECO:0000313|EMBL:QKK51133.1};
RN   [1] {ECO:0000313|EMBL:QKK51133.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Rigault P., Hohmann N., Wolf E., Koch M.;
RL   Submitted (MAR-2019) 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 + 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}.
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DR   EMBL; MK637814; QKK51133.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6M8ZIZ6; -.
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   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:QKK51133.1};
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};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, 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..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   TRANSMEM        148..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   TRANSMEM        187..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   TRANSMEM        223..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   TRANSMEM        260..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   TRANSMEM        287..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        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        546..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   TRANSMEM        596..619
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   TRANSMEM        719..738
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..442
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
FT   DOMAIN          448..689
FT                   /note="NADH:ubiquinone/plastoquinone oxidoreductase
FT                   chloroplast chain 5 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01010"
SQ   SEQUENCE   739 AA;  83821 MW;  1567FA830693084C CRC64;
     MQHTYQYSWI IPLIPLPVPI LLGVGLLLFP TATKNLRRLW AFLSIFLLSI VMVFSVDLSI
     QQITRSSAHQ YLRSWTINNE VSFEFGHFVD PLTSIMSILI TTVGIFVLIY SDNYMYHDQG
     YLRFFAYMSF FNTSMLGLVI SSNLIQVYIF WEFVGMCSYL LIGFWFTRPI AANACQKAFV
     TNRVGDFGLL LGILGLYWIT GSFEFQDLFK IFNNCIYNNK VDFLFVTLCA FLLFAGPIAK
     SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLVARL LPLFKVIPYI MYLIPLVGTI
     TALLGATLAL AQKDIKRSLA YSTMSQLGYI MLALGMGSYR AALFHLITHA YSKALLFLGS
     GSIIHSMEAI VGYSPAKSQN MVLMGGLKKH VPITKIAFFL GTLSLCGIPP LACFWSKDEI
     LNDSWLYSPI FAIIAYFTAG LTAFYMFRVY LLTFEGHLNI HFQNYSNKKS SSFYSISLWG
     KEEQKNINRD FHLVPLLIMN NKERVSFFLK KAYKITSNAR NRTFITITSF GIKTPFSYPH
     ESDNTILFPM LILVLFSFFV GAIGIPFNQE GIGFDILSKL LTPSINPLHQ NAKNFVYWYA
     FFTNAIFSVS IAFLGIFIAS SLYNPFYSSL QNFNLVNSFV KRGPTRIFWE KISHFLYDWS
     YNRGYIDTFY TISLTKGIRG LAELTHFFDK RVIDGITNGI GITSFFVGEG IKYVGGGRIS
     SHLLIFFSYV LVLIFLLIY
//