ID   A0A0S2IGG9_CUCPE        Unreviewed;       748 AA.
AC   A0A0S2IGG9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   07-OCT-2020, entry version 15.
DE   RecName: Full=NAD(P)H dehydrogenase subunit 5 {ECO:0000256|ARBA:ARBA00014641};
DE   AltName: Full=NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic {ECO:0000256|ARBA:ARBA00018648};
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit 5 {ECO:0000256|ARBA:ARBA00022291};
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:ARBA00003229}.
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}.
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DR   EMBL; KT898818; ALO22672.1; -; 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   InterPro; IPR001516; Proton_antipo_N.
DR   Pfam; PF01010; Proton_antipo_C; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   Pfam; PF00662; Proton_antipo_N; 1.
DR   PRINTS; PR01435; NPOXDRDTASE5.
DR   TIGRFAMs; TIGR01974; NDH_I_L; 1.
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:0000256|ARBA:ARBA00022640, 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          72..129
FT                   /note="Proton_antipo_N"
FT                   /evidence="ECO:0000259|Pfam:PF00662"
FT   DOMAIN          141..442
FT                   /note="Proton_antipo_M"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
FT   DOMAIN          448..695
FT                   /note="Proton_antipo_C"
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
//