ID   Q32695_9ASTR            Unreviewed;       742 AA.
AC   Q32695;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 110.
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:AAC37763.1};
OS   Asteriscus sericeus.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AAC37763.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae; Inuleae;
OC   Inulinae; Asteriscus.
OX   NCBI_TaxID=41614 {ECO:0000313|EMBL:AAC37763.1};
RN   [1] {ECO:0000313|EMBL:AAC37763.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=7479788; DOI=10.1073/pnas.92.22.10379;
RA   Kim K.J., Jansen R.K.;
RT   "ndhF sequence evolution and the major clades in the sunflower family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:10379-10383(1995).
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}.
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DR   EMBL; L39454; AAC37763.1; -; Genomic_DNA.
DR   PIR; T13495; T13495.
DR   AlphaFoldDB; Q32695; -.
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};
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..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   TRANSMEM        223..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   TRANSMEM        263..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        354..375
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        549..570
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   TRANSMEM        605..623
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364062"
FT   TRANSMEM        722..740
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..689
FT                   /note="NADH:ubiquinone/plastoquinone oxidoreductase
FT                   chloroplast chain 5 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01010"
SQ   SEQUENCE   742 AA;  84236 MW;  3107440E0EAA6E76 CRC64;
     MEQTYQYAWI IPFLPLPVPM LIGLGLLLFP TATKSLRRMW AFQSVLLLSI VMIFSMNLSI
     QQINSSSVYQ YVWSWIINND FSLEFGYLID PLTSIMSILI TTVGILVLIY SDNYMSHDHG
     YLRFFAYMSF FSTSMLGLVT SSNLIQIYIF WELVGICSYL LIGFWFTRPV AAKACQKAFV
     TNRVGDFGLL LGILGFYWIT GSFEFRDLFQ IFNNLISNNE VNFVFVTLCA VLLFAGAIAK
     SAQFPLHVWL PDAMEGPTPI SALIRAATMV AAGIFLVARL MPLFIVIPYI MNFISLIGII
     TVFLGATLAL AQKDIKRGLA YSTMSQLGYM MLALGMGSYR SALFHLITHA YSKALLFLGS
     GSVIHSMEAL VGYCPKKSQN MVLMGGLTKH VPITKNSFLL GTLSLCGIPP LACFWSKDEI
     LNDSWLYSPI FAIIAWSTAG LTAFYMCRIY LLTFEGHLNV HFQNYSGKRN TPFYSISLWG
     KEASKISNKN FRLVTLLKMK KNACPSFFSN KVYEMDENAR NMIQPFLSIP PNFGNTKTSL
     YPYESDNTML FPILILILFT LFVGFLGIPF NQDVDILSKW LTPSINLLHK NSNSSIDWYE
     FCKDAVFSVS IVSFGIFIAF FLYKPVYSSF QNLDLINLFV KMGPKRNFSD KVKNAIYDWS
     YNRGYLDAFY GTFLTAGMRK LAEFTHFFDR RIIDGIPNGV GLISFFVAEV IKSLGGGRIS
     SYLFFYFFYV SIFLLIYYFL HL
//