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Database: UniProt
Entry: A0A251U366_HELAN
LinkDB: A0A251U366_HELAN
Original site: A0A251U366_HELAN 
ID   A0A251U366_HELAN        Unreviewed;       459 AA.
AC   A0A251U366;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic {ECO:0000256|ARBA:ARBA00018648};
DE   AltName: Full=NAD(P)H dehydrogenase subunit 5 {ECO:0000256|ARBA:ARBA00031649};
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit 5 {ECO:0000256|ARBA:ARBA00029876};
GN   ORFNames=HannXRQ_Chr08g0212841 {ECO:0000313|EMBL:OTG17499.1};
OS   Helianthus annuus (Common sunflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG17499.1, ECO:0000313|Proteomes:UP000215914};
RN   [1] {ECO:0000313|Proteomes:UP000215914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RX   PubMed=28538728; DOI=10.1038/nature22380;
RA   Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA   Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA   Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA   Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA   Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA   Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA   Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA   Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA   Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA   Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA   Vincourt P., Rieseberg L.H., Langlade N.B.;
RT   "The sunflower genome provides insights into oil metabolism, flowering and
RT   Asterid evolution.";
RL   Nature 546:148-152(2017).
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}.
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; CM007897; OTG17499.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A251U366; -.
DR   STRING; 4232.A0A251U366; -.
DR   InParanoid; A0A251U366; -.
DR   OMA; KIHERIR; -.
DR   Proteomes; UP000215914; Chromosome 8.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR   InterPro; IPR002128; NADH_UbQ_OxRdtase_chlpt_su5_C.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   InterPro; IPR003945; NU5C-like.
DR   InterPro; IPR001516; Proton_antipo_N.
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; 2.
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};
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:ARBA00022528};
KW   Plastoquinone {ECO:0000256|ARBA:ARBA00022957};
KW   Quinone {ECO:0000256|ARBA:ARBA00022719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215914};
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        92..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        131..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        170..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        204..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        245..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        279..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        348..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        381..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          75..115
FT                   /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00662"
FT   DOMAIN          124..268
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
FT   DOMAIN          271..393
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
FT   DOMAIN          401..455
FT                   /note="NADH:ubiquinone/plastoquinone oxidoreductase
FT                   chloroplast chain 5 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01010"
SQ   SEQUENCE   459 AA;  51625 MW;  E04708BF2EDB1898 CRC64;
     MEQTYQYAWI IPFLPLPVPM LIGLGHLLFP TATKSLRRMW AFQSVLLLSI VMIFSLNLSI
     QQINSSSVYQ YVWSWIINND FSLEFGYLID PLTSIMSILI TTVGIMVLIY SDNYITSMLG
     LVTSSNLIQI YIFWELVGMC SYLLIGFWFT RPVAAKACQK AFVTNRVGDF GLLLGILGFY
     WIMGSFEFRD LFQIFNNLIS NNEVNSVFVT LCVVLLFAGA IAKSAQFPLH VWLPDAMEGP
     TPISALIHAA TMVAVGIFLV ARLMPLFIRG FAYSTMSQLG YMMLALGMGS YRSALFHLIT
     HAYSKALLLL GSGSVIHSME TLVGYCPKKS QNMVLMGGLK KHVPITKNSF LLGRLSLCGI
     PPLACFWSKD EILNNSWLYS PIFAIIAWST AGFTAFYMCW IYLLTFEGHL NVHFQNYSGK
     RNTPLYSISL WGKEGSKISN KNLNFCLKSD PNLSFYSAF
//
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