NU5C_HUPLU
ID NU5C_HUPLU Reviewed; 734 AA.
AC Q5SCZ9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic;
DE EC=7.1.1.-;
DE AltName: Full=NAD(P)H dehydrogenase subunit 5;
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 5;
GN Name=ndhF;
OS Huperzia lucidula (Shining clubmoss) (Lycopodium lucidulum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Lycopodiales; Lycopodiaceae; Huperzioideae; Huperzia.
OX NCBI_TaxID=37429;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15788152; DOI=10.1016/j.gene.2005.01.018;
RA Wolf P.G., Karol K.G., Mandoli D.F., Kuehl J.V., Arumuganathan K.,
RA Ellis M.W., Mishler B.D., Kelch D.G., Olmstead R.G., Boore J.L.;
RT "The first complete chloroplast genome sequence of a lycophyte, Huperzia
RT lucidula (Lycopodiaceae).";
RL Gene 350:117-128(2005).
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 (By similarity).
CC {ECO:0000250}.
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 -!- 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 -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC are encoded in the nucleus. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR EMBL; AY660566; AAT80767.1; -; Genomic_DNA.
DR RefSeq; YP_209571.1; NC_006861.1.
DR AlphaFoldDB; Q5SCZ9; -.
DR SMR; Q5SCZ9; -.
DR GeneID; 3283728; -.
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; IPR018393; NADHpl_OxRdtase_5_subgr.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
DR PANTHER; PTHR42829; PTHR42829; 1.
DR Pfam; PF01010; Proton_antipo_C; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR TIGRFAMs; TIGR01974; NDH_I_L; 1.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW Thylakoid; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..734
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000360939"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..559
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 601..621
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 707..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 512..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 734 AA; 81374 MW; F74FA8F12A34416C CRC64;
MESIYKYGWI IPLLPLVSSI TIGLGLFFFP KATKSLRRTY AIISTLLLSI AMFISFDLLW
QQIAGSPTYR YLWSWIPDQD VTLEVGYPID PLTSIMLVLV TTIGVTVMIH SDSYMSHDQG
YVRFFAYLSL STASMLGLVI SPNLIQIYIF RELVGMCSYL LIGFWFTRPS AANACQKAFI
TNRVGDFGLL LGTSGFYWIT GSFKFEDLFE RFNESLANHE VSLFLATPCA LLFPLGPVAK
SAQFPLHVWL PDAMEGPTPI SAPIHAATMV AAGIFLVARM FPLFQTLPLV MSSISWVGGV
TASLGATVAL AQKDLKRVLA YSTMSQLGYM MLALGIGSYR AASFHLITHA YPKALSSPGS
GSVIHSMEPI VGYCPDKSQN IALMGGLRKY VPITGTTFLL GTLSLCGIPP LACFWSKDEI
IADSWLYFPI LGWIARFTAG LTGFYTFRMY SLTLEGDFRA NPSKNLISSY VSPWENSRFG
TSSQKQTDSA LPLAQNRIES FDPSENIQEF SDKNVKNSVS TQSSREEYSP HPKESDNTML
FPLLILTIPT LLVGFIGVPS YQEEMGPDLL SHWLDPSLSL SNQINYENWL LEFIANATVS
VGTASLGIFT ASILYGPIPF FPRDLRQKTD LQLEGILGHF SSLLYNWSYS RGYIDGYYNI
VFIKGTRILA KIISFFDQWI IDGIVNGVGI SGSFGGEGSR YGEGGRISYY LFGFISGTII
LLLVVINYKH DFFP
