NU5C_LIGVU
ID NU5C_LIGVU Reviewed; 738 AA.
AC Q9TLA3;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 76.
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 Ligustrum vulgare (Common privet) (Ligustrum insulare).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Oleaceae; Oleeae; Ligustrum.
OX NCBI_TaxID=13597;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10877943; DOI=10.1006/mpev.1999.0769;
RA Olmstead R.G., Kim K.-J., Jansen R.K., Wagstaff S.J.;
RT "The phylogeny of the asteridae sensu lato based on chloroplast ndhF gene
RT sequences.";
RL Mol. Phylogenet. Evol. 16:96-112(2000).
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; AF130164; AAF08126.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9TLA3; -.
DR SMR; Q9TLA3; -.
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..738
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000118188"
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 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 546..566
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 603..623
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 718..738
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 738 AA; 83478 MW; CD78ECA8DCF1BCAF CRC64;
MEQTYQYAWI IPFVPLPVPM LIGVGLLLFP TATKNLRRMW AFPSILLLSI VMIFSINLSI
QQIDSSCIYQ YVWSWTINND FSLEFGYLID PLTSIMSMLI TTVGIMVLIY SDNYMAHDQG
YLRFFASMSF FSTSMLGLVT SSNLIQIYIF WELVGMCSYL LIGFWFTRPL AANACQKAFV
TNRVGDFGLL LGILGFYWIT GSFEFRDLFE ILNNFISKNE VNSSFGTLCA ALLFTGAVAK
SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLVARL LPLFIVIPYI MNFISFIGII
TVLLGATLAL AQKDIKRGLA YSTMSQLGYM MLALGMGSYR SALFHLITHA YSKALLFLGS
GSIIHSMETI VGYSPDKSQN MVLMGGLRKH VPITQISFLL GTLSLCGIPP LACFWSKDEI
LNDSWLYSPI FAIIAWSTAG LTAFYMFRIY LLTFEGHLNV HFQNYSGKQN TPFYSISLWG
KGDSKRINKN FRLLKMNNSK SSSFFSKKPY RSGKNVRNRV GPFLTIVHFE NQKSYSYPYE
SDNTMLFPLL VLGILTLFVG SLGIPFNQEL DILTKWLTPS INLLHQKWND SIDWYEFWKD
ASFSVSIAYF GIFIASFLYK PIYSSFPNFF LINLFVKTGP KRSLWDKILN GLYNWSYNRA
YIDAFYTTSL TGAVRGLAQV THFFDRRVID GITNGVGVMS FFVGEGIKYV GGGRISSYLF
FYLSCVSIFL LGLYFPVF
