NU5C_TECST
ID NU5C_TECST Reviewed; 750 AA.
AC Q9TLC2;
DT 02-NOV-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 Tecoma stans (Yellow bells) (Stenolobium stans).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Bignoniaceae; Tecomeae; Tecoma.
OX NCBI_TaxID=69904;
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; AF130145; AAF08107.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9TLC2; -.
DR SMR; Q9TLC2; -.
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..750
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000118205"
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 283..303
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 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 607..627
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..744
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 750 AA; 85201 MW; D83CFB6C73F4B648 CRC64;
MEQTYQYAWI IPFLPLPVPM LIGVGLLLFP TATKNLRRMW AFTSILLLSI VMIFATNLSI
QQINTSSIYQ YVWSWTLDND FSLEFGYLID PLTSIMSMLI TTVGIMVLIY SDNYMAHDQG
YLRFFAYMSF FSTSMFGLVT SSNLIQIYIF WELVGMCSYL LIGFWFTRPP AANACQKAFV
TNRVGDFGLL LGILGFYWIT GSFEFRDLFQ IFNNLISNNE VNSPFVTLCA ALLFAGAVAK
SAQFPLHIWL PDAMEGPTPI SALIHAATMV AAGIFLVARL LTLFIVIPYI LNIISLIGLI
TVLLGATLAL AQKDIKRGLA YSTMSQLGYM ILALGIGSYR SALFHLITHA YSKALLFLGS
GSVIHSMETI VGYSPDKSQN MVLMGGLTKH VPITKTSFLL GTLSLSGIPP LACFWSKDEI
LNDSWLYSPI FAIIAWATAG LTAFYMFRIY LLTFEGHLNC HFQNYSGSQN TSLYSISLWG
STCSQRINKN FHLLRMNNNE SSSFFSKKTY RSDQTLRKTN RGRPFINIVH FDTKKPFSYP
YESDNTMLFP LLVLVLFTLF VGSIGIPFNQ EGTDLDILSK WLAPSINLLH QKSKDSTDWY
EFLKDAIFSV SIAYFGIFLA SFLYKPIYSS LKNFDFINFF VKTGPKRYRW DKILTVLYDW
SYNRAYIDPF YTTCFTGAIR GLAQLTYFFD RRVIDGITNG VGIMSFFLGE GIKYASGGRI
SSYLFFYFCC VSIFLVIYYK FYLFSLYIPF
