NU5C_CYCTA
ID NU5C_CYCTA Reviewed; 739 AA.
AC A6H5N8;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 44.
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 Cycas taitungensis (Prince sago) (Cycas taiwaniana).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Cycadidae; Cycadales; Cycadaceae; Cycas.
OX NCBI_TaxID=54799;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17383970; DOI=10.1093/molbev/msm059;
RA Wu C.-S., Wang Y.-N., Liu S.-M., Chaw S.-M.;
RT "Chloroplast genome (cpDNA) of Cycas taitungensis and 56 cp protein-coding
RT genes of Gnetum parvifolium: insights into cpDNA evolution and phylogeny of
RT extant seed plants.";
RL Mol. Biol. Evol. 24:1366-1379(2007).
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; AP009339; BAF65004.1; -; Genomic_DNA.
DR RefSeq; YP_001312262.1; NC_009618.1.
DR AlphaFoldDB; A6H5N8; -.
DR SMR; A6H5N8; -.
DR GeneID; 5309604; -.
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..739
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000360929"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..344
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 547..567
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 739 AA; 82438 MW; 6FC8A1F3E573A2EA CRC64;
MELIYKYVWI VPFLPLSASV PIGSGSLLFP RATRGLHHIW ALISISLLGI AMLLSFNLFL
QQITGGPVYQ YLWSWTINKN FSPELGYLID PLTSIMPISV TTVGIMVMIY SDNYMSHDQG
YVRFFAYLSL FNASMLGLVI SPNLVQIYIF WELVGMCSYL LIGSWFTRPS AANACQKAFI
TNRIGDFGLL LGILGFYQIT GSFKFRYLLG RSNESIASNE VSSFFATLCA FLLFLGPVAK
SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLVARL FPLFKALPFI MNLISWTGGI
TALLGATMAL AQSDLKRGLA YSTMSQSGYM VLALGTGSYR AALFHPITHA YSKALLFLGS
GSVIHSMESL VGYCPAESQN MALMGGLSKY MPITGTTFLL GTLSLCGIPP FACFWSKDEI
ISDSWLYSTI LGGIARSAAG FTAFYMSRMY FLAFEGDLRV NLYNDPIPFY SISMWGEKES
GTFTETEMGS MPQLPGNKNS SSSEGVFQFS GKMEQFDGKP MEYLVITHPL DKGDPPYPKE
SDNTMLLPSL VLGLFTLFVG SIGVSFVQGE ISSDILSQRL TLSMNHFHEN HPENWSEFFV
DAIPSVGIAF SSTFVAFVLY GPINFNFSSP YLWYKRDSRL KGIPDRFINV IYNWSYYRGY
IDIYYNKIFT MGIRRLAELT YLFDRWVIDG IIDRVGILGL FVGEGMKYLG GGRTSSYLFG
FLFFAVIFLL TIFIFIWIR
