NU5C_MANES
ID NU5C_MANES Reviewed; 752 AA.
AC B1NWJ6;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 41.
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 Manihot esculenta (Cassava) (Jatropha manihot).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TME3;
RX PubMed=18214421; DOI=10.1007/s00122-007-0706-y;
RA Daniell H., Wurdack K.J., Kanagaraj A., Lee S.-B., Saski C., Jansen R.K.;
RT "The complete nucleotide sequence of the cassava (Manihot esculenta)
RT chloroplast genome and the evolution of atpF in Malpighiales: RNA editing
RT and multiple losses of a group II intron.";
RL Theor. Appl. Genet. 116:723-737(2008).
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; EU117376; ABV66200.1; -; Genomic_DNA.
DR RefSeq; YP_001718483.1; NC_010433.1.
DR AlphaFoldDB; B1NWJ6; -.
DR SMR; B1NWJ6; -.
DR GeneID; 6000055; -.
DR KEGG; mesc:6000055; -.
DR OrthoDB; 526738at2759; -.
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..752
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000360948"
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 219..239
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 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 728..748
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 752 AA; 85345 MW; 96B62DCE502B8734 CRC64;
MEHIYQYSWI IPFVTLPVPM LIGAGLLLFP AATKKLRRMW AFPSVFLLSI VMIFSIDLSI
QQINSSFIYQ YIWSWTINND FSLEFGHLID PLTSILSVLI TTVGILVLFY SDNYMSHDQG
YLRFFAYMSF FTTSMLGLVT SSNLIQIYIF WELVGVCSYL LIGFWFTRPI ASNACQKAFV
TNRVGDFGLL LGILGLYWIT GSFEFRDLFK IFNNLIYNNQ VNFLFVTLCA VLLFSGAIAK
SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLVARL FPLFVIIPFI MNLIALIGII
TVFLGATLAL AQKDIKRSLA YSTMSQLGYM MLALGMGSYR AALFHLITHA YSKALLFLGS
GSIIHSMEAI LGYSPDKSQN MVLMGGLTKH IPITKTAFLL GTLSLCGIPP FACFWSKDEI
LNDSWLYSPI FAIIACFTAG LTAFYMFRVY LLTFDGHFNA HFQSYSGKKN SSFYSISLWG
KEGSKMLNKN LRLLALLTMN NKERASFFWK NTYQIDGNVR NMTWPFITIQ NFNTKRIFSY
PHESDNTMLF PMLILVLFTL FIGAIGIPFN QFNQEGMLLD IDILSKLLTP SLNLLHQNPE
NSVDWYEFVT NATFSASIAF FGIFIASFLY KPVYSSLQNL NFFNSFAKKG PKRILWDKII
NVIYNWSSNR GYIDAFYAIS FIGGIRKLAE LIHFFDKQII DGTPNGVGVT SFFVGEGIKN
VGSGRISFYL LFYLFYALIF LLIYYSVYKF II
