NU5C_CHLAT
ID NU5C_CHLAT Reviewed; 655 AA.
AC Q19V60;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 25-MAY-2022, entry version 51.
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 Chlorokybus atmophyticus (Soil alga).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Chlorokybophyceae; Chlorokybales;
OC Chlorokybaceae; Chlorokybus.
OX NCBI_TaxID=3144;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 48.80;
RX PubMed=17222354; DOI=10.1186/1741-7007-5-2;
RA Lemieux C., Otis C., Turmel M.;
RT "A clade uniting the green algae Mesostigma viride and Chlorokybus
RT atmophyticus represents the deepest branch of the Streptophyta in
RT chloroplast genome-based phylogenies.";
RL BMC Biol. 5:2-2(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; DQ422812; ABD62194.2; -; Genomic_DNA.
DR RefSeq; YP_001019159.1; NC_008822.1.
DR AlphaFoldDB; Q19V60; -.
DR SMR; Q19V60; -.
DR GeneID; 4783326; -.
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..655
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000360922"
FT TRANSMEM 7..27
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 124..144
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 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 635..655
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 655 AA; 73344 MW; B430D5FD0F70DA47 CRC64;
MEFIYRYAWL IPILPFLGSM IIGLGLISLR RATQTLRWRF AFFNIVLLGI ALIFSISILI
SQLNGHPPYK WLIEWIVTNQ FSLEIGYSID PLTSVMLVLV TSVAILVMIY SDSYMSYDQG
YVRFFAYLSL FTASMLGLVL SPNLVQIYVF WELVGMCSYL LIGFWFTRPA AADACQKAFV
TNRVGDFGLF LGILGLYWVT GSFEFQTISN RLSNVLLGDF VLPGSHPVQV ELLVLFNLLV
FLGPMAKSAQ FPLHVWLPDA MEGPTPISAL IHAATMVAAG VFLVARMFPI FNQFPIVMGF
IAWIGAITAI IAAIIAVTQN DLKKGLAYST ISQLGYMIMA MGVGSYTAGL FHLITHAYSK
ALLFLGSGSV IHGMEPVVGF NPSKNQNMLF MGKMREFMPV TAITFLLGTL SLCGIPPMAC
FWSKDEILSQ TFQAQPILWI IAWVTAGLTS FYMFRMYFLV FEGKQFRGGE FIYDVRAKSL
PKESNKKILI PLIILALVTT LVGFVGTPFN NMFAKFINLT RLEEHPFEWN EFLSMSGSSV
GIALIGLTLA SLIYKESKID ANQIANTLTP LYKLSFNKFY IDHIYQIGFI KVNRSLAQKA
LELDQQIIDG FINFTGFFTI MTGEILKYVE NGRVQSYVFV IIFATLIFVL ASQGF
