NU4LC_CHLAT
ID NU4LC_CHLAT Reviewed; 101 AA.
AC Q19V55;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 4L, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01456};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01456};
DE AltName: Full=NAD(P)H dehydrogenase subunit 4L {ECO:0000255|HAMAP-Rule:MF_01456};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 4L {ECO:0000255|HAMAP-Rule:MF_01456};
GN Name=ndhE {ECO:0000255|HAMAP-Rule:MF_01456};
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.
CC {ECO:0000255|HAMAP-Rule:MF_01456}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01456};
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01456};
CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC are encoded in the nucleus. {ECO:0000255|HAMAP-Rule:MF_01456}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01456}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01456}.
CC -!- SIMILARITY: Belongs to the complex I subunit 4L family.
CC {ECO:0000255|HAMAP-Rule:MF_01456}.
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DR EMBL; DQ422812; ABD62193.2; -; Genomic_DNA.
DR RefSeq; YP_001019165.1; NC_008822.1.
DR AlphaFoldDB; Q19V55; -.
DR SMR; Q19V55; -.
DR GeneID; 4783210; -.
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:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01456; NDH1_NuoK; 1.
DR InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K.
DR InterPro; IPR039428; NUOK/Mnh_C1-like.
DR PANTHER; PTHR11434; PTHR11434; 1.
DR Pfam; PF00420; Oxidored_q2; 1.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW Thylakoid; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..101
FT /note="NAD(P)H-quinone oxidoreductase subunit 4L,
FT chloroplastic"
FT /id="PRO_0000360316"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
SQ SEQUENCE 101 AA; 11089 MW; CA18A1B7CE49BC26 CRC64;
MILDSLLILA ASVFCIGIYG LITSRNVVRI LMSLELLLNA VNINFVAFSN FIDSIEIKGQ
VISIFIMTIA AAEAAVGLAL ILAIYRNRDT VDIESFNLLK R