NU3C_ACOCL
ID NU3C_ACOCL Reviewed; 120 AA.
AC Q3V529;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 3, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01394};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01394};
DE AltName: Full=NAD(P)H dehydrogenase subunit 3 {ECO:0000255|HAMAP-Rule:MF_01394};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 3 {ECO:0000255|HAMAP-Rule:MF_01394};
GN Name=ndhC {ECO:0000255|HAMAP-Rule:MF_01394};
OS Acorus calamus (Sweet flag).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Acoraceae; Acorus.
OX NCBI_TaxID=4465;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15930156; DOI=10.1093/molbev/msi173;
RA Goremykin V.V., Holland B., Hirsch-Ernst K.I., Hellwig F.H.;
RT "Analysis of Acorus calamus chloroplast genome and its phylogenetic
RT implications.";
RL Mol. Biol. Evol. 22:1813-1822(2005).
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_01394}.
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_01394};
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_01394};
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_01394}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01394}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01394}.
CC -!- SIMILARITY: Belongs to the complex I subunit 3 family.
CC {ECO:0000255|HAMAP-Rule:MF_01394}.
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DR EMBL; AJ879453; CAI53799.1; -; Genomic_DNA.
DR RefSeq; YP_319770.1; NC_007407.1.
DR AlphaFoldDB; Q3V529; -.
DR SMR; Q3V529; -.
DR GeneID; 3677389; -.
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:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.58.1610; -; 1.
DR HAMAP; MF_01394; NDH1_NuoA; 1.
DR InterPro; IPR023043; NAD(P)H_OxRDtase_bac/plastid.
DR InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3.
DR InterPro; IPR038430; NDAH_ubi_oxred_su3_sf.
DR PANTHER; PTHR11058; PTHR11058; 1.
DR Pfam; PF00507; Oxidored_q4; 1.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW Thylakoid; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..120
FT /note="NAD(P)H-quinone oxidoreductase subunit 3,
FT chloroplastic"
FT /id="PRO_0000362802"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
SQ SEQUENCE 120 AA; 13768 MW; 142CD25FFE0E9A93 CRC64;
MFLLHEYDIF WAFLLISSVI PILAFLISGV LAPTREGPEK LSSYESGIEP IGDAWVQFRI
RYYMFALVFV VFDVETVFLY PWAMSFDVLG VSVFLEALIF VLILIVGSVY AWRKGALEWS