NU3C_CUCSA
ID NU3C_CUCSA Reviewed; 120 AA.
AC Q4VZH0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 58.
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}; OrderedLocusNames=CsCp043;
OS Cucumis sativus (Cucumber).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Baekmibaekdadagi;
RX PubMed=16362300; DOI=10.1007/s00299-005-0097-y;
RA Kim J.-S., Jung J.D., Lee J.-A., Park H.-W., Oh K.-H., Jeong W.J.,
RA Choi D.-W., Liu J.R., Cho K.Y.;
RT "Complete sequence and organization of the cucumber (Cucumis sativus L. cv.
RT Baekmibaekdadagi) chloroplast genome.";
RL Plant Cell Rep. 25:334-340(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Borszczagowski;
RX PubMed=17607527; DOI=10.2478/s11658-007-0029-7;
RA Plader W.W., Yukawa Y., Sugiura M., Malepszy S.;
RT "The complete structure of the cucumber (Cucumis sativus L.) chloroplast
RT genome: its composition and comparative analysis.";
RL Cell. Mol. Biol. Lett. 12:584-594(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chipper, and cv. Gy14;
RX PubMed=17546086; DOI=10.1139/g07-003;
RA Chung S.-M., Gordon V.S., Staub J.E.;
RT "Sequencing cucumber (Cucumis sativus L.) chloroplast genomes identifies
RT differences between chilling-tolerant and -susceptible cucumber lines.";
RL Genome 50:215-225(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_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; DQ119058; AAZ94656.1; -; Genomic_DNA.
DR EMBL; AJ970307; CAJ00763.1; -; Genomic_DNA.
DR EMBL; DQ865975; ABI97422.1; -; Genomic_DNA.
DR EMBL; DQ865976; ABI98750.1; -; Genomic_DNA.
DR RefSeq; YP_247604.1; NC_007144.1.
DR AlphaFoldDB; Q4VZH0; -.
DR SMR; Q4VZH0; -.
DR GeneID; 3429255; -.
DR KEGG; csv:3429255; -.
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_0000362826"
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; 13881 MW; EFFA85DA20D06047 CRC64;
MFLLYEYDIF WVFLIISSVI PILAFLISGV LAPLSKEPEK LSSYESGIEP MGDAWVQFRI
RYYMFALVFV VFDVETVFLY PWAMSFDVLG VSVFIEALIF VLILIVGLVY AWRKGALEWS
