NDHU_ARATH
ID NDHU_ARATH Reviewed; 218 AA.
AC Q84VQ4; Q63Z93;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit U, chloroplastic {ECO:0000305};
DE EC=7.1.1.- {ECO:0000305};
DE AltName: Full=NAD(P)H dehydrogenase subunit U {ECO:0000303|PubMed:21785130};
DE Short=NDH subunit U {ECO:0000305};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit U {ECO:0000305};
DE AltName: Full=Protein CHLORORESPIRATORY REDUCTION L {ECO:0000303|PubMed:21505067};
DE Flags: Precursor;
GN Name=ndhU {ECO:0000303|PubMed:21785130};
GN Synonyms=CRRL {ECO:0000303|PubMed:21505067};
GN OrderedLocusNames=At5g21430 {ECO:0000312|Araport:AT5G21430};
GN ORFNames=F13M11.2 {ECO:0000312|EMBL:AAO73883.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP COMPONENT OF THE NDH COMPLEX, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21505067; DOI=10.1105/tpc.110.080291;
RA Yamamoto H., Peng L., Fukao Y., Shikanai T.;
RT "An Src homology 3 domain-like fold protein forms a ferredoxin binding site
RT for the chloroplast NADH dehydrogenase-like complex in Arabidopsis.";
RL Plant Cell 23:1480-1493(2011).
RN [6]
RP NOMENCLATURE, AND COMPONENT OF THE NDH COMPLEX.
RX PubMed=21785130; DOI=10.1093/pcp/pcr098;
RA Ifuku K., Endo T., Shikanai T., Aro E.M.;
RT "Structure of the chloroplast NADH dehydrogenase-like complex: nomenclature
RT for nuclear-encoded subunits.";
RL Plant Cell Physiol. 52:1560-1568(2011).
RN [7]
RP COMPONENT OF THE NDH COMPLEX, AND SUBUNIT.
RX PubMed=24225949; DOI=10.1074/jbc.m113.511584;
RA Yamamoto H., Shikanai T.;
RT "In planta mutagenesis of Src homology 3 domain-like fold of NdhS, a
RT ferredoxin-binding subunit of the chloroplast NADH dehydrogenase-like
RT complex in Arabidopsis: a conserved Arg-193 plays a critical role in
RT ferredoxin binding.";
RL J. Biol. Chem. 288:36328-36337(2013).
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. {ECO:0000305}.
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:0000305};
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:0000305};
CC -!- SUBUNIT: Part of the chloroplast NDH complex, composed of a mixture of
CC chloroplast and nucleus encoded subunits (PubMed:21785130). Component
CC of the electron donor-binding subcomplex, at least composed of NDHS,
CC NDHT and NDHU (PubMed:21505067, PubMed:24225949).
CC {ECO:0000269|PubMed:21505067, ECO:0000269|PubMed:21785130,
CC ECO:0000269|PubMed:24225949}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:21505067}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q84VQ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84VQ4-2; Sequence=VSP_057442;
CC -!- DISRUPTION PHENOTYPE: Malfunction of the NDH complex.
CC {ECO:0000269|PubMed:21505067}.
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DR EMBL; AC140977; AAO73883.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92949.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92950.1; -; Genomic_DNA.
DR EMBL; AY091157; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT015681; AAU15180.1; -; mRNA.
DR RefSeq; NP_001031919.1; NM_001036842.1. [Q84VQ4-2]
DR RefSeq; NP_850862.1; NM_180531.4. [Q84VQ4-1]
DR AlphaFoldDB; Q84VQ4; -.
DR SMR; Q84VQ4; -.
DR STRING; 3702.AT5G21430.1; -.
DR PaxDb; Q84VQ4; -.
DR PRIDE; Q84VQ4; -.
DR ProteomicsDB; 251168; -. [Q84VQ4-1]
DR EnsemblPlants; AT5G21430.1; AT5G21430.1; AT5G21430. [Q84VQ4-1]
DR EnsemblPlants; AT5G21430.2; AT5G21430.2; AT5G21430. [Q84VQ4-2]
DR GeneID; 832247; -.
DR Gramene; AT5G21430.1; AT5G21430.1; AT5G21430. [Q84VQ4-1]
DR Gramene; AT5G21430.2; AT5G21430.2; AT5G21430. [Q84VQ4-2]
DR KEGG; ath:AT5G21430; -.
DR Araport; AT5G21430; -.
DR TAIR; locus:1005716171; AT5G21430.
DR eggNOG; ENOG502RXG6; Eukaryota.
DR HOGENOM; CLU_103116_0_0_1; -.
DR InParanoid; Q84VQ4; -.
DR OMA; CSYAEVP; -.
DR PhylomeDB; Q84VQ4; -.
DR PRO; PR:Q84VQ4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84VQ4; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IMP:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0010598; C:NAD(P)H dehydrogenase complex (plastoquinone); IMP:UniProtKB.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR044199; NdhU_chloroplastic.
DR PANTHER; PTHR47726; PTHR47726; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Membrane; NAD; NADP; Plastid;
KW Plastoquinone; Quinone; Reference proteome; Thylakoid; Transit peptide;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 54..218
FT /note="NAD(P)H-quinone oxidoreductase subunit U,
FT chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431817"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 95..159
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 47..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 141
FT /note="Missing (in isoform 2)"
FT /id="VSP_057442"
SQ SEQUENCE 218 AA; 24438 MW; FA29630525BC222B CRC64;
MASLSTITQP SLVHIPGESV LHHVPSTCSF PWKPTINTKR IICSPARNSS EVSAEAETEG
GSSTAVDEAP KESPSLISAL NVERALRGLP ITDVDHYGRL GIFRNCSYDQ VTIGYKERVK
ELKEQGLDEE QLKTKMDLIK ESYTILSTVE ERRMYDWSLA RSEKAERYVW PFEVDIMEPS
REEPPPQEPE DVGPTRILGY FIGAWLVLGV ALSVAFNR
