PNSB3_ARATH
ID PNSB3_ARATH Reviewed; 204 AA.
AC Q9LU21;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Photosynthetic NDH subunit of subcomplex B 3, chloroplastic {ECO:0000303|PubMed:21785130};
DE Short=Protein PnsB3 {ECO:0000303|PubMed:21785130};
DE AltName: Full=NDH-DEPENDENT CYCLIC ELECTRON FLOW 4 {ECO:0000303|PubMed:18785996};
DE Flags: Precursor;
GN Name=PNSB3 {ECO:0000303|PubMed:21785130};
GN Synonyms=NDF4 {ECO:0000303|PubMed:18785996};
GN OrderedLocusNames=At3g16250 {ECO:0000312|Araport:AT3G16250};
GN ORFNames=MYA6.6 {ECO:0000312|EMBL:BAB01265.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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].
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 REVIEW.
RX PubMed=19995722; DOI=10.1093/mp/ssp052;
RA Suorsa M., Sirpioe S., Aro E.M.;
RT "Towards characterization of the chloroplast NAD(P)H dehydrogenase
RT complex.";
RL Mol. Plant 2:1127-1140(2009).
RN [5]
RP COMPONENT OF THE NDH COMPLEX, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18785996; DOI=10.1111/j.1365-313x.2008.03680.x;
RA Takabayashi A., Ishikawa N., Obayashi T., Ishida S., Obokata J., Endo T.,
RA Sato F.;
RT "Three novel subunits of Arabidopsis chloroplastic NAD(P)H dehydrogenase
RT identified by bioinformatic and reverse genetic approaches.";
RL Plant J. 57:207-219(2009).
RN [6]
RP REVIEW.
RX PubMed=21029720; DOI=10.1016/j.bbabio.2010.10.015;
RA Peng L., Yamamoto H., Shikanai T.;
RT "Structure and biogenesis of the chloroplast NAD(P)H dehydrogenase
RT complex.";
RL Biochim. Biophys. Acta 1807:945-953(2011).
RN [7]
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).
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 -!- SUBUNIT: Part of the chloroplast NDH complex, composed of a mixture of
CC chloroplast and nucleus encoded subunits. Component of the NDH
CC subcomplex B, at least composed of PnsB1, PnsB2, PnsB3, PnsB4 and
CC PnsB5. {ECO:0000269|PubMed:18785996, ECO:0000269|PubMed:21785130}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:18785996}.
CC -!- DISRUPTION PHENOTYPE: Malfunction of the NDH complex.
CC {ECO:0000269|PubMed:18785996}.
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DR EMBL; AB023046; BAB01265.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75790.1; -; Genomic_DNA.
DR EMBL; AY042867; AAK68807.1; -; mRNA.
DR EMBL; BT006260; AAP13368.1; -; mRNA.
DR RefSeq; NP_188246.1; NM_112496.3.
DR PDB; 7WFF; EM; 3.59 A; c=1-204.
DR PDB; 7WG5; EM; 3.89 A; c=1-204.
DR PDBsum; 7WFF; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; Q9LU21; -.
DR SMR; Q9LU21; -.
DR IntAct; Q9LU21; 9.
DR STRING; 3702.AT3G16250.1; -.
DR TCDB; 3.D.1.8.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; Q9LU21; -.
DR PRIDE; Q9LU21; -.
DR ProteomicsDB; 226195; -.
DR EnsemblPlants; AT3G16250.1; AT3G16250.1; AT3G16250.
DR GeneID; 820871; -.
DR Gramene; AT3G16250.1; AT3G16250.1; AT3G16250.
DR KEGG; ath:AT3G16250; -.
DR Araport; AT3G16250; -.
DR TAIR; locus:2094882; AT3G16250.
DR eggNOG; ENOG502S4WU; Eukaryota.
DR HOGENOM; CLU_082632_10_0_1; -.
DR InParanoid; Q9LU21; -.
DR OMA; HEWNIPK; -.
DR OrthoDB; 1569985at2759; -.
DR PhylomeDB; Q9LU21; -.
DR PRO; PR:Q9LU21; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LU21; baseline and differential.
DR Genevisible; Q9LU21; AT.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0010598; C:NAD(P)H dehydrogenase complex (plastoquinone); IDA:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IBA:GO_Central.
DR GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR GO; GO:0009773; P:photosynthetic electron transport in photosystem I; IMP:TAIR.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR001055; Adrenodoxin.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR23426; PTHR23426; 1.
DR Pfam; PF00111; Fer2; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Chloroplast; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Plastid; Reference proteome; Thylakoid; Transit peptide;
KW Transport.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..204
FT /note="Photosynthetic NDH subunit of subcomplex B 3,
FT chloroplastic"
FT /id="PRO_0000431821"
FT DOMAIN 76..180
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 120
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 126
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 129
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 162
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 204 AA; 22418 MW; 393C457756AF1B02 CRC64;
MGSVQLSGSG LVASLPPNHS FSHKTKLNKP NSYFFRSKHN AARTKTVRAI STAPASQPPA
ADEPDEPPAV DFAFVHSVLL PDGTPDVHWR RANGGQKLRD IMLDSNIELY GPYSKPLSNC
AGVGTCATCM VEIVNGKELL NPRTDIEKEK LKRKPKNWRL ACQTNVGNPD STGLVVIQQL
PEWKAHEWNI PKNIPNDDDL ETST
