PNSB2_ARATH
ID PNSB2_ARATH Reviewed; 348 AA.
AC Q94AQ8; Q9XIR6;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Photosynthetic NDH subunit of subcomplex B 2, chloroplastic {ECO:0000303|PubMed:21785130};
DE Short=Protein PnsB2 {ECO:0000303|PubMed:21785130};
DE AltName: Full=NAD(P)H DEHYDROGENASE SUBUNIT 45 {ECO:0000303|PubMed:18974055};
DE AltName: Full=NDH-DEPENDENT CYCLIC ELECTRON FLOW 2 {ECO:0000303|PubMed:18785996};
DE Flags: Precursor;
GN Name=PNSB2 {ECO:0000303|PubMed:21785130};
GN Synonyms=NDF2 {ECO:0000303|PubMed:18785996},
GN NDH45 {ECO:0000303|PubMed:18974055};
GN OrderedLocusNames=At1g64770 {ECO:0000312|Araport:AT1G64770};
GN ORFNames=F13O11.8 {ECO:0000312|EMBL:AAD38252.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP COMPONENT OF THE NDH COMPLEX, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18974055; DOI=10.1074/jbc.m805404200;
RA Sirpio S., Allahverdiyeva Y., Holmstrom M., Khrouchtchova A., Haldrup A.,
RA Battchikova N., Aro E.M.;
RT "Novel nuclear-encoded subunits of the chloroplast NAD(P)H dehydrogenase
RT complex.";
RL J. Biol. Chem. 284:905-912(2009).
RN [6]
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 [7]
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 [8]
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 [9]
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:18974055,
CC ECO:0000269|PubMed:21785130}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:18785996, ECO:0000269|PubMed:18974055}; Peripheral
CC membrane protein {ECO:0000269|PubMed:18974055}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q94AQ8-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Malfunction of the NDH complex (PubMed:18974055,
CC PubMed:18785996). H(2)O(2) accumulation in Dark-Light transition
CC (PubMed:18974055). {ECO:0000269|PubMed:18785996,
CC ECO:0000269|PubMed:18974055}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD38252.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006193; AAD38252.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34285.1; -; Genomic_DNA.
DR EMBL; AY045871; AAK76545.1; -; mRNA.
DR EMBL; AY113953; AAM45001.1; -; mRNA.
DR EMBL; AY085928; AAM63140.1; -; mRNA.
DR PIR; H96670; H96670.
DR RefSeq; NP_564840.1; NM_105151.4. [Q94AQ8-1]
DR PDB; 7WFF; EM; 3.59 A; b=1-348.
DR PDB; 7WG5; EM; 3.89 A; b=1-348.
DR PDBsum; 7WFF; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; Q94AQ8; -.
DR SMR; Q94AQ8; -.
DR STRING; 3702.AT1G64770.3; -.
DR PaxDb; Q94AQ8; -.
DR PRIDE; Q94AQ8; -.
DR ProteomicsDB; 226159; -. [Q94AQ8-1]
DR EnsemblPlants; AT1G64770.1; AT1G64770.1; AT1G64770. [Q94AQ8-1]
DR GeneID; 842785; -.
DR Gramene; AT1G64770.1; AT1G64770.1; AT1G64770. [Q94AQ8-1]
DR KEGG; ath:AT1G64770; -.
DR Araport; AT1G64770; -.
DR eggNOG; ENOG502QWGY; Eukaryota.
DR HOGENOM; CLU_048345_0_1_1; -.
DR OMA; SCTYCTH; -.
DR PhylomeDB; Q94AQ8; -.
DR PRO; PR:Q94AQ8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94AQ8; baseline and differential.
DR Genevisible; Q94AQ8; AT.
DR GO; GO:0009534; C:chloroplast thylakoid; IDA:UniProtKB.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010598; C:NAD(P)H dehydrogenase complex (plastoquinone); IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0047938; F:glucose-6-phosphate 1-epimerase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009773; P:photosynthetic electron transport in photosystem I; IMP:UniProtKB.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR014718; GH-type_carb-bd.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chloroplast; Membrane; Plastid;
KW Reference proteome; Thylakoid; Transit peptide; Transport.
FT TRANSIT 1..17
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 18..348
FT /note="Photosynthetic NDH subunit of subcomplex B 2,
FT chloroplastic"
FT /id="PRO_0000431820"
SQ SEQUENCE 348 AA; 38006 MW; EC289B8B358030CA CRC64;
MASLISFSLL PKPKAVRSSI SAPQTQTINT EKLEDKFGRK GIKFSESNNI PMVELKVRNG
SSLKLSLSDA HVLSYKPKVY WKDEGFEEVL YTVDGDESRG GVGVVIVNGE EPKGGSSVIS
GCDWSVKDTD SDAIDALQIE LSCTAGVLDI TYIVSLYPVS MATALVVKNN GRKPVTLKPG
IMSYLRFKKR SGAGIQGLKG CSYCPNPPLS SPFELLSPSE AMKAESSGWF GSEEGEKPGI
WAVEDSVITL LEKKMSRIYG APPAERLKAV YNTPPSKFET IDQGRGLFFR MIRIGFEEMY
VGSPGSMWDK YGKQHYFVCT GPTSMLVPVD VASGETWRGA MVIEHDNL
