TPS5_ARATH
ID TPS5_ARATH Reviewed; 862 AA.
AC O23617; Q8GWQ1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 5;
DE EC=2.4.1.15;
DE AltName: Full=Trehalose-6-phosphate synthase 5;
DE Short=AtTPS5;
GN Name=TPS5; OrderedLocusNames=At4g17770; ORFNames=dl4920W, FCAALL.9;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11701378; DOI=10.1016/s1360-1385(01)02125-2;
RA Leyman B., Van Dijck P., Thevelein J.M.;
RT "An unexpected plethora of trehalose biosynthesis genes in Arabidopsis
RT thaliana.";
RL Trends Plant Sci. 6:510-513(2001).
RN [7]
RP INDUCTION BY SUCROSE.
RX PubMed=15181209; DOI=10.1104/pp.104.039503;
RA Schluepmann H., van Dijken A.J.H., Aghdasi M., Wobbes B., Paul M.,
RA Smeekens S.C.M.;
RT "Trehalose mediated growth inhibition of Arabidopsis seedlings is due to
RT trehalose-6-phosphate accumulation.";
RL Plant Physiol. 135:879-890(2004).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=15181208; DOI=10.1104/pp.104.039743;
RA van Dijken A.J.H., Schluepmann H., Smeekens S.C.M.;
RT "Arabidopsis trehalose-6-phosphate synthase 1 is essential for normal
RT vegetative growth and transition to flowering.";
RL Plant Physiol. 135:969-977(2004).
RN [9]
RP PHOSPHORYLATION AT SER-5 AND THR-32, MUTAGENESIS OF SER-5 AND THR-32,
RP INTERACTION WITH GRF/14-3-3, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16771775; DOI=10.1111/j.1365-313x.2006.02780.x;
RA Harthill J.E., Meek S.E.M., Morrice N., Peggie M.W., Borch J., Wong B.H.C.,
RA Mackintosh C.;
RT "Phosphorylation and 14-3-3 binding of Arabidopsis trehalose-phosphate
RT synthase 5 in response to 2-deoxyglucose.";
RL Plant J. 47:211-223(2006).
RN [10]
RP INTERACTION WITH MBF1C, AND INDUCTION BY HEAT.
RX PubMed=18201973; DOI=10.1074/jbc.m709187200;
RA Suzuki N., Bajad S., Shuman J., Shulaev V., Mittler R.;
RT "The transcriptional co-activator MBF1c is a key regulator of
RT thermotolerance in Arabidopsis thaliana.";
RL J. Biol. Chem. 283:9269-9275(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-
CC trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15;
CC -!- SUBUNIT: Binds to the phosphopeptide-binding site of GRF/14-3-3 and to
CC MBF1c.
CC -!- TISSUE SPECIFICITY: Low expression in leaves, stems, flower buds,
CC flowers and siliques. {ECO:0000269|PubMed:15181208}.
CC -!- INDUCTION: 90-fold induction by sucrose after 24 hours and by heat
CC stress. {ECO:0000269|PubMed:15181209, ECO:0000269|PubMed:18201973}.
CC -!- PTM: Both Ser-5 and Thr-32 must be phosphorylated for binding to
CC GRF/14-3-3. {ECO:0000269|PubMed:16771775}.
CC -!- MISCELLANEOUS: 2-deoxyglucose, but not phenformin, enhances the
CC phosphorylation of TPS5.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 20 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the trehalose
CC phosphatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10557.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78780.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97344; CAB10557.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161547; CAB78780.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83948.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM68026.1; -; Genomic_DNA.
DR EMBL; BT005967; AAO64902.1; -; mRNA.
DR EMBL; AK118703; BAC43297.1; -; mRNA.
DR PIR; H71447; H71447.
DR RefSeq; NP_001329809.1; NM_001341241.1.
DR RefSeq; NP_567538.1; NM_117886.3.
DR AlphaFoldDB; O23617; -.
DR SMR; O23617; -.
DR BioGRID; 12791; 2.
DR STRING; 3702.AT4G17770.1; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR iPTMnet; O23617; -.
DR PaxDb; O23617; -.
DR PRIDE; O23617; -.
DR ProteomicsDB; 232502; -.
DR EnsemblPlants; AT4G17770.1; AT4G17770.1; AT4G17770.
DR EnsemblPlants; AT4G17770.2; AT4G17770.2; AT4G17770.
DR GeneID; 827498; -.
DR Gramene; AT4G17770.1; AT4G17770.1; AT4G17770.
DR Gramene; AT4G17770.2; AT4G17770.2; AT4G17770.
DR KEGG; ath:AT4G17770; -.
DR Araport; AT4G17770; -.
DR TAIR; locus:2129425; AT4G17770.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_3_1_1; -.
DR InParanoid; O23617; -.
DR OMA; YFVRTNQ; -.
DR OrthoDB; 772297at2759; -.
DR PhylomeDB; O23617; -.
DR BRENDA; 2.4.1.15; 399.
DR PRO; PR:O23617; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23617; baseline and differential.
DR Genevisible; O23617; AT.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005992; P:trehalose biosynthetic process; IBA:GO_Central.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IBA:GO_Central.
DR CDD; cd03788; GT20_TPS; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR003337; Trehalose_PPase.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR Pfam; PF02358; Trehalose_PPase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR TIGRFAMs; TIGR00685; T6PP; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..862
FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT forming] 5"
FT /id="PRO_0000324826"
FT REGION 60..546
FT /note="Glycosyltransferase"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16771775"
FT MOD_RES 32
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:16771775"
FT MUTAGEN 5
FT /note="S->A: Abolishes binding to GRF/14-3-3."
FT /evidence="ECO:0000269|PubMed:16771775"
FT MUTAGEN 32
FT /note="T->A: Abolishes binding to GRF/14-3-3."
FT /evidence="ECO:0000269|PubMed:16771775"
SQ SEQUENCE 862 AA; 97454 MW; ADA155DB26DCB470 CRC64;
MVSRSYSNLL DLASGNFHSF SREKKRFPRV ATVTGVLSEL DDDNNSNSVC SDAPSSVTQD
RIIIVGNQLP IKSHRNSAGK LSFSWDNDSL LLQLKDGMRE DMEVVYIGCL KEQIDTVEQD
DVSQRLLENF KCVPAYIPPE LFTKYYHGFC KQHLWPLFHY MLPLTPDLGG RFDRSLWQAY
LSVNKIFADK VMEVISPDDD FVWVHDYHLM VLPTFLRKRF NRVKLGFFLH SPFPSSEIYR
TLPVRNELLR ALLNADLIGF HTFDYARHFL SCCSRMLGLS YQSKRGTIGL EYYGRTVSIK
ILPVGIHISQ LQSILNLPET QTKVAELRDQ FLDQKVLLGV DDMDIFKGIS LKLLAMEQLL
TQHPEKRGRV VLVQIANPAR GRGKDVQEVQ SETEATVKRI NEMFGRPGYQ PVVLIDTPLQ
FFERIAYYVI AECCLVTAVR DGMNLIPYEY IICRQGNPKL NETIGLDPSA AKKSMLVVSE
FIGCSPSLSG AIRVNPWNID AVTEAMDYAL IVSEAEKQMR HEKHHKYVST HDVAYWARSF
IQDLERACGD HVRKRCWGIG FGLGFRVVAL DPSFKKLSIE HIVSAYKRTK NRAILLDYDG
TMVQPGSIRT TPTRETIEIL NNLSSDPKNI VYLVSGKDRR TLTEWFSSCD DLGLGAEHGY
FIRPNDGTDW ETSSLVSGFE WKQIAEPVMR LYTETTDGST IETKETALVW NYQFADPDFG
SCQAKELMEH LESVLTNDPV SVKTGQQLVE VKPQGVNKGL VAERLLTTMQ EKGKLLDFIL
CVGDDRSDED MFEVIMSAKD GPALSPVAEI FACTVGQKPS KAKYYLDDTA EIIRMLDGLA
ATNTTISDQT DSTATVPTKD LF
