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 27-MAR-2024, entry version 136. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 IntAct; O23617; 18. DR STRING; 3702.O23617; -. DR CAZy; GT20; Glycosyltransferase Family 20. DR iPTMnet; O23617; -. DR PaxDb; 3702-AT4G17770-1; -. 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; AT4G17770; TPS5. DR eggNOG; KOG1050; Eukaryota. DR HOGENOM; CLU_002351_3_1_1; -. DR InParanoid; O23617; -. DR OMA; GVIMNAR; -. DR OrthoDB; 1023at2759; -. 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 GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro. DR CDD; cd03788; GT20_TPS; 1. DR CDD; cd01627; HAD_TPP; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01484; HAD-SF-IIB; 1. DR NCBIfam; TIGR00685; T6PP; 1. DR PANTHER; PTHR10788:SF94; ALPHA,ALPHA-TREHALOSE-PHOSPHATE SYNTHASE [UDP-FORMING] 5; 1. DR PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1. DR Pfam; PF00982; Glyco_transf_20; 1. DR Pfam; PF02358; Trehalose_PPase; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. DR Genevisible; O23617; AT. 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 //