O23617 (TPS5_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 5
EC=2.4.1.15

Alternative name(s):
Trehalose-6-phosphate synthase 5
Short name=AtTPS5

Gene names

Name:	TPS5
Ordered Locus Names:	At4g17770
ORF Names:	dl4920W, FCAALL.9

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	862 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate.
Subunit structure	Binds to the phosphopeptide-binding site of GRF/14-3-3 and to MBF1c. Ref.9 Ref.10
Tissue specificity	Low expression in leaves, stems, flower buds, flowers and siliques. Ref.8
Induction	90-fold induction by sucrose after 24 hours and by heat stress. Ref.7 Ref.10
Post-translational modification	Both Ser-5 and Thr-32 must be phosphorylated for binding to GRF/14-3-3. Ref.9
Miscellaneous	2-deoxyglucose, but not phenformin, enhances the phosphorylation of TPS5.
Sequence similarities	In the N-terminal section; belongs to the glycosyltransferase 20 family. In the C-terminal section; belongs to the trehalose phosphatase family.
Sequence caution	The sequence CAB10557.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB78780.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Molecular function	Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	trehalose biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular_function	transferase activity, transferring glycosyl groups Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 862	862	Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 5		PRO_0000324826
Regions
	Region	60 – 546	487	Glycosyltransferase
Amino acid modifications
	Modified residue	5	1	Phosphoserine Ref.9
	Modified residue	32	1	Phosphothreonine Ref.9
Experimental info
	Mutagenesis	5	1	S → A: Abolishes binding to GRF/14-3-3. Ref.9
	Mutagenesis	32	1	T → A: Abolishes binding to GRF/14-3-3. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	O23617 [UniParc]. Last modified March 18, 2008. Version 2. Checksum: ADA155DB26DCB470	FASTA	862	97,454
	10 20 30 40 50 60 MVSRSYSNLL DLASGNFHSF SREKKRFPRV ATVTGVLSEL DDDNNSNSVC SDAPSSVTQD 70 80 90 100 110 120 RIIIVGNQLP IKSHRNSAGK LSFSWDNDSL LLQLKDGMRE DMEVVYIGCL KEQIDTVEQD 130 140 150 160 170 180 DVSQRLLENF KCVPAYIPPE LFTKYYHGFC KQHLWPLFHY MLPLTPDLGG RFDRSLWQAY 190 200 210 220 230 240 LSVNKIFADK VMEVISPDDD FVWVHDYHLM VLPTFLRKRF NRVKLGFFLH SPFPSSEIYR 250 260 270 280 290 300 TLPVRNELLR ALLNADLIGF HTFDYARHFL SCCSRMLGLS YQSKRGTIGL EYYGRTVSIK 310 320 330 340 350 360 ILPVGIHISQ LQSILNLPET QTKVAELRDQ FLDQKVLLGV DDMDIFKGIS LKLLAMEQLL 370 380 390 400 410 420 TQHPEKRGRV VLVQIANPAR GRGKDVQEVQ SETEATVKRI NEMFGRPGYQ PVVLIDTPLQ 430 440 450 460 470 480 FFERIAYYVI AECCLVTAVR DGMNLIPYEY IICRQGNPKL NETIGLDPSA AKKSMLVVSE 490 500 510 520 530 540 FIGCSPSLSG AIRVNPWNID AVTEAMDYAL IVSEAEKQMR HEKHHKYVST HDVAYWARSF 550 560 570 580 590 600 IQDLERACGD HVRKRCWGIG FGLGFRVVAL DPSFKKLSIE HIVSAYKRTK NRAILLDYDG 610 620 630 640 650 660 TMVQPGSIRT TPTRETIEIL NNLSSDPKNI VYLVSGKDRR TLTEWFSSCD DLGLGAEHGY 670 680 690 700 710 720 FIRPNDGTDW ETSSLVSGFE WKQIAEPVMR LYTETTDGST IETKETALVW NYQFADPDFG 730 740 750 760 770 780 SCQAKELMEH LESVLTNDPV SVKTGQQLVE VKPQGVNKGL VAERLLTTMQ EKGKLLDFIL 790 800 810 820 830 840 CVGDDRSDED MFEVIMSAKD GPALSPVAEI FACTVGQKPS KAKYYLDDTA EIIRMLDGLA 850 860 ATNTTISDQT DSTATVPTKD LF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana." Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E. , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N. Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"An unexpected plethora of trehalose biosynthesis genes in Arabidopsis thaliana." Leyman B., Van Dijck P., Thevelein J.M. Trends Plant Sci. 6:510-513(2001) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[7]	"Trehalose mediated growth inhibition of Arabidopsis seedlings is due to trehalose-6-phosphate accumulation." Schluepmann H., van Dijken A.J.H., Aghdasi M., Wobbes B., Paul M., Smeekens S.C.M. Plant Physiol. 135:879-890(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY SUCROSE.
[8]	"Arabidopsis trehalose-6-phosphate synthase 1 is essential for normal vegetative growth and transition to flowering." van Dijken A.J.H., Schluepmann H., Smeekens S.C.M. Plant Physiol. 135:969-977(2004) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"Phosphorylation and 14-3-3 binding of Arabidopsis trehalose-phosphate synthase 5 in response to 2-deoxyglucose." Harthill J.E., Meek S.E.M., Morrice N., Peggie M.W., Borch J., Wong B.H.C., Mackintosh C. Plant J. 47:211-223(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-5 AND THR-32, MUTAGENESIS OF SER-5 AND THR-32, INTERACTION WITH GRF/14-3-3, MASS SPECTROMETRY.
[10]	"The transcriptional co-activator MBF1c is a key regulator of thermotolerance in Arabidopsis thaliana." Suzuki N., Bajad S., Shuman J., Shulaev V., Mittler R. J. Biol. Chem. 283:9269-9275(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MBF1C, INDUCTION BY HEAT.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z97344 Genomic DNA. Translation: CAB10557.1. Sequence problems. AL161547 Genomic DNA. Translation: CAB78780.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE83948.1. BT005967 mRNA. Translation: AAO64902.1. AK118703 mRNA. Translation: BAC43297.1.
IPI	IPI00534390.
PIR	H71447.
RefSeq	NP_567538.1. NM_117886.2.
UniGene	At.4501.
3D structure databases
HSSP	HSSP built from PDB template 1GZ5 based on UniProtKB P31677.
ProteinModelPortal	O23617.
SMR	O23617. Positions 144-546.
ModBase	Search...
Protein family/group databases
CAZy	GT20. Glycosyltransferase Family 20.
Proteomic databases
PaxDb	O23617.
PRIDE	O23617.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G17770.1; AT4G17770.1; AT4G17770.
GeneID	827498.
KEGG	ath:AT4G17770.
Organism-specific databases
TAIR	At4g17770.
Phylogenomic databases
eggNOG	COG0380.
HOGENOM	HOG000191476.
InParanoid	O23617.
KO	K16055.
OMA	MEVISPD.
PhylomeDB	O23617.
ProtClustDB	CLSN2917573.
Gene expression databases
ArrayExpress	O23617.
Genevestigator	O23617.
Family and domain databases
Gene3D	3.40.50.1000. 2 hits.
InterPro	IPR001830. Glyco_trans_20. IPR023214. HAD-like_dom. IPR006379. HAD-SF_hydro_IIB. IPR003337. Trehalose_PPase. [Graphical view]
Pfam	PF00982. Glyco_transf_20. 1 hit. PF02358. Trehalose_PPase. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01484. HAD-SF-IIB. 1 hit. TIGR00685. T6PP. 1 hit.
ProtoNet	Search...

Entry information

Entry name

TPS5_ARATH

Accession

Primary (citable) accession number: O23617
Secondary accession number(s): Q8GWQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	March 18, 2008
Last modified:	May 1, 2013
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program