Q9SYM4 (TPS1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 1
EC=2.4.1.15

Alternative name(s):
Trehalose-6-phosphate synthase 1
Short name=AtTPS1

Gene names

Name:	TPS1
Ordered Locus Names:	At1g78580
ORF Names:	T30F21.9

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	942 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for normal embryo development, vegetative growth and transition to flowering. Regulates embryo growth, cell wall deposition, starch and sucrose degradation, but not cell differentiation. Involved in the regulation of glucose sensing and signaling genes during plant development. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14
Catalytic activity	UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate.
Subcellular location	Vacuole. Secreted › cell wall. Cytoplasm. Note: Determined in transgenic tobacco plants expressing TPS1. Ref.15
Tissue specificity	Expressed in seedlings, leaves, roots, stems, flowers and siliques. Ref.1 Ref.6 Ref.8
Developmental stage	Up-regulated during seed development. Ref.8
Induction	Low induction by sucrose after 24 hours. Down-regulated by dark incubation. Ref.6 Ref.10
Domain	The N-terminal part (1-88) has an inhibitory function on the enzymatic activity.
Disruption phenotype	Embryonic lethality. Ref.8 Ref.11 Ref.13 Ref.14
Sequence similarities	In the N-terminal section; belongs to the glycosyltransferase 20 family. In the C-terminal section; belongs to the trehalose phosphatase family.

Ontologies

Keywords
Cellular component	Cell wall Cytoplasm Secreted Vacuole
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell division Inferred from mutant phenotype Ref.14. Source: TAIR embryo development ending in seed dormancy Inferred from mutant phenotype Ref.14. Source: TAIR plant-type cell wall biogenesis Inferred from mutant phenotype Ref.14. Source: TAIR sugar mediated signaling pathway Inferred from mutant phenotype Ref.12. Source: TAIR trehalose biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-KW vacuole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity Inferred from genetic interaction Ref.6. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 942	942	Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 1		PRO_0000324822
Regions
	Region	92 – 559	468	Glycosyltransferase
	Compositional bias	71 – 76	6	Poly-Ala
	Compositional bias	822 – 890	69	Ser-rich
Experimental info
	Mutagenesis	17	1	R → Q: 3-fold increase in activity. Ref.7
	Mutagenesis	27	1	L → P: 4-fold increase in activity. Ref.7
	Sequence conflict	105	1	A → P in CAA69879. Ref.1
	Sequence conflict	348	1	I → K in CAA69879. Ref.1
	Sequence conflict	359 – 360	2	AG → TD in CAA69879. Ref.1
	Sequence conflict	401	1	Q → K in CAA69879. Ref.1
	Sequence conflict	408	1	T → P in CAA69879. Ref.1
	Sequence conflict	415	1	K → T in CAA69879. Ref.1
	Sequence conflict	428	1	N → I in CAA69879. Ref.1
	Sequence conflict	431	1	F → L in CAA69879. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9SYM4 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: B22AC11EA34CDDDB	FASTA	942	105,976
	10 20 30 40 50 60 MPGNKYNCSS SHIPLSRTER LLRDRELREK RKSNRARNPN DVAGSSENSE NDLRLEGDSS 70 80 90 100 110 120 RQYVEQYLEG AAAAMAHDDA CERQEVRPYN RQRLLVVANR LPVSAVRRGE DSWSLEISAG 130 140 150 160 170 180 GLVSALLGVK EFEARWIGWA GVNVPDEVGQ KALSKALAEK RCIPVFLDEE IVHQYYNGYC 190 200 210 220 230 240 NNILWPLFHY LGLPQEDRLA TTRSFQSQFA AYKKANQMFA DVVNEHYEEG DVVWCHDYHL 250 260 270 280 290 300 MFLPKCLKEY NSKMKVGWFL HTPFPSSEIH RTLPSRSELL RSVLAADLVG FHTYDYARHF 310 320 330 340 350 360 VSACTRILGL EGTPEGVEDQ GRLTRVAAFP IGIDSDRFIR ALEVPEVIQH MKELKERFAG 370 380 390 400 410 420 RKVMLGVDRL DMIKGIPQKI LAFEKFLEEN ANWRDKVVLL QIAVPTRTDV PEYQKLTSQV 430 440 450 460 470 480 HEIVGRINGR FGTLTAVPIH HLDRSLDFHA LCALYAVTDV ALVTSLRDGM NLVSYEFVAC 490 500 510 520 530 540 QEAKKGVLIL SEFAGAAQSL GAGAILVNPW NITEVAASIG QALNMTAEER EKRHRHNFHH 550 560 570 580 590 600 VKTHTAQEWA ETFVSELNDT VIEAQLRISK VPPELPQHDA IQRYSKSNNR LLILGFNATL 610 620 630 640 650 660 TEPVDNQGRR GDQIKEMDLN LHPELKGPLK ALCSDPSTTI VVLSGSSRSV LDKNFGEYDM 670 680 690 700 710 720 WLAAENGMFL RLTNGEWMTT MPEHLNMEWV DSVKHVFKYF TERTPRSHFE TRDTSLIWNY 730 740 750 760 770 780 KYADIEFGRL QARDLLQHLW TGPISNASVD VVQGSRSVEV RAVGVTKGAA IDRILGEIVH 790 800 810 820 830 840 SKSMTTPIDY VLCIGHFLGK DEDVYTFFEP ELPSDMPAIA RSRPSSDSGA KSSSGDRRPP 850 860 870 880 890 900 SKSTHNNNKS GSKSSSSSNS NNNNKSSQRS LQSERKSGSN HSLGNSRRPS PEKISWNVLD 910 920 930 940 LKGENYFSCA VGRTRTNARY LLGSPDDVVC FLEKLADTTS SP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and molecular characterization of the Arabidopsis TPS1 gene, encoding trehalose-6-phosphate synthase." Blazquez M.A., Santos E., Flores C.L., Martinez-Zapater J.M., Salinas J., Gancedo C. Plant J. 13:685-689(1998) [PubMed: 9681010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 389-942. Strain: cv. Columbia.
[5]	"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: 11701378] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[6]	"Trehalose metabolism in Arabidopsis: occurrence of trehalose and molecular cloning and characterization of trehalose-6-phosphate synthase homologues." Vogel G., Fiehn O., Jean-Richard-dit-Bressel L., Boller T., Wiemken A., Aeschbacher R.A., Wingler A. J. Exp. Bot. 52:1817-1826(2001) [PubMed: 11520870] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION. Strain: cv. Landsberg erecta.
[7]	"Truncation of Arabidopsis thaliana and Selaginella lepidophylla trehalose-6-phosphate synthase unlocks high catalytic activity and supports high trehalose levels on expression in yeast." Van Dijck P., Mascorro-Gallardo J.O., De Bus M., Royackers K., Iturriaga G., Thevelein J.M. Biochem. J. 366:63-71(2002) [PubMed: 11978181] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ARG-17 AND LEU-27.
[8]	"Trehalose-6-phosphate synthase 1, which catalyses the first step in trehalose synthesis, is essential for Arabidopsis embryo maturation." Eastmond P.J., van Dijken A.J.H., Spielman M., Kerr A., Tissier A.F., Dickinson H.G., Jones J.D.G., Smeekens S.C., Graham I.A. Plant J. 29:225-235(2002) [PubMed: 11851922] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
[9]	"Trehalose 6-phosphate is indispensable for carbohydrate utilization and growth in Arabidopsis thaliana." Schluepmann H., Pellny T., van Dijken A.J.H., Smeekens S.C.M., Paul M. Proc. Natl. Acad. Sci. U.S.A. 100:6849-6854(2003) [PubMed: 12748379] [Abstract] Cited for: FUNCTION.
[10]	"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: 15181209] [Abstract] Cited for: INDUCTION BY SUCROSE.
[11]	"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: 15181208] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[12]	"Trehalose metabolism and glucose sensing in plants." Avonce N., Leyman B., Thevelein J., Iturriaga G. Biochem. Soc. Trans. 33:276-279(2005) [PubMed: 15667325] [Abstract] Cited for: FUNCTION.
[13]	"The role of trehalose-6-phosphate synthase in Arabidopsis embryo development." Gomez L.D., Baud S., Graham I.A. Biochem. Soc. Trans. 33:280-282(2005) [PubMed: 15667326] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[14]	"Delayed embryo development in the ARABIDOPSIS TREHALOSE-6-PHOSPHATE SYNTHASE 1 mutant is associated with altered cell wall structure, decreased cell division and starch accumulation." Gomez L.D., Baud S., Gilday A., Li Y., Graham I.A. Plant J. 46:69-84(2006) [PubMed: 16553896] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[15]	"Immunogold localization of trehalose-6-phosphate synthase in leaf segments of wild-type and transgenic tobacco plants expressing the AtTPS1 gene from Arabidopsis thaliana." Almeida A.M., Santos M., Villalobos E., Araujo S.S., van Dijck P., Leyman B., Cardoso L.A., Santos D., Fevereiro P.S., Torne J.M. Protoplasma 230:41-49(2007) [PubMed: 17111094] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y08568 mRNA. Translation: CAA69879.1. AC007260 Genomic DNA. Translation: AAD30578.1. CP002684 Genomic DNA. Translation: AEE36123.1. AF370287 mRNA. Translation: AAK44102.2.
IPI	IPI00532980.
PIR	D96814.
RefSeq	NP_177979.1. NM_106505.4.
UniGene	At.198. At.71030.
3D structure databases
HSSP	HSSP built from PDB template 1GZ5 based on UniProtKB P31677.
ProteinModelPortal	Q9SYM4.
SMR	Q9SYM4. Positions 92-563.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9SYM4.
Protein family/group databases
CAZy	GT20. Glycosyltransferase Family 20.
Proteomic databases
PRIDE	Q9SYM4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G78580.1; AT1G78580.1; AT1G78580.
GeneID	844194.
GenomeReviews	Gene locus AT1G78580 in contig CT485782_GR.
KEGG	ath:AT1G78580.
NMPDR	fig|3702.1.peg.7408.
Organism-specific databases
TAIR	At1g78580.
Phylogenomic databases
eggNOG	KOG1050.
GeneTree	EPGT00070000029651.
HOGENOM	HBG559076.
InParanoid	Q9SYM4.
OMA	PEHLNME.
PhylomeDB	Q9SYM4.
ProtClustDB	PLN03064.
Gene expression databases
Genevestigator	Q9SYM4.
Family and domain databases
InterPro	IPR001830. Glyco_trans_20. IPR023214. HAD-like_dom. IPR012766. Trehalose_OtsA. IPR003337. Trehalose_PPase. [Graphical view]
Gene3D	G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KO	K00697.
Pfam	PF00982. Glyco_transf_20. 1 hit. PF02358. Trehalose_PPase. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR02400. Trehalose_OtsA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

TPS1_ARATH

Accession

Primary (citable) accession number: Q9SYM4
Secondary accession number(s): P93653, Q94K55

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	May 1, 2000
Last modified:	December 14, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program