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Q9LMI0

- TPS7_ARATH

UniProt

Q9LMI0 - TPS7_ARATH

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Protein

Probable alpha,alpha-trehalose-phosphate synthase [UDP-forming] 7

Gene
TPS7, TPSA, At1g06410, T2D23.11
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate.

GO - Molecular functioni

  1. transferase activity, transferring glycosyl groups Source: UniProtKB-KW

GO - Biological processi

  1. trehalose biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciARA:AT1G06410-MONOMER.

Protein family/group databases

CAZyiGT20. Glycosyltransferase Family 20.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable alpha,alpha-trehalose-phosphate synthase [UDP-forming] 7 (EC:2.4.1.15)
Alternative name(s):
Trehalose-6-phosphate synthase 7
Short name:
AtTPS7
Gene namesi
Name:TPS7
Synonyms:TPSA
Ordered Locus Names:At1g06410
ORF Names:T2D23.11
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G06410.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 851851Probable alpha,alpha-trehalose-phosphate synthase [UDP-forming] 7PRO_0000324828Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Phosphoserine By similarity
Modified residuei32 – 321Phosphothreonine By similarity

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9LMI0.
PRIDEiQ9LMI0.

Expressioni

Tissue specificityi

Expressed in seedlings, leaves, roots, stems, flowers and siliques.1 Publication

Gene expression databases

GenevestigatoriQ9LMI0.

Interactioni

Subunit structurei

Binds to the phosphopeptide-binding site of GRF/14-3-3.1 Publication

Protein-protein interaction databases

BioGridi22393. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9LMI0.
SMRiQ9LMI0. Positions 142-541, 588-831.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni59 – 540482GlycosyltransferaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the glycosyltransferase 20 family.
In the C-terminal section; belongs to the trehalose phosphatase family.

Phylogenomic databases

eggNOGiCOG0380.
HOGENOMiHOG000191476.
InParanoidiQ9LMI0.
KOiK16055.
OMAiNEINAYY.
PhylomeDBiQ9LMI0.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR001830. Glyco_trans_20.
IPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR003337. Trehalose_PPase.
[Graphical view]
PfamiPF00982. Glyco_transf_20. 1 hit.
PF02358. Trehalose_PPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
TIGR00685. T6PP. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9LMI0-1 [UniParc]FASTAAdd to Basket

« Hide

MISRSYTNLL DLASGNFPVM GRERRRLPRV MTVPGNVSEF DEDQAYSVSS    50
DNPSSVSSDR MIIVANRLPL KAEKRNGSWS FSWDQDSLYL QLKDGLPEDM 100
EILYVGSLSV DVDSNEQDDV AQILLDKFKC VPTFFPPDLQ SKFYDGFCKR 150
QIWPLFHYML PFSADHGGRF DRSLWEAYVA TNKLFFQKVI EVINPDDDFV 200
WIHDYHLMVL PTFLRRRFNR IRMGFFLHSP FPSSEIYRSL PVREEILKAL 250
LNSDLIGFHT FDYARHFLTC CSRMLGLEYQ SKRGYIGLEY YGRTVGIKIM 300
PVGINMGRIQ SVMRYSEEEG KVMELRNRFE GKTVLLGIDD MDIFKGINLK 350
LLAMEQMLRQ HPNWRGRAVL VQIVNPARGK GIDVEEIRGE IEESCRRING 400
EFGKPGYQPI IYIDTPVSIN EINAYYHIAE CVVVTAVRDG MNLTPYEYIV 450
CRQGLLGSES DFSGPKKSML VASEFIGCSP SLSGAIRVNP WNVEATGEAL 500
NEALSMSDAE KQLRHEKHFR YVSTHDVAYW SRSFLQDLER ICVDHFKKRC 550
WGMGISFGFR VVALDPNFRK LSIPCIVSDY KRAKSRAILL DYDGTLMPQN 600
SINKAPSQEV LNFLDALCED KKNSIFIVSG RGRESLSKWF TPCKKIGIAA 650
EHGYFLKWSG SEEWETCGQS SDFGWMQIVE PVMKQYTEST DGSSIEIKES 700
ALVWQYRDAD PGFGSLQAKE MLEHLESVLA NEPVAVKSGH YIVEVKPQGV 750
SKGSVSEKIF SSMAGKGKPV DFVLCIGDDR SDEDMFEAIG NAMSKRLLCD 800
NALVFACTVG QKPSKAKYYL DDTTEVTCML ESLAEASEAS NFSMRELDEA 850
L 851
Length:851
Mass (Da):96,688
Last modified:October 1, 2000 - v1
Checksum:i1799F009CF8E4A1B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC068143 Genomic DNA. Translation: AAF82169.1.
CP002684 Genomic DNA. Translation: AEE27983.1.
AK228947 mRNA. Translation: BAF00836.1.
PIRiA86200.
RefSeqiNP_172129.1. NM_100521.2.
UniGeneiAt.43841.

Genome annotation databases

EnsemblPlantsiAT1G06410.1; AT1G06410.1; AT1G06410.
GeneIDi837152.
KEGGiath:AT1G06410.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC068143 Genomic DNA. Translation: AAF82169.1 .
CP002684 Genomic DNA. Translation: AEE27983.1 .
AK228947 mRNA. Translation: BAF00836.1 .
PIRi A86200.
RefSeqi NP_172129.1. NM_100521.2.
UniGenei At.43841.

3D structure databases

ProteinModelPortali Q9LMI0.
SMRi Q9LMI0. Positions 142-541, 588-831.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 22393. 1 interaction.

Protein family/group databases

CAZyi GT20. Glycosyltransferase Family 20.

Proteomic databases

PaxDbi Q9LMI0.
PRIDEi Q9LMI0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G06410.1 ; AT1G06410.1 ; AT1G06410 .
GeneIDi 837152.
KEGGi ath:AT1G06410.

Organism-specific databases

TAIRi AT1G06410.

Phylogenomic databases

eggNOGi COG0380.
HOGENOMi HOG000191476.
InParanoidi Q9LMI0.
KOi K16055.
OMAi NEINAYY.
PhylomeDBi Q9LMI0.

Enzyme and pathway databases

BioCyci ARA:AT1G06410-MONOMER.

Gene expression databases

Genevestigatori Q9LMI0.

Family and domain databases

Gene3Di 3.40.50.1000. 2 hits.
InterProi IPR001830. Glyco_trans_20.
IPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR003337. Trehalose_PPase.
[Graphical view ]
Pfami PF00982. Glyco_transf_20. 1 hit.
PF02358. Trehalose_PPase. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 1 hit.
TIGRFAMsi TIGR01484. HAD-SF-IIB. 1 hit.
TIGR00685. T6PP. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: cv. Landsberg erecta.
  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] [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. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 559-851.
    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] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  6. "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, INTERACTION WITH GRF/14-3-3, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  8. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTPS7_ARATH
AccessioniPrimary (citable) accession number: Q9LMI0
Secondary accession number(s): Q0WPW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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