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Protein

Trehalase

Gene

TRE1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in the regulation of trehalose content by hydrolyzing trehalose to glucose.3 Publications

Catalytic activityi

Alpha,alpha-trehalose + H2O = beta-D-glucose + alpha-D-glucose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei224 – 2241SubstrateBy similarity
Binding sitei268 – 2681SubstrateBy similarity
Binding sitei378 – 3781Substrate; via carbonyl oxygenBy similarity
Active sitei380 – 3801Proton donor/acceptorBy similarity
Active sitei580 – 5801Proton donor/acceptorBy similarity
Binding sitei595 – 5951SubstrateBy similarity

GO - Molecular functioni

  • alpha,alpha-trehalase activity Source: TAIR

GO - Biological processi

  • trehalose catabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Stress response

Protein family/group databases

CAZyiGH37. Glycoside Hydrolase Family 37.

Names & Taxonomyi

Protein namesi
Recommended name:
Trehalase (EC:3.2.1.28)
Alternative name(s):
Alpha,alpha-trehalase
Alpha,alpha-trehalose glucohydrolase
Trehalase 1
Short name:
AtTRE1
Gene namesi
Name:TRE1
Ordered Locus Names:At4g24040
ORF Names:T19F6.15, T19F6.30
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G24040.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei20 – 4021HelicalSequence analysisAdd
BLAST
Transmembranei45 – 6521HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions, but plants accumulate high levels of trehalose and starch.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 626626TrehalasePRO_0000417663Add
BLAST

Proteomic databases

PaxDbiQ9SU50.
PRIDEiQ9SU50.

Expressioni

Tissue specificityi

Highly expressed in flowers. Expressed at low levels in leaves and stems.2 Publications

Gene expression databases

GenevisibleiQ9SU50. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G24040.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SU50.
SMRiQ9SU50. Positions 152-614.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni231 – 2322Substrate bindingBy similarity
Regioni277 – 2793Substrate bindingBy similarity
Regioni344 – 3463Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 37 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0602. Eukaryota.
COG1626. LUCA.
HOGENOMiHOG000215465.
InParanoidiQ9SU50.
KOiK01194.
OMAiCREATAN.
PhylomeDBiQ9SU50.

Family and domain databases

InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR001661. Glyco_hydro_37.
IPR018232. Glyco_hydro_37_CS.
[Graphical view]
PANTHERiPTHR23403. PTHR23403. 1 hit.
PfamiPF01204. Trehalase. 1 hit.
[Graphical view]
PRINTSiPR00744. GLHYDRLASE37.
SUPFAMiSSF48208. SSF48208. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
PS00928. TREHALASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9SU50-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSYKLNNPN LLISTHTHNK LFLSSSPFNL LFSFPSFIYL KQQRSLFFFF
60 70 80 90 100
FFFLCFSFTT SMLDSDTDTD SGPVVATTKL VTFLQRVQHT ALRSYPKKQT
110 120 130 140 150
PDPKSYIDLS LKRPYSLSTI ESAFDDLTSE SHDQPVPVET LEKFVKEYFD
160 170 180 190 200
GAGEDLLHHE PVDFVSDPSG FLSNVENEEV REWAREVHGL WRNLSCRVSD
210 220 230 240 250
SVRESADRHT LLPLPEPVII PGSRFREVYY WDSYWVIKGL MTSQMFTTAK
260 270 280 290 300
GLVTNLMSLV ETYGYALNGA RAYYTNRSQP PLLSSMVYEI YNVTKDEELV
310 320 330 340 350
RKAIPLLLKE YEFWNSGKHK VVIRDANGYD HVLSRYYAMW NKPRPESSVF
360 370 380 390 400
DEESASGFST MLEKQRFHRD IATAAESGCD FSTRWMRDPP NFTTMATTSV
410 420 430 440 450
VPVDLNVFLL KMELDIAFMM KVSGDQNGSD RFVKASKARE KAFQTVFWNE
460 470 480 490 500
KAGQWLDYWL SSSGEESETW KAENQNTNVF ASNFAPIWIN SINSDENLVK
510 520 530 540 550
KVVTALKNSG LIAPAGILTS LTNSGQQWDS PNGWAPQQEM IVTGLGRSSV
560 570 580 590 600
KEAKEMAEDI ARRWIKSNYL VYKKSGTIHE KLKVTELGEY GGGGEYMPQT
610 620
GFGWSNGVIL AFLEEYGWPS HLSIEA
Length:626
Mass (Da):71,355
Last modified:May 1, 2000 - v1
Checksum:iA23D8E2C9C2D048F
GO

Sequence cautioni

The sequence AAB63620.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002343 Genomic DNA. Translation: AAB63620.1. Sequence problems.
AL109619 Genomic DNA. Translation: CAB51647.1.
AL161560 Genomic DNA. Translation: CAB81322.1.
CP002687 Genomic DNA. Translation: AEE84844.1.
AK118407 mRNA. Translation: BAC43016.1.
BT010732 mRNA. Translation: AAR23702.1.
PIRiT13444.
RefSeqiNP_194135.1. NM_118536.3.
UniGeneiAt.28685.

Genome annotation databases

EnsemblPlantsiAT4G24040.1; AT4G24040.1; AT4G24040.
GeneIDi828504.
GrameneiAT4G24040.1; AT4G24040.1; AT4G24040.
KEGGiath:AT4G24040.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002343 Genomic DNA. Translation: AAB63620.1. Sequence problems.
AL109619 Genomic DNA. Translation: CAB51647.1.
AL161560 Genomic DNA. Translation: CAB81322.1.
CP002687 Genomic DNA. Translation: AEE84844.1.
AK118407 mRNA. Translation: BAC43016.1.
BT010732 mRNA. Translation: AAR23702.1.
PIRiT13444.
RefSeqiNP_194135.1. NM_118536.3.
UniGeneiAt.28685.

3D structure databases

ProteinModelPortaliQ9SU50.
SMRiQ9SU50. Positions 152-614.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G24040.1.

Protein family/group databases

CAZyiGH37. Glycoside Hydrolase Family 37.

Proteomic databases

PaxDbiQ9SU50.
PRIDEiQ9SU50.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G24040.1; AT4G24040.1; AT4G24040.
GeneIDi828504.
GrameneiAT4G24040.1; AT4G24040.1; AT4G24040.
KEGGiath:AT4G24040.

Organism-specific databases

TAIRiAT4G24040.

Phylogenomic databases

eggNOGiKOG0602. Eukaryota.
COG1626. LUCA.
HOGENOMiHOG000215465.
InParanoidiQ9SU50.
KOiK01194.
OMAiCREATAN.
PhylomeDBiQ9SU50.

Miscellaneous databases

PROiQ9SU50.

Gene expression databases

GenevisibleiQ9SU50. AT.

Family and domain databases

InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR001661. Glyco_hydro_37.
IPR018232. Glyco_hydro_37_CS.
[Graphical view]
PANTHERiPTHR23403. PTHR23403. 1 hit.
PfamiPF01204. Trehalase. 1 hit.
[Graphical view]
PRINTSiPR00744. GLHYDRLASE37.
SUPFAMiSSF48208. SSF48208. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
PS00928. TREHALASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Arabidopsis cDNA clones."
    Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y., Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M., Shinozaki K., Ecker J.R.
    Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Cited for: FUNCTION, TISSUE SPECIFICITY.
  6. "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.
  7. "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.
  8. "The Arabidopsis thaliana trehalase is a plasma membrane-bound enzyme with extracellular activity."
    Frison M., Parrou J.L., Guillaumot D., Masquelier D., Francois J., Chaumont F., Batoko H.
    FEBS Lett. 581:4010-4016(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "Capillary electrophoresis-mass spectrometry analysis of trehalose-6-phosphate in Arabidopsis thaliana seedlings."
    Delatte T.L., Schluepmann H., Smeekens S.C., de Jong G.J., Somsen G.W.
    Anal. Bioanal. Chem. 400:1137-1144(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  10. "TREHALOSE PHOSPHATE SYNTHASE11-dependent trehalose metabolism promotes Arabidopsis thaliana defense against the phloem-feeding insect Myzus persicae."
    Singh V., Louis J., Ayre B.G., Reese J.C., Pegadaraju V., Shah J.
    Plant J. 67:94-104(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiTRE1_ARATH
AccessioniPrimary (citable) accession number: Q9SU50
Secondary accession number(s): O22986
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2012
Last sequence update: May 1, 2000
Last modified: February 17, 2016
This is version 109 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. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.