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Protein

Trehalose phosphorylase

Gene

TP

Organism
Pleurotus sajor-caju (Oyster mushroom)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Reversibly catalyzes the synthesis and degradation of trehalose from glucose and alpha-D-glucose 1-phosphate. The equilibrium lies in the direction of trehalose synthesis.By similarity1 Publication

Catalytic activityi

Alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate.1 Publication

Kineticsi

  1. KM=74.8 mM for trehalose (at pH 7.0)1 Publication
  2. KM=5.4 mM for phosphate (at pH 7.0)1 Publication
  3. KM=34.3 mM for glucose (at pH 6.3)1 Publication
  4. KM=44.6 mM for alpha-D-glucose 1-phosphate (at pH 6.3)1 Publication

    pH dependencei

    Optimum pH for phosphorolysis of trehalose is 6.7. Stable between pH 6.0 and 7.0.1 Publication

    Temperature dependencei

    Optimum temperature for phosphorolysis of trehalose is 36 degrees Celsius. Stable below 30 degrees Celsius, activity decreases to 58% of maximum after 3 minutes incubation at 40 degrees Celsius.1 Publication

    GO - Molecular functioni

    GO - Biological processi

    • glucose 6-phosphate metabolic process Source: UniProtKB
    • glucose metabolic process Source: UniProtKB
    • trehalose metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-5944.
    BRENDAi2.4.1.231. 4915.
    SABIO-RKQ9UV63.

    Protein family/group databases

    CAZyiGT4. Glycosyltransferase Family 4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trehalose phosphorylaseImported (EC:2.4.1.231)
    Alternative name(s):
    Trehalose synthaseBy similarity
    Short name:
    TSaseBy similarity
    Gene namesi
    Name:TP1 Publication
    OrganismiPleurotus sajor-caju (Oyster mushroom)
    Taxonomic identifieri50053 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesLentinaceaeLentinus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 2626By similarityPRO_0000405297Add
    BLAST
    Chaini27 – 751725Trehalose phosphorylaseBy similarityPRO_0000405298Add
    BLAST

    Expressioni

    Tissue specificityi

    Expressed in mycelia, stipes and pilei.1 Publication

    Inductioni

    By heat stress, cold stress and salt stress.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UV63.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR001296. Glyco_trans_1.
    [Graphical view]
    PfamiPF00534. Glycos_transf_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9UV63-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSTPHHQFES KSSTAIRRRL SSSVSSKQRP NIMTTTFASL TPMWAGVAGT
    60 70 80 90 100
    LVNNNTQYEI AVTVHDGVYS TDFASVIIPV TPGDTVKNSK DIEAQVLNLI
    110 120 130 140 150
    RKFSAEHLCK FLGAGITLAL LKECPNLCTR LWLDMDIVPI VFNIKPFHTD
    160 170 180 190 200
    SVTRPNIKHR ISSTTGSYVP SGSETPTVYV EASHLGDPSH LSPNAAQKLP
    210 220 230 240 250
    IPRTLDEQSD SAARKCLMYF GPNNNPRLSI GARNPVTVDA GGKIHLIDDL
    260 270 280 290 300
    EEYRMTVGAG TWNAVIKLAD ELREKKVKIG FFSSTPQGGG VALMRHALIR
    310 320 330 340 350
    FLTALDVDVA WYVPNPSPQV FRTTKNNHNI LQGVAAPDLR LTQEAKDAFD
    360 370 380 390 400
    AWILKNGLRW TAEGGPLAPG GVDVVFIDDP QMPGLIPLIK KVRPEVPIVY
    410 420 430 440 450
    RSHIEIRNDL VHVAWSPQEE VWKYLWNNIQ LADLFISHPV SKFVPSDVPT
    460 470 480 490 500
    EKLALLGAAT DWLDGLNKDL DPWDSPFYMG EFRPRGSHLN RGEFRSLCAK
    510 520 530 540 550
    EKMHELNWPA RDYIVQVARF DPSKGIPNVV DSYYKFRNLL RTRSPDMDES
    560 570 580 590 600
    EHPQLLICGH GAVDDPDASI IYDQIMALVN SDPYKEYAHD IVVMRLPPSD
    610 620 630 640 650
    ELLNAMMANS RIALQLSTRE GFEVKVSEAL HTGKPVIACR TGGIPLQIQH
    660 670 680 690 700
    GKSGYLTTPG EKDAVAGHFY DFYTDEALYR KMSDFARTHV SNEVGTVGNA
    710 720 730 740 750
    AAWLYLAVMY SRGEKIKPNG AWINDFFREE TGEPYKEGET KLPRTKLDMQ

    G
    Length:751
    Mass (Da):83,653
    Last modified:May 1, 2000 - v1
    Checksum:i659C4B1E990A2012
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF149777 mRNA. Translation: AAF22230.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF149777 mRNA. Translation: AAF22230.1.

    3D structure databases

    ProteinModelPortaliQ9UV63.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGT4. Glycosyltransferase Family 4.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-5944.
    BRENDAi2.4.1.231. 4915.
    SABIO-RKQ9UV63.

    Family and domain databases

    InterProiIPR001296. Glyco_trans_1.
    [Graphical view]
    PfamiPF00534. Glycos_transf_1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiTREPH_PLESA
    AccessioniPrimary (citable) accession number: Q9UV63
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 8, 2011
    Last sequence update: May 1, 2000
    Last modified: November 11, 2015
    This is version 46 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. 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.