ID   TREPH_PLESA             Reviewed;         751 AA.
AC   Q9UV63;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Trehalose phosphorylase {ECO:0000312|EMBL:AAF22230.1};
DE            EC=2.4.1.231;
DE   AltName: Full=Trehalose synthase {ECO:0000250|UniProtKB:O75003};
DE            Short=TSase {ECO:0000250|UniProtKB:O75003};
DE   Flags: Precursor;
GN   Name=TP {ECO:0000303|PubMed:12880768};
OS   Pleurotus sajor-caju (Oyster mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Lentinus.
OX   NCBI_TaxID=50053;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAF22230.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=ASI2070 {ECO:0000312|EMBL:AAF22230.1};
RC   TISSUE=Mycelium {ECO:0000312|EMBL:AAF22230.1};
RX   PubMed=12880768; DOI=10.1016/s1046-5928(03)00104-9;
RA   Han S.E., Kwon H.B., Lee S.B., Yi B.Y., Murayama I., Kitamoto Y.,
RA   Byun M.O.;
RT   "Cloning and characterization of a gene encoding trehalose phosphorylase
RT   (TP) from Pleurotus sajor-caju.";
RL   Protein Expr. Purif. 30:194-202(2003).
CC   -!- FUNCTION: Reversibly catalyzes the synthesis and degradation of
CC       trehalose from glucose and alpha-D-glucose 1-phosphate. The equilibrium
CC       lies in the direction of trehalose synthesis.
CC       {ECO:0000250|UniProtKB:O75003, ECO:0000269|PubMed:12880768}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-
CC         glucose 1-phosphate; Xref=Rhea:RHEA:16257, ChEBI:CHEBI:16551,
CC         ChEBI:CHEBI:17925, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601;
CC         EC=2.4.1.231; Evidence={ECO:0000269|PubMed:12880768};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=74.8 mM for trehalose (at pH 7.0) {ECO:0000269|PubMed:12880768};
CC         KM=5.4 mM for phosphate (at pH 7.0) {ECO:0000269|PubMed:12880768};
CC         KM=34.3 mM for glucose (at pH 6.3) {ECO:0000269|PubMed:12880768};
CC         KM=44.6 mM for alpha-D-glucose 1-phosphate (at pH 6.3)
CC         {ECO:0000269|PubMed:12880768};
CC       pH dependence:
CC         Optimum pH for phosphorolysis of trehalose is 6.7. Stable between pH
CC         6.0 and 7.0. {ECO:0000269|PubMed:12880768};
CC       Temperature dependence:
CC         Optimum temperature for phosphorolysis of trehalose is 36 degrees
CC         Celsius. Stable below 30 degrees Celsius, activity decreases to 58%
CC         of maximum after 3 minutes incubation at 40 degrees Celsius.
CC         {ECO:0000269|PubMed:12880768};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O75003}.
CC   -!- TISSUE SPECIFICITY: Expressed in mycelia, stipes and pilei.
CC       {ECO:0000269|PubMed:12880768}.
CC   -!- INDUCTION: By heat stress, cold stress and salt stress.
CC       {ECO:0000269|PubMed:12880768}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR   EMBL; AF149777; AAF22230.1; -; mRNA.
DR   AlphaFoldDB; Q9UV63; -.
DR   SMR; Q9UV63; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   BioCyc; MetaCyc:MON-5944; -.
DR   BRENDA; 2.4.1.231; 4915.
DR   SABIO-RK; Q9UV63; -.
DR   GO; GO:0033832; F:alpha,alpha-trehalose phosphorylase (configuration-retaining) activity; IDA:UniProtKB.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; IDA:UniProtKB.
DR   GO; GO:0006006; P:glucose metabolic process; IDA:UniProtKB.
DR   GO; GO:0005991; P:trehalose metabolic process; IDA:UniProtKB.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glucose metabolism; Glycosyltransferase;
KW   Transferase.
FT   PROPEP          1..26
FT                   /evidence="ECO:0000250|UniProtKB:O75003"
FT                   /id="PRO_0000405297"
FT   CHAIN           27..751
FT                   /note="Trehalose phosphorylase"
FT                   /evidence="ECO:0000250|UniProtKB:O75003"
FT                   /id="PRO_0000405298"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   751 AA;  83653 MW;  659C4B1E990A2012 CRC64;
     MSTPHHQFES KSSTAIRRRL SSSVSSKQRP NIMTTTFASL TPMWAGVAGT LVNNNTQYEI
     AVTVHDGVYS TDFASVIIPV TPGDTVKNSK DIEAQVLNLI RKFSAEHLCK FLGAGITLAL
     LKECPNLCTR LWLDMDIVPI VFNIKPFHTD SVTRPNIKHR ISSTTGSYVP SGSETPTVYV
     EASHLGDPSH LSPNAAQKLP IPRTLDEQSD SAARKCLMYF GPNNNPRLSI GARNPVTVDA
     GGKIHLIDDL EEYRMTVGAG TWNAVIKLAD ELREKKVKIG FFSSTPQGGG VALMRHALIR
     FLTALDVDVA WYVPNPSPQV FRTTKNNHNI LQGVAAPDLR LTQEAKDAFD AWILKNGLRW
     TAEGGPLAPG GVDVVFIDDP QMPGLIPLIK KVRPEVPIVY RSHIEIRNDL VHVAWSPQEE
     VWKYLWNNIQ LADLFISHPV SKFVPSDVPT EKLALLGAAT DWLDGLNKDL DPWDSPFYMG
     EFRPRGSHLN RGEFRSLCAK EKMHELNWPA RDYIVQVARF DPSKGIPNVV DSYYKFRNLL
     RTRSPDMDES EHPQLLICGH GAVDDPDASI IYDQIMALVN SDPYKEYAHD IVVMRLPPSD
     ELLNAMMANS RIALQLSTRE GFEVKVSEAL HTGKPVIACR TGGIPLQIQH GKSGYLTTPG
     EKDAVAGHFY DFYTDEALYR KMSDFARTHV SNEVGTVGNA AAWLYLAVMY SRGEKIKPNG
     AWINDFFREE TGEPYKEGET KLPRTKLDMQ G