TREPH_PLEPU
ID TREPH_PLEPU Reviewed; 739 AA.
AC A6YRN9;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Trehalose phosphorylase {ECO:0000312|EMBL:ABR88135.1};
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:0000250|UniProtKB:Q9UV63};
OS Pleurotus pulmonarius (Indian oyster mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=28995;
RN [1] {ECO:0000312|EMBL:ABR88135.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tian Z.D., Xie C.H., Liu J.;
RT "Isolation and functional characterization of trehalose phosphorylase gene
RT in Pleurotus pulmonarius (Fr.).";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250|UniProtKB:O75003, ECO:0000250|UniProtKB:Q9UV63}.
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:0000250|UniProtKB:Q9UV63};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O75003}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF645805; ABR88135.1; -; mRNA.
DR AlphaFoldDB; A6YRN9; -.
DR SMR; A6YRN9; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR BRENDA; 2.4.1.231; 4914.
DR GO; GO:0033832; F:alpha,alpha-trehalose phosphorylase (configuration-retaining) activity; ISS:UniProtKB.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; ISS:UniProtKB.
DR GO; GO:0005991; P:trehalose metabolic process; ISS:UniProtKB.
DR InterPro; IPR001296; Glyco_trans_1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glucose metabolism; Glycosyltransferase;
KW Transferase.
FT PROPEP 1..26
FT /evidence="ECO:0000250|UniProtKB:O75003"
FT /id="PRO_0000405295"
FT CHAIN 27..739
FT /note="Trehalose phosphorylase"
FT /evidence="ECO:0000250|UniProtKB:O75003"
FT /id="PRO_0000405296"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 82028 MW; 6A8444D92D48EA95 CRC64;
MSTPHHQFES KSSTAIRRRL SSSVSSKQRP NIMTTTFASL TPMWAGVAGT LVNNNTQYEI
AVTVHDGVYS TDFASVIIPV TPGDTVKNSK DIEAQVLNLI RKFSAEHLCK FLGAGITLAL
LKECPNLCTR LWLDMDIVPI VFNIKPFHTD SVTRPNIKHR ISSTTGSYVP SGSETPTVYV
EASHLDDPSH LSPNAAQKLP IPRTLDEQSD SAARKCLMYF GPNNNPRLSI GARNQVTVDA
GGKIHLIDDL EEYRETVGAG TWNAVIKLAD ELREKKVKIG FFSSTPQGGG VALMRHALIR
FLTALDVDVA WYVPNPSPQV FRTTKNNHNI LQGVAAPDLR LTQEAKDAFD AWILKNGLRW
TAEGGPLAPG GVDVVFIDDP QMPGLIPLIK KVRPEVPIVY RSHIEIRSDL VHVAGSPQEE
VWKYLWNNIQ LADLFISHPV SKFVPSDVPT EKLALLGAAT DWLDGLNKDL DPWDSQFYMG
EFRSPCAKEK MHELNWPARD YIVQVARFDP SKGIPNVVDS YYKFRNLLRT RSPDMDESEH
PQLLICGHGA VDDPDASIIY DQIMALVNSD PYKEYAHDIV VMRLPPSDEL LNAMMANSRI
ALQLSTREGF EVKVSEALHT GKPVIACRTG GIPLQIQHGK SGYLTTPGDN DAVAGHLYDL
YTDEALYRKM SDFARTHVSD EVGTVGNAAA WLYLAVMYSR GEKIKPNGAW INDLLREETG
EPYKEGETKL PRTKLDMQG