TREPH_GRIFR
ID TREPH_GRIFR Reviewed; 732 AA.
AC O75003; E1ACW7;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Trehalose phosphorylase {ECO:0000250|UniProtKB:Q9UV63};
DE EC=2.4.1.231;
DE AltName: Full=Trehalose synthase {ECO:0000312|EMBL:BAA31350.1};
DE Short=TSase {ECO:0000303|PubMed:9763690, ECO:0000303|PubMed:9797287};
DE Flags: Precursor;
OS Grifola frondosa (Maitake) (Polyporus frondosus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Grifolaceae; Grifola.
OX NCBI_TaxID=5627;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA31349.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 26-46; 91-98;
RP 240-251; 256-271; 387-402; 564-578; 606-614 AND 697-708, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=CM-236 / FERM BP-35 {ECO:0000269|PubMed:9763690};
RC TISSUE=Mycelium {ECO:0000269|PubMed:9763690};
RX PubMed=9763690; DOI=10.1007/s002530051276;
RA Saito K., Yamazaki H., Ohnishi Y., Fujimoto S., Takahashi E.,
RA Horinouchi S.;
RT "Production of trehalose synthase from a basidiomycete, Grifola frondosa,
RT in Escherichia coli.";
RL Appl. Microbiol. Biotechnol. 50:193-198(1998).
RN [2] {ECO:0000312|EMBL:ADM15725.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Xu F., Liu Y., Wang S., Zhao S., Geng X., Meng L.;
RT "Overexpression of trehalose synthase gene from Grifola frondosa in
RT Pleurotus ostreatus.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=CM-236 / FERM BP-35 {ECO:0000269|PubMed:9797287};
RX PubMed=9797287; DOI=10.1128/aem.64.11.4340-4345.1998;
RA Saito K., Kase T., Takahashi E., Horinouchi S.;
RT "Purification and characterization of a trehalose synthase from the
RT basidiomycete Grifola frondosa.";
RL Appl. Environ. Microbiol. 64:4340-4345(1998).
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:0000269|PubMed:9763690, ECO:0000269|PubMed:9797287}.
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:9763690,
CC ECO:0000269|PubMed:9797287};
CC -!- ACTIVITY REGULATION: Activity abolished by 1 mM Cu(2+). 0.1 mM Cu(2+)
CC reduces trehalose phosphorolysis to 76% and trehalose synthesis to 48%
CC of maximum activity. 1 mM Zn(2+) abolishes trehalose synthesis, and
CC reduces trehalose phosphorolysis to 40% of maximum activity. Unaffected
CC by EDTA. {ECO:0000269|PubMed:9797287}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5 for trehalose phosphorolysis activity, 6.5-6.8 for
CC trehalose synthesis activity. {ECO:0000269|PubMed:9797287};
CC Temperature dependence:
CC Optimum temperature is 32.5 degrees Celsius for trehalose
CC phosphorolysis activity, 37.5 degrees Celsius for trehalose synthesis
CC activity. Stable up to 35 degrees Celsius for trehalose
CC phosphorolysis activity, 32.5 degrees Celsius for trehalose synthesis
CC activity. {ECO:0000269|PubMed:9797287};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9797287}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; AB010104; BAA31349.1; -; Genomic_DNA.
DR EMBL; AB010105; BAA31350.1; -; mRNA.
DR EMBL; HM631875; ADM15725.1; -; mRNA.
DR PIR; T00130; T00130.
DR AlphaFoldDB; O75003; -.
DR SMR; O75003; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR BioCyc; MetaCyc:MON-5943; -.
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; Direct protein sequencing; Glucose metabolism;
KW Glycosyltransferase; Transferase.
FT PROPEP 1..25
FT /evidence="ECO:0000269|PubMed:9763690"
FT /id="PRO_0000405293"
FT CHAIN 26..732
FT /note="Trehalose phosphorylase"
FT /evidence="ECO:0000269|PubMed:9763690"
FT /id="PRO_0000405294"
FT CONFLICT 30
FT /note="I -> V (in Ref. 2; ADM15725)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="T -> S (in Ref. 2; ADM15725)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="V -> I (in Ref. 2; ADM15725)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="M -> V (in Ref. 2; ADM15725)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="S -> A (in Ref. 2; ADM15725)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="V -> I (in Ref. 2; ADM15725)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="E -> D (in Ref. 2; ADM15725)"
FT /evidence="ECO:0000305"
FT CONFLICT 718
FT /note="P -> A (in Ref. 2; ADM15725)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 732 AA; 81582 MW; 5E01041357118DAF CRC64;
MAPPHQFQSK PSDVIRRRLS SAVSSKRPNI PGYTSLTPMW AGIAGAVVNN NTQFEVAISI
HDSVYNTDFA SSVVPYSPNE PEAQAGIIEK HVLETLRKFS TEHMCKFLGA GVTVILLREA
PNLCTRLWLD MDIVPIVFNI KPFHTDSITR PNVRHRISST TGSYVPSGAE TPTVYYDPAQ
LQDPNKLSAN VQTRLPIPRT VDEQADSAAR KCIMYFGPGN NPRLQIGPRN QVAVDAGGKI
HLIDDIDEYR KTVGKGTWNS VIKLADELRE KKIKIGFFSS TPQGGGVALM RHAIIRFFTA
LDVDAAWYVP NPSPSVFRTT KNNHNILQGV ADPSLRLTKE AADNFDSWIL KNGLRWTAEG
GPLAPGGVDI AFIDDPQMPG LIPLIKRIRP DLPIIYRSHI EIRSDLVHVK GSPQEEVWNY
LWNNIQHSDL FISHPVNKFV PSDVPLEKLA LLGAATDWLD GLSKHLDAWD SQYYMGEFRN
LCVKEKMNEL GWPAREYIVQ IARFDPSKGI PNVIDSYARF RKLCVDKVME DDIPQLLLCG
HGAVDDPDAS IIYDQVLQLI HAKYKEYAPD IVVMRCPPSD QLLNTLMANA KFALQLSTRE
GFEVKVSEAL HAGKPVIACR TGGIPLQIEH GKSGYLCEPG DNAAVAQHML DLYTDEDLYD
TMSEYARTHV SDEVGTVGNA AAWMYLAVMY VSRGVKLRPH GAWINDLMRT EMGEPYRPGE
PRLPRGELHV QG
