TREP_THEBR
ID TREP_THEBR Reviewed; 774 AA.
AC Q8L164;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Alpha,alpha-trehalose phosphorylase;
DE Short=TPase;
DE EC=2.4.1.64;
GN Name=treP;
OS Thermoanaerobacter brockii (Thermoanaerobium brockii).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=29323;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GENE NAME.
RC STRAIN=ATCC 35047 / HTRI;
RX PubMed=12400703; DOI=10.1271/bbb.66.1976;
RA Maruta K., Mukai K., Yamashita H., Kubota M., Chaen H., Fukuda S.,
RA Kurimoto M.;
RT "Gene encoding a trehalose phosphorylase from Thermoanaerobacter brockii
RT ATCC 35047.";
RL Biosci. Biotechnol. Biochem. 66:1976-1980(2002).
RN [2]
RP PROTEIN SEQUENCE OF 2-16, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 35047 / HTRI;
RX DOI=10.5458/jag.46.399;
RA Chaen H., Nakada T., Nishimoto T., Kuroda N., Fukuda S., Sugimoto T.,
RA Kurimoto M., Tsujisaka Y.;
RT "Purification and characterization of thermostable trehalose phosphorylase
RT from Thermoanaerobium brockii.";
RL J. Appl. Glycosci. 46:399-405(1999).
CC -!- FUNCTION: Catalyzes the reversible phosphorolytic cleavage of
CC trehalose. Phosphorolysis is specific for trehalose, but D-xylose, D-
CC galactose, L-arabinose, D-fucose, L-fucose, D-glucosamine and 2-deoxy
CC D-glucose can act as substitutes for D-glucose in the synthetic
CC reaction. {ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha,alpha-trehalose + phosphate = beta-D-glucose 1-phosphate
CC + D-glucose; Xref=Rhea:RHEA:23512, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:43474, ChEBI:CHEBI:57684; EC=2.4.1.64;
CC Evidence={ECO:0000269|Ref.2};
CC -!- ACTIVITY REGULATION: Inhibited by Cu(2+), Hg(2+), Mg(2+), Mn(2+),
CC Pb(2+) and Zn(2+). {ECO:0000269|Ref.2}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.94 mM for trehalose {ECO:0000269|Ref.2};
CC KM=0.57 mM for phosphate {ECO:0000269|Ref.2};
CC KM=2.4 mM for D-glucose {ECO:0000269|Ref.2};
CC KM=0.75 mM for beta-D-glucose 1-phosphate {ECO:0000269|Ref.2};
CC Note=kcat is 110 sec(-1) for trehalose. kcat is 110 sec(-1) for
CC phosphate. kcat is 140 sec(-1) for D-glucose. kcat is 140 sec(-1) for
CC beta-D-glucose 1-phosphate.;
CC pH dependence:
CC Optimum pH is 7.0-7.5 for phosphorolysis, and 6.0-7.0 for synthetic
CC reaction. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. {ECO:0000269|Ref.2};
CC -!- PATHWAY: Glycan degradation; trehalose degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR EMBL; AB073930; BAB97299.1; -; Genomic_DNA.
DR PIR; JC7887; JC7887.
DR AlphaFoldDB; Q8L164; -.
DR SMR; Q8L164; -.
DR CAZy; GH65; Glycoside Hydrolase Family 65.
DR PRIDE; Q8L164; -.
DR BRENDA; 2.4.1.64; 1463.
DR UniPathway; UPA00300; -.
DR GO; GO:0047656; F:alpha,alpha-trehalose phosphorylase activity; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005993; P:trehalose catabolic process; IDA:UniProtKB.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR005194; Glyco_hydro_65_C.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR Pfam; PF03633; Glyco_hydro_65C; 1.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycosyltransferase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..774
FT /note="Alpha,alpha-trehalose phosphorylase"
FT /id="PRO_0000418978"
FT ACT_SITE 498
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 369..370
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 610..611
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
SQ SEQUENCE 774 AA; 89252 MW; C136E8FEABE20E47 CRC64;
MANKTKKPIY PFEDWVIRET QFSIDTNYRN ETIFTLANGY IGMRGTFEER YSGPKNTSFN
GTYINGFYEI HDIVYPEGGY GFAKIGQTML NVADSKIIKL YVDGEEFDLL QGKILFYERV
LDMKKGFVER KVKWESPTGK ILEVKIKRIV SLNRQHLAAI SFTMQPVNFT GKIRFVSAID
GNVSNINDSE DVRVGSNLKG KVLKTIDKSV EGLKGWIVQK TQKSNFSYAC AIDNVLVADS
KYEVSNSLEE DGVKVIVDLE AEKGTSYTLN KFISYYTSKD FDENKLVALA LEEIEKAKND
GFETIEKEQE EFLNSFWKDA DVIIEGDKAL QQGIRFNEFH LLQSVGRDGK TNIAAKGLTG
GGYEGHYFWD SDIYIMPFFL YTKPEIAKAL VMYRYNLLDA ARSRAKELGH KGALYPWRTI
DGPECSAYFP AGTAQYHINA DIVYALKRYV EATNDVDFLY DYGCEILFET ARFWEDLGAY
IPLKGNKFCI NCVTGPDEYT ALVDNNAYTN YMAKMNLEYA YDIANKMKKE VPQKYQKVAS
KLNLKDEEIV AWKKAADNMY LPYSKELDII PQDDSFLYKE RITVDEIPED QFPLLLHWHY
LNIYRYQICK QPDVLLLMFL QREKFTKDEL KKNYDYYEPI TTHDSSLSPA IFSILANEIG
YTDKAYKYFM MTARMDLDDY NDNVKDGIHA ASMAGTWSAV VNGFGGMRVY TNELHFEPRL
PKEWNLLSFN VRYKGRKINV KLTKENVVFA LLEGEPIEIY YFDKKILLEK GEIK
