ID   TREP_GEOSE              Reviewed;         765 AA.
AC   Q8GRC3;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   02-SEP-2026, entry version 61.
DE   RecName: Full=Alpha,alpha-trehalose phosphorylase;
DE            Short=TPase;
DE            EC=2.4.1.64;
GN   Name=treP;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Anoxybacillaceae;
OC   Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=SK-1;
RX   PubMed=12400680; DOI=10.1271/bbb.66.1835;
RA   Inoue Y., Ishii K., Tomita T., Yatake T., Fukui F.;
RT   "Characterization of trehalose phosphorylase from Bacillus
RT   stearothermophilus SK-1 and nucleotide sequence of the corresponding
RT   gene.";
RL   Biosci. Biotechnol. Biochem. 66:1835-1843(2002).
CC   -!- FUNCTION: Catalyzes the reversible phosphorolytic cleavage of
CC       trehalose. Phosphorolysis is specific for trehalose.
CC       {ECO:0000269|PubMed:12400680}.
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|PubMed:12400680};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.1 mM for trehalose {ECO:0000269|PubMed:12400680};
CC         KM=1.1 mM for phosphate {ECO:0000269|PubMed:12400680};
CC       pH dependence:
CC         Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:12400680};
CC       Temperature dependence:
CC         Optimum temperature is 75 degrees Celsius.
CC         {ECO:0000269|PubMed:12400680};
CC   -!- PATHWAY: Glycan degradation; trehalose degradation.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12400680}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR   EMBL; AB079610; BAC20640.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8GRC3; -.
DR   SMR; Q8GRC3; -.
DR   CAZy; GH65; Glycoside Hydrolase Family 65.
DR   KEGG; ag:BAC20640; -.
DR   BioCyc; MetaCyc:MONOMER-5885; -.
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:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:TreeGrafter.
DR   GO; GO:0005993; P:trehalose catabolic process; IDA:UniProtKB.
DR   FunFam; 2.60.420.10:FF:000001; Family 65 glycosyl hydrolase; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 1.
DR   Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR037018; GH65_N.
DR   InterPro; IPR005194; Glyco_hydro_65_C.
DR   InterPro; IPR005195; Glyco_hydro_65_M.
DR   InterPro; IPR005196; Glyco_hydro_65_N.
DR   InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR   PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR   PANTHER; PTHR11051:SF8; PROTEIN-GLUCOSYLGALACTOSYLHYDROXYLYSINE GLUCOSIDASE; 1.
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; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosyltransferase; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12400680"
FT   CHAIN           2..765
FT                   /note="Alpha,alpha-trehalose phosphorylase"
FT                   /id="PRO_0000418977"
FT   ACT_SITE        479
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         352..353
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         591..592
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
SQ   SEQUENCE   765 AA;  87952 MW;  8E7FC4E8CDB1C1CF CRC64;
     MSWSISSNQL NIENLLNEES LFFTGNGYIG VRGNFEEKYY DGASSIRGTY INAFHDITDI
     NYGEKLYAFP ETQQKLVNVI DAQTVQIYFG EEEERFSLFE GEVIQYERHL HMDKGFSERV
     IHWRSPGGKE VKLKFKRLTS FIYKELFIQE ITIEPVNFFG KTKVVSTVNG DVSNFVDPSD
     PRVGSGHAKL LTVSDTVIEG DFVSIETKTK RSNLYAACTS TCRLNIDFQR EYVKNEKSVE
     TVLTFELTEK AIMTKINIYT DTLRHGDRPL RTGLDLCQKL SCLTFNDLKE QQKHYLDKFW
     LYADVEISGD QALQEGIRFN LFHLLQSAGR DRFSNIAAKG LSGEGYEGHY FWDTEIYMVP
     VFLMTNPELA KQLLIYRYSI LDKARERARE MGHRKGALFP WRTISGGECS SYFPAGTAQY
     HISADIAYSY VQYYLVTKDL DFLKSYGAEL LIETARLWMD TGHYHEGKFK IDAVTGPDEY
     TCIVNNNYYT NVMAKHNLRW AAKSVAELEK HAPDTLASLK AKLEITDEEI AEWIKAAEAM
     YLPYDPTLNI NPQDDTFLQK QVWDFDNTPK EHYPLLLHYH PLTLYRYQVC KQADTVLAHF
     LLEDEQDESV IRDSYHYYEK ITTHDSSLSS CVFSIMAAKI GELDKAYEYF IETARLDLDN
     THGNTKDGLH MANMGGTWMA IVYGFAGLRI KESGLSLAPV IPKQWQSYRF SIQYLGRHIS
     VSVDTKGTKV NLLNGEELTI KLYGKKHQLT KDEPLEITFN NGRVD
//