ID   TREC_ECOLI              Reviewed;         551 AA.
AC   P28904; Q2M668;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 3.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Trehalose-6-phosphate hydrolase {ECO:0000303|PubMed:8083158};
DE            EC=3.2.1.93 {ECO:0000269|PubMed:8083158};
DE   AltName: Full=Alpha,alpha-phosphotrehalase;
GN   Name=treC; Synonyms=olgH; OrderedLocusNames=b4239, JW4198;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC   STRAIN=K12;
RX   PubMed=8083158; DOI=10.1128/jb.176.18.5654-5664.1994;
RA   Rimmele M., Boos W.;
RT   "Trehalose-6-phosphate hydrolase of Escherichia coli.";
RL   J. Bacteriol. 176:5654-5664(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 160-392.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8421692; DOI=10.1073/pnas.90.2.577;
RA   Sun X., Harder J., Krook M., Joernvall H., Sjoeberg B.-M., Reichard P.;
RT   "A possible glycine radical in anaerobic ribonucleotide reductase from
RT   Escherichia coli: nucleotide sequence of the cloned nrdD gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:577-581(1993).
CC   -!- FUNCTION: Hydrolyzes trehalose-6-phosphate to glucose and glucose 6-
CC       phosphate. Can also very effectively hydrolyze p-nitrophenyl-alpha-D-
CC       glucopyranoside, but it does not recognize trehalose, sucrose, maltose,
CC       isomaltose, or maltodextrins. {ECO:0000269|PubMed:8083158}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha,alpha-trehalose 6-phosphate + H2O = D-glucose + D-
CC         glucose 6-phosphate; Xref=Rhea:RHEA:23008, ChEBI:CHEBI:4167,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:58429, ChEBI:CHEBI:61548; EC=3.2.1.93;
CC         Evidence={ECO:0000269|PubMed:8083158};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6 mM for trehalose-6-phosphate {ECO:0000269|PubMed:8083158};
CC         Vmax=5.5 umol/min/mg enzyme {ECO:0000269|PubMed:8083158};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:8083158}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; U06195; AAC43382.1; -; Genomic_DNA.
DR   EMBL; U14003; AAA97136.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77196.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78238.1; -; Genomic_DNA.
DR   EMBL; L06097; AAA24225.1; -; Genomic_DNA.
DR   PIR; S56465; S56465.
DR   RefSeq; NP_418660.1; NC_000913.3.
DR   RefSeq; WP_001336303.1; NZ_LN832404.1.
DR   AlphaFoldDB; P28904; -.
DR   SMR; P28904; -.
DR   BioGRID; 4259319; 17.
DR   BioGRID; 853051; 1.
DR   DIP; DIP-11024N; -.
DR   IntAct; P28904; 8.
DR   STRING; 511145.b4239; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   jPOST; P28904; -.
DR   PaxDb; P28904; -.
DR   PRIDE; P28904; -.
DR   EnsemblBacteria; AAC77196; AAC77196; b4239.
DR   EnsemblBacteria; BAE78238; BAE78238; BAE78238.
DR   GeneID; 948762; -.
DR   KEGG; ecj:JW4198; -.
DR   KEGG; eco:b4239; -.
DR   PATRIC; fig|1411691.4.peg.2462; -.
DR   EchoBASE; EB1374; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_1_2_6; -.
DR   InParanoid; P28904; -.
DR   OMA; PNGEKWA; -.
DR   PhylomeDB; P28904; -.
DR   BioCyc; EcoCyc:TRE6PHYDRO-MON; -.
DR   BioCyc; MetaCyc:TRE6PHYDRO-MON; -.
DR   SABIO-RK; P28904; -.
DR   PRO; PR:P28904; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0008788; F:alpha,alpha-phosphotrehalase activity; IDA:EcoCyc.
DR   GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR   GO; GO:0005993; P:trehalose catabolic process; IMP:EcoCyc.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.90.400.10; -; 1.
DR   InterPro; IPR022567; DUF3459.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045857; O16G_dom_2.
DR   InterPro; IPR012769; Trehalose_TreC.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF11941; DUF3459; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   TIGRFAMs; TIGR02403; trehalose_treC; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..551
FT                   /note="Trehalose-6-phosphate hydrolase"
FT                   /id="PRO_0000054319"
FT   ACT_SITE        200
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P00691"
FT   ACT_SITE        251
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P00691"
FT   SITE            325
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00691"
FT   CONFLICT        74
FT                   /note="D -> V (in Ref. 1; AAC43382)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   551 AA;  63838 MW;  975F89F8D91621A6 CRC64;
     MTHLPHWWQN GVIYQIYPKS FQDTTGSGTG DLRGVIQHLD YLHKLGVDAI WLTPFYVSPQ
     VDNGYDVANY TAIDPTYGTL DDFDELVTQA KSRGIRIILD MVFNHTSTQH AWFREALNKE
     SPYRQFYIWR DGEPETPPNN WRSKFGGSAW RWHAESEQYY LHLFAPEQAD LNWENPAVRA
     ELKKVCEFWA DRGVDGLRLD VVNLISKDPR FPEDLDGDGR RFYTDGPRAH EFLHEMNRDV
     FTPRGLMTVG EMSSTSLEHC QRYAALTGSE LSMTFNFHHL KVDYPGGEKW TLAKPDFVAL
     KTLFRHWQQG MHNVAWNALF WCNHDQPRIV SRFGDEGEYR VPAAKMLAMV LHGMQGTPYI
     YQGEEIGMTN PHFTRITDYR DVESLNMFAE LRNDGRDADE LLAILASKSR DNSRTPMQWS
     NGDNAGFTAG EPWIGLGDNY QQINVEAALA DDSSVFYTYQ KLIALRKQEA ILTWGNYQDL
     LPNSPVLWCY RREWKGQTLL VIANLSREIQ PWQAGQMRGN WQLVMHNYEE ASPQPCAMNL
     RPFEAVWWLQ K