ID   TREH_MYCS2              Reviewed;         668 AA.
AC   A0R0W9; I7GCG8;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Trehalase;
DE            EC=3.2.1.28;
DE   AltName: Full=Alpha,alpha-trehalase;
DE   AltName: Full=Alpha,alpha-trehalose glucohydrolase;
GN   OrderedLocusNames=MSMEG_4535, MSMEI_4422; ORFNames=MSMEG4528;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17319935; DOI=10.1111/j.1742-4658.2007.05715.x;
RA   Carroll J.D., Pastuszak I., Edavana V.K., Pan Y.T., Elbein A.D.;
RT   "A novel trehalase from Mycobacterium smegmatis - purification, properties,
RT   requirements.";
RL   FEBS J. 274:1701-1714(2007).
CC   -!- FUNCTION: Catalyzes the hydrolysis of alpha,alpha-trehalose into two
CC       molecules of D-glucose. Does not hydrolyze maltose, isomaltose,
CC       sucrose, cellobiose, p-nitrophenyl-alpha-D-glucopyranoside, and methyl-
CC       alpha-D-glucopyranoside. Is also inactive on alpha,beta-trehalose,
CC       beta,beta-trehalose, alpha,alpha-trehalose-6,6'-dibehenate,
CC       trehalulose, nigerose, and trehalose dimycolate.
CC       {ECO:0000269|PubMed:17319935}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-
CC         glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28;
CC         Evidence={ECO:0000269|PubMed:17319935};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:17319935};
CC   -!- COFACTOR:
CC       Name=phosphate; Xref=ChEBI:CHEBI:43474;
CC         Evidence={ECO:0000269|PubMed:17319935};
CC   -!- COFACTOR:
CC       Note=Shows an absolute requirement for inorganic phosphate and Mg(2+)
CC       for activity. The function of the phosphate may involve stabilizing the
CC       protein conformation and/or initiating protein aggregation. Mg(2+)
CC       cannot be replaced by Ca(2+), Mn(2+) or Zn(2+).
CC       {ECO:0000269|PubMed:17319935};
CC   -!- ACTIVITY REGULATION: Inhibited by pyrophosphate and polyphosphates.
CC       Also competitively inhibited by validoxylamine and castanospermine, but
CC       not by trehazolin. {ECO:0000269|PubMed:17319935}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=20 mM for alpha,alpha-trehalose {ECO:0000269|PubMed:17319935};
CC       pH dependence:
CC         Optimum pH is 7.1. The trehalase activity drops sharply at pH values
CC         of 6.5 and below, as well as at pH values of 8.0 and above.
CC         {ECO:0000269|PubMed:17319935};
CC   -!- PATHWAY: Glycan degradation; trehalose degradation; D-glucose from
CC       alpha,alpha-trehalose: step 1/1.
CC   -!- SUBUNIT: Homomultimer of 20 or more subunits.
CC       {ECO:0000269|PubMed:17319935}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family. {ECO:0000305}.
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DR   EMBL; CP000480; ABK72415.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP40876.1; -; Genomic_DNA.
DR   RefSeq; WP_011729900.1; NZ_SIJM01000052.1.
DR   RefSeq; YP_888807.1; NC_008596.1.
DR   AlphaFoldDB; A0R0W9; -.
DR   SMR; A0R0W9; -.
DR   STRING; 246196.MSMEI_4422; -.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
DR   PRIDE; A0R0W9; -.
DR   EnsemblBacteria; ABK72415; ABK72415; MSMEG_4535.
DR   EnsemblBacteria; AFP40876; AFP40876; MSMEI_4422.
DR   GeneID; 66735862; -.
DR   KEGG; msg:MSMEI_4422; -.
DR   KEGG; msm:MSMEG_4535; -.
DR   PATRIC; fig|246196.19.peg.4437; -.
DR   eggNOG; COG3387; Bacteria.
DR   OMA; VEWMCVP; -.
DR   OrthoDB; 318658at2; -.
DR   UniPathway; UPA00300; UER00535.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IDA:UniProtKB.
DR   GO; GO:0042301; F:phosphate ion binding; IDA:UniProtKB.
DR   GO; GO:0005993; P:trehalose catabolic process; IDA:UniProtKB.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011613; GH15-like.
DR   InterPro; IPR045582; Trehalase-like_N.
DR   Pfam; PF19291; DUF5911; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Magnesium;
KW   Reference proteome.
FT   CHAIN           1..668
FT                   /note="Trehalase"
FT                   /id="PRO_0000413979"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   668 AA;  74690 MW;  22AE1581E85F503A CRC64;
     MVLQQTEPTD GADRKASDGP LTVTAPVPYA AGPTLRNPFP PIADYGFLSD CETTCLISSA
     GSVEWLCVPR PDSPSVFGAI LDRGAGHFRL GPYGVSVPAA RRYLPGSLIL ETTWQTHTGW
     LIVRDALVMG PWHDIDTRSR THRRTPMDWD AEHILLRTVR CVSGTVELVM SCEPAFDYHR
     VSATWEYSGP AYGEAIARAS RNPDSHPTLR LTTNLRIGIE GREARARTRL TEGDNVFVAL
     SWSKHPAPQT YEEAADKMWK TSEAWRQWIN VGDFPDHPWR AYLQRSALTL KGLTYSPTGA
     LLAAPTTSLP ETPQGERNWD YRYSWIRDST FALWGLYTLG LDREADDFFS FIADVSGANN
     GERHPLQVMY GVGGERSLVE EELHHLSGYD NSRPVRIGNG AYNQRQHDIW GTMLDSVYLH
     AKSREQIPDA LWPVLKNQVE EAIKHWKEPD RGIWEVRGEP QHFTSSKIMC WVALDRGSKL
     AELQGEKSYA QQWRAIAEEI KADVLARGVD KRGVLTQRYG DDALDASLLL AVLTRFLPAD
     DPRIRATVLA IADELTEDGL VLRYRVEETD DGLAGEEGTF TICSFWLVSA LVEIGEISRA
     KHLCERLLSF ASPLHLYAEE IEPRTGRHLG NFPQAFTHLA LINAVVHVIR AEEEADSSGV
     FVPANAPM