ID   OTSB_MYCA1              Reviewed;         391 AA.
AC   A0QKN5;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Trehalose-phosphate phosphatase;
DE            Short=TPP;
DE            EC=3.1.3.12;
DE   AltName: Full=Trehalose-6-phosphate phosphatase;
GN   Name=otsB; OrderedLocusNames=MAV_4338;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
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.
CC   -!- FUNCTION: Removes the phosphate from trehalose 6-phosphate to produce
CC       free trehalose. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-
CC         trehalose + phosphate; Xref=Rhea:RHEA:23420, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:43474, ChEBI:CHEBI:58429; EC=3.1.3.12;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC   -!- SIMILARITY: Belongs to the trehalose phosphatase family. {ECO:0000305}.
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DR   EMBL; CP000479; ABK67241.1; -; Genomic_DNA.
DR   RefSeq; WP_011726010.1; NC_008595.1.
DR   AlphaFoldDB; A0QKN5; -.
DR   SMR; A0QKN5; -.
DR   EnsemblBacteria; ABK67241; ABK67241; MAV_4338.
DR   KEGG; mav:MAV_4338; -.
DR   HOGENOM; CLU_037265_4_1_11; -.
DR   OMA; HKLAKHP; -.
DR   OrthoDB; 1374424at2; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000001574; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004805; F:trehalose-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1000; -; 2.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR044651; OTSB-like.
DR   InterPro; IPR003337; Trehalose_PPase.
DR   PANTHER; PTHR43768; PTHR43768; 1.
DR   Pfam; PF02358; Trehalose_PPase; 1.
DR   SUPFAM; SSF56784; SSF56784; 2.
DR   TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR   TIGRFAMs; TIGR00685; T6PP; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..391
FT                   /note="Trehalose-phosphate phosphatase"
FT                   /id="PRO_0000370700"
FT   ACT_SITE        147
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         147..149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         330
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   391 AA;  40409 MW;  991DF0C4BD0EF374 CRC64;
     MGESGPVVID PRRHDAVLFG VGDALGSALA SQLGQIGVGT AAIAADDPAA AADRLRVRPG
     RCVVVAGDPA AVEAARAAGF ALVIGLAPDG RDGDGLRAAG ADAVIAELEQ ITVRTGDRRM
     SQLPDASQAL TGGADGLAGR HPAVFFDFDG TLSDIVDDPD AARPVAGATA ALTRLAARCP
     VAVLSGRDLA DVTKRVGVPG IWYAGSHGFE LTAPDGSHHQ NDDAAAAIPV LAQAAGRLSD
     ELGTIPGVVV EHKRFGVAVH YRNAARDRVG EVAAAVRAAG RHDALRVTTG REVIELRPDL
     DWDKGKTLHW VIEHLRRSGS GALTPVYLGD DITDEDAFDA VRGGPVQGVP ILVRHNDDGD
     RATAALFALD SPARAAEFTE RLADQLERGE G