OTSB_MYCBP
ID OTSB_MYCBP Reviewed; 391 AA.
AC A1KP65;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=BCG_3444;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
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; AM408590; CAL73433.1; -; Genomic_DNA.
DR RefSeq; WP_003417892.1; NC_008769.1.
DR AlphaFoldDB; A1KP65; -.
DR SMR; A1KP65; -.
DR KEGG; mbb:BCG_3444; -.
DR HOGENOM; CLU_037265_4_1_11; -.
DR OMA; HKLAKHP; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000001472; 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_0000370702"
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; 41720 MW; 87AAC490926F9187 CRC64;
MRKLGPVTID PRRHDAVLFD TTLDATQELV RQLQEVGVGT GVFGSGLDVP IVAAGRLAVR
PGRCVVVSAH SAGVTAARES GFALIIGVDR TGCRDALRRD GADTVVTDLS EVSVRTGDRR
MSQLPDALQA LGLADGLVAR QPAVFFDFDG TLSDIVEDPD AAWLAPGALE ALQKLAARCP
IAVLSGRDLA DVTQRVGLPG IWYAGSHGFE LTAPDGTHHQ NDAAAAAIPV LKQAAAELRQ
QLGPFPGVVV EHKRFGVAVH YRNAARDRVG EVAAAVRTAE QRHALRVTTG REVIELRPDV
DWDKGKTLLW VLDHLPHSGS APLVPIYLGD DITDEDAFDV VGPHGVPIVV RHTDDGDRAT
AALFALDSPA RVAEFTDRLA RQLREAPLRA T
