OTSB_MYCUA
ID OTSB_MYCUA Reviewed; 390 AA.
AC A0PMI0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=MUL_0921;
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=362242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99;
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(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; CP000325; ABL03549.1; -; Genomic_DNA.
DR RefSeq; WP_011739172.1; NC_008611.1.
DR AlphaFoldDB; A0PMI0; -.
DR SMR; A0PMI0; -.
DR STRING; 362242.MUL_0921; -.
DR EnsemblBacteria; ABL03549; ABL03549; MUL_0921.
DR KEGG; mul:MUL_0921; -.
DR eggNOG; COG0561; Bacteria.
DR eggNOG; COG0637; Bacteria.
DR HOGENOM; CLU_037265_4_1_11; -.
DR OMA; HKLAKHP; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000000765; 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..390
FT /note="Trehalose-phosphate phosphatase"
FT /id="PRO_0000370708"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 150..152
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 390 AA; 41040 MW; 8BA78D5FA884DB12 CRC64;
MSVTIDPRRH DAVLFDTALN STQALVRQLQ QARVGTATFA SGGGGHDAAI QALIESADRV
GARPGRCVVI TADAASVAAA RDSGFALVIG VDQAGHRDAL PDHGADTVLA DLDEVRVRAG
DRHMSELPDA LQALGRPDGL TVPRPAVFFD FDGTLSEIVD DPDAATPTAG AVAALQQLAA
QCPVAILSGR DLADVSQRVG LPGIWYAGSH GFELTAPDGT HHQNEAAAAA IPVLEQAAAQ
LRDRLGSIPG VMVEHKRFGV ATHYRNAARN RVGKIAAVVR AAGQRDGLRV TTGREVIELH
PDIDWDKGKT LRWVIDHLPD QRAAPLVPIY LGDDITDEDA FDAVGPNGVA IMVRHNEDGD
RATAALFALE SPARVAEFTG RLASQLSTLG
