OTSB_SINFN
ID OTSB_SINFN Reviewed; 265 AA.
AC P55611;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Probable trehalose-phosphate phosphatase;
DE Short=TPP;
DE EC=3.1.3.12;
DE AltName: Full=Trehalose 6-phosphate phosphatase;
DE AltName: Full=Trehalose-phosphatase;
GN Name=otsB; OrderedLocusNames=NGR_a02100; ORFNames=y4pB;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG Plasmid sym pNGR234a.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=9163424; DOI=10.1038/387394a0;
RA Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA Perret X.;
RT "Molecular basis of symbiosis between Rhizobium and legumes.";
RL Nature 387:394-401(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=19376903; DOI=10.1128/aem.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
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; U00090; AAB91812.1; -; Genomic_DNA.
DR RefSeq; NP_444015.1; NC_000914.2.
DR RefSeq; WP_010875237.1; NC_000914.2.
DR AlphaFoldDB; P55611; -.
DR SMR; P55611; -.
DR STRING; 394.NGR_a02100; -.
DR EnsemblBacteria; AAB91812; AAB91812; NGR_a02100.
DR KEGG; rhi:NGR_a02100; -.
DR PATRIC; fig|394.7.peg.221; -.
DR eggNOG; COG1877; Bacteria.
DR HOGENOM; CLU_037265_2_0_5; -.
DR OMA; YGAERWD; -.
DR OrthoDB; 1374424at2; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234a.
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; -; 1.
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; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR TIGRFAMs; TIGR00685; T6PP; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Plasmid; Reference proteome.
FT CHAIN 1..265
FT /note="Probable trehalose-phosphate phosphatase"
FT /id="PRO_0000058101"
FT ACT_SITE 35
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 35..37
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 265 AA; 27958 MW; AD21CF43EF7D794A CRC64;
MSCQTQLLSA SEAALGEDFL SALSTDLDNW ALFLDIDGTL LDLAETPDAV AVPPSLPASL
DHLSKKLGGA LALVTGRGLD YADQLFSPAN FPIAGLHGAE RRDPDGRVHK AAETADFERL
KAELVAATAS WAGVLIEDKG AAVAAHYRLA PDRQLELEQL MEWALYRAGP DWAIQHGKMV
VEIRPARANK GDAVAAFLGQ PPFAGRRAIA IGDDVTDEAM FRTVNRLGGL SIRIGPPVPA
SEALGSIPSA EALRGIIAAL ALLNI