OTSBH_THEAC
ID OTSBH_THEAC Reviewed; 229 AA.
AC Q9HIW7;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Trehalose-6-phosphate phosphatase-related protein;
DE Short=T6PP;
DE EC=3.1.3.12;
DE AltName: Full=Trehalose 6-phosphate phosphatase;
DE AltName: Full=Trehalose-phosphatase;
GN OrderedLocusNames=Ta1209;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP COFACTOR, AND INDUCTION.
RX PubMed=16815921; DOI=10.1110/ps.062096606;
RA Rao K.N., Kumaran D., Seetharaman J., Bonanno J.B., Burley S.K.,
RA Swaminathan S.;
RT "Crystal structure of trehalose-6-phosphate phosphatase-related protein:
RT biochemical and biological implications.";
RL Protein Sci. 15:1735-1744(2006).
CC -!- FUNCTION: Removes the phosphate from trehalose 6-phosphate (Tre6P) to
CC produce free trehalose. Also catalyzes the dephosphorylation of para-
CC nitrophenyl phosphate (pNPP), but with lesser efficiency (in vitro).
CC {ECO:0000269|PubMed:16815921}.
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 Evidence={ECO:0000269|PubMed:16815921};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16815921};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.7 mM for Tre6P (at pH 8 and 50 degrees Celsius)
CC {ECO:0000269|PubMed:16815921};
CC KM=18 mM for pNPP (at pH 8 and 50 degrees Celsius)
CC {ECO:0000269|PubMed:16815921};
CC Note=kcat is 10 sec(-1) and 0.8 sec(-1) for Tre6P and pNPP,
CC respectively (at pH 8 and 50 degrees Celsius).;
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC -!- INDUCTION: By Tre6P. {ECO:0000305|PubMed:16815921}.
CC -!- SIMILARITY: Belongs to the trehalose phosphatase family. {ECO:0000305}.
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DR EMBL; AL445066; CAC12334.1; -; Genomic_DNA.
DR PDB; 1U02; X-ray; 1.92 A; A=2-229.
DR PDBsum; 1U02; -.
DR AlphaFoldDB; Q9HIW7; -.
DR SMR; Q9HIW7; -.
DR STRING; 273075.Ta1209m; -.
DR EnsemblBacteria; CAC12334; CAC12334; CAC12334.
DR KEGG; tac:Ta1209; -.
DR eggNOG; arCOG01216; Archaea.
DR HOGENOM; CLU_037265_2_1_2; -.
DR OMA; ICYHGAC; -.
DR BRENDA; 3.1.3.12; 6324.
DR UniPathway; UPA00299; -.
DR EvolutionaryTrace; Q9HIW7; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..229
FT /note="Trehalose-6-phosphate phosphatase-related protein"
FT /id="PRO_0000424546"
FT ACT_SITE 5
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 5..7
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 5
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16815921"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16815921"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16815921"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1U02"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:1U02"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:1U02"
FT HELIX 24..36
FT /evidence="ECO:0007829|PDB:1U02"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1U02"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:1U02"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1U02"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1U02"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1U02"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1U02"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:1U02"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:1U02"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:1U02"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:1U02"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:1U02"
FT HELIX 125..139
FT /evidence="ECO:0007829|PDB:1U02"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1U02"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:1U02"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:1U02"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:1U02"
FT HELIX 179..186
FT /evidence="ECO:0007829|PDB:1U02"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:1U02"
FT STRAND 191..199
FT /evidence="ECO:0007829|PDB:1U02"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:1U02"
FT HELIX 210..227
FT /evidence="ECO:0007829|PDB:1U02"
SQ SEQUENCE 229 AA; 25896 MW; DF13250C8F401B8C CRC64;
MIFLDYDGTL VPIIMNPEES YADAGLLSLI SDLKERFDTY IVTGRSPEEI SRFLPLDINM
ICYHGACSKI NGQIVYNNGS DRFLGVFDRI YEDTRSWVSD FPGLRIYRKN LAVLYHLGLM
GADMKPKLRS RIEEIARIFG VETYYGKMII ELRVPGVNKG SAIRSVRGER PAIIAGDDAT
DEAAFEANDD ALTIKVGEGE THAKFHVADY IEMRKILKFI EMLGVQKKQ
