ID   GOB1_CAEBR              Reviewed;         434 AA.
AC   A8X485;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Trehalose-phosphatase;
DE            EC=3.1.3.12 {ECO:0000250|UniProtKB:Q9XTQ5};
DE   AltName: Full=Trehalose-6-phosphate phosphatase;
DE            Short=TPP;
GN   Name=gob-1; ORFNames=CBG07712;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Catalyzes the hydrolysis of trehalose 6-phosphate to
CC       trehalose and phosphate; prevents the accumulation of toxic levels of
CC       trehalose 6-phosphate. {ECO:0000250|UniProtKB:Q9XTQ5}.
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:0000250|UniProtKB:Q9XTQ5};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:A8NS89};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:A8NS89};
CC   -!- SIMILARITY: Belongs to the gob-1 trehalose phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; HE601041; CAP27445.1; -; Genomic_DNA.
DR   RefSeq; XP_002645945.1; XM_002645899.1.
DR   AlphaFoldDB; A8X485; -.
DR   SMR; A8X485; -.
DR   STRING; 6238.CBG07712; -.
DR   GeneID; 8587944; -.
DR   KEGG; cbr:CBG_07712; -.
DR   CTD; 8587944; -.
DR   WormBase; CBG07712; CBP39651; WBGene00029675; Cbr-gob-1.
DR   eggNOG; ENOG502RY87; Eukaryota.
DR   HOGENOM; CLU_033472_0_0_1; -.
DR   InParanoid; A8X485; -.
DR   OMA; CGRYRSS; -.
DR   OrthoDB; 766517at2759; -.
DR   Proteomes; UP000008549; Chromosome X.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004805; F:trehalose-phosphatase activity; ISS:UniProtKB.
DR   GO; GO:1901136; P:carbohydrate derivative catabolic process; ISS:UniProtKB.
DR   GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR001830; Glyco_trans_20.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR041064; T6PP_helical.
DR   PANTHER; PTHR10788; PTHR10788; 1.
DR   Pfam; PF18572; T6PP_N; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..434
FT                   /note="Trehalose-phosphatase"
FT                   /id="PRO_0000385171"
FT   ACT_SITE        158
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:A8NS89"
FT   BINDING         156
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:A8NS89"
FT   BINDING         158
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:A8NS89"
FT   BINDING         275..277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A8NS89"
FT   BINDING         366
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:A8NS89"
SQ   SEQUENCE   434 AA;  48434 MW;  00C5EA27596544F5 CRC64;
     MTVASQSIEE FKECLYHMQE TRKLLTMQLL ATGKITSAEI QILKRTLEEM QDERTTDFYI
     RHIHSRGATF AINIRDEILG LKKDFLFLEN FASECESEES FTNRLKLCDL PGLLSNNQID
     IRLMNGFAEE VAKCKEFLMD LITIESDGIK PLFITDWDGT MKDYCSQYAT NLQPAYSAIV
     MGVFARNFTR AFAVLTAGPL RHPGILDLTS LPIDGPVMFS GSWGREWWLG GRRVVHDDGI
     PEEGSVAIGQ LYEQLEEILH EGEFVQFALV GSGVQKKVDR LTLGVQTVFG QVPKELSAKY
     IDAVKERIHR VDPNSQYLIL ENCSPLEIEV CVHSSGAIWN KGDGVAALVE FNKDSLKLGK
     VCVAGDTTSD LPMLQKAAQE NPTQVRALFV NVNKEIQSTI NKIVGDSSRT CFISCPDVAH
     AAFAQIIIEL TQNA