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Entry: A0A2C9CL00_KUEST
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ID   A0A2C9CL00_KUEST        Unreviewed;       566 AA.
AC   A0A2C9CL00;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Trehalose 6-phosphate phosphatase {ECO:0000256|RuleBase:RU361117};
DE            EC=3.1.3.12 {ECO:0000256|RuleBase:RU361117};
GN   ORFNames=KSMBR1_3780 {ECO:0000313|EMBL:SOH06253.1};
OS   Kuenenia stuttgartiensis.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Brocadiaceae; Candidatus Kuenenia.
OX   NCBI_TaxID=174633 {ECO:0000313|EMBL:SOH06253.1, ECO:0000313|Proteomes:UP000221734};
RN   [1] {ECO:0000313|Proteomes:UP000221734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Frank J.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Removes the phosphate from trehalose 6-phosphate to produce
CC       free trehalose. {ECO:0000256|RuleBase:RU361117}.
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:0000256|RuleBase:RU361117};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361117};
CC   -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005199, ECO:0000256|RuleBase:RU361117}.
CC   -!- SIMILARITY: Belongs to the trehalose phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00008770, ECO:0000256|RuleBase:RU361117}.
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DR   EMBL; LT934425; SOH06253.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9CL00; -.
DR   KEGG; kst:KSMBR1_3780; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000221734; Chromosome Kuenenia_stuttgartiensis_MBR1.
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; HAD superfamily/HAD-like; 2.
DR   InterPro; IPR010976; B-phosphoglucomutase_hydrolase.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR044651; OTSB-like.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   InterPro; IPR003337; Trehalose_PPase.
DR   NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR   NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR   NCBIfam; TIGR02009; PGMB-YQAB-SF; 1.
DR   NCBIfam; TIGR00685; T6PP; 1.
DR   PANTHER; PTHR43768; TREHALOSE 6-PHOSPHATE PHOSPHATASE; 1.
DR   PANTHER; PTHR43768:SF3; TREHALOSE 6-PHOSPHATE PHOSPHATASE; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   Pfam; PF02358; Trehalose_PPase; 1.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU361117};
KW   Magnesium {ECO:0000256|RuleBase:RU361117};
KW   Metal-binding {ECO:0000256|RuleBase:RU361117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000221734}.
SQ   SEQUENCE   566 AA;  62312 MW;  9B88E4F153C01F33 CRC64;
     MTRSIDILPY EPAIIPAAKY NRNICIRRKV ISPGNLKQTG GASMVHKKSA YTISREDFDA
     VIFDLDGVVT DTASVHADAW KKMFDEFLSQ YAACNNKPFQ PFDIDADYRL YVDGKPRFDG
     VRSFLRSRGV NLPEGQPDDL PGTESIHGLG KLKNEYFLKH IGDHGAEVYD STIDFIHSLK
     KQGCKTAIIS SSRNCAMILD STNLSSLFDV RVDGLDSEVL GIKGKPAPDI FLEAARQLKA
     KPERAVVIED AISGVQAGKA GKFRLVVGVA RTGDKESLLE NGADVVVEDL SEIGVRNDIE
     VIHGLPSALD SIDDIANQAR GKRIAVFLDY DGTLTPIVET PDKAIMAEDM REAVIKLSNN
     CTVGIISGRD LKDVQEKVEI DSFVYAGSHG FDIAGPEGLN IKSQAGAEFL PVLDKAEKEL
     SEKLRSIEGV FVERKKFAIA IHYRLVTPEK AELVDEIVDK VASVYPELRK AYGKKIFELQ
     PDIDWHKGKA LLTLLKALKL DGDDVLPFYI GDDVTDEDAF WTLKGSGIGI VVWDEPYETA
     ASYSLKNPEE VRKFLLKLIP LGGGHE
//
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