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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//