ID A0A1R1CJM2_9BACL Unreviewed; 267 AA.
AC A0A1R1CJM2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Acid sugar phosphatase {ECO:0000256|PIRNR:PIRNR000915};
DE EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR000915};
GN ORFNames=BK133_26820 {ECO:0000313|EMBL:OMF22253.1};
OS Paenibacillus sp. FSL H8-0548.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1920422 {ECO:0000313|EMBL:OMF22253.1, ECO:0000313|Proteomes:UP000187405};
RN [1] {ECO:0000313|EMBL:OMF22253.1, ECO:0000313|Proteomes:UP000187405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H8-0548 {ECO:0000313|EMBL:OMF22253.1,
RC ECO:0000313|Proteomes:UP000187405};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the dephosphorylation of 2-6 carbon acid sugars in
CC vitro. {ECO:0000256|PIRNR:PIRNR000915}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000915-3};
CC Note=Divalent metal ions. Mg(2+) is the most effective.
CC {ECO:0000256|PIRSR:PIRSR000915-3};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. NagD family.
CC {ECO:0000256|PIRNR:PIRNR000915}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMF22253.1}.
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DR EMBL; MRTK01000057; OMF22253.1; -; Genomic_DNA.
DR RefSeq; WP_076339467.1; NZ_MRTK01000057.1.
DR AlphaFoldDB; A0A1R1CJM2; -.
DR STRING; 1920422.BK133_26820; -.
DR OrthoDB; 9810449at2; -.
DR Proteomes; UP000187405; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR01460; HAD-SF-IIA; 1.
DR PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR19288:SF98; SUGAR-PHOSPHATASE ARAL; 1.
DR Pfam; PF13344; Hydrolase_6; 1.
DR Pfam; PF13242; Hydrolase_like; 1.
DR PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|PIRNR:PIRNR000915, ECO:0000256|PIRSR:PIRSR000915-3};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR000915,
KW ECO:0000256|PIRSR:PIRSR000915-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000187405}.
FT ACT_SITE 11
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT ACT_SITE 13
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ SEQUENCE 267 AA; 28956 MW; CE240724403DD844 CRC64;
MLNEIEGYII DLDGTIYRGN QAIDGAMEAI DHLKKHGKKI VYLSNRGNIS RVMCQEKLQR
MGISAAIDEI LLTSTVTAQY LRMHEPLAKV WTLGDYGLRE ELQSWDIDMA KHPEEANHLV
ITLHESLTYK ELNQAFRAVS SGAEIIATNA DKSFPGEDGE SIDVAGMVAA IVATTGKDVK
LVVGKPSAMM AEAALRTLGV TPERCLVIGD SLASDIALGK RAGIKTALVL SGSSSSQDAL
LANEQPDWVW NSISDLIPLL ALKEELI
//